ID NCAP_SARS2 Reviewed; 419 AA.
AC P0DTC9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=N;
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04096};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04096};
OS Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus;
OC Severe acute respiratory syndrome coronavirus.
OX NCBI_TaxID=2697049;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT "A new coronavirus associated with human respiratory disease in China.";
RL Nature 579:265-269(2020).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=33060197; DOI=10.1126/science.abe9403;
RG QCRG Structural Biology Consortium;
RG Zoonomia Consortium;
RA Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H.,
RA Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R.,
RA Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M.,
RA McGregor M., Cakir Z., Jang G., O'Meara M.J., Tummino T.A., Zhang Z.,
RA Foussard H., Rojc A., Zhou Y., Kuchenov D., Huettenhain R., Xu J.,
RA Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B.,
RA Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z.C., Pulido E.H.,
RA Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A.,
RA Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M.,
RA Billesboelle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S.,
RA Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E.,
RA Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N.,
RA Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D.,
RA Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S.,
RA Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L.,
RA Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A.,
RA Moss F.R. III, Nguyen P., Paulino J., Pawar K.I., Peters J.K.,
RA Pospiech T.H. Jr., Safari M., Sangwan S., Schaefer K., Thomas P.V.,
RA Thwin A.C., Trenker R., Tse E., Tsui T.K.M., Wang F., Whitis N., Yu Z.,
RA Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S.,
RA Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E.,
RA Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P.,
RA Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I.,
RA Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M.,
RA Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A.,
RA Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M.,
RA Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C.,
RA Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J.,
RA Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y.,
RA Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R.,
RA Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C.,
RA Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M.,
RA Garcia-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A.,
RA Basler C.F., Vignuzzi M., Peden A.A., Beltrao P., Krogan N.J.;
RT "Comparative host-coronavirus protein interaction networks reveal pan-viral
RT disease mechanisms.";
RL Science 0:0-0(2020).
RN [3] {ECO:0007744|PDB:6WZO, ECO:0007744|PDB:6WZQ}
RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 247-364, AND SUBUNIT.
RX PubMed=32654247; DOI=10.1002/pro.3909;
RA Ye Q., West A.M.V., Silletti S., Corbett K.D.;
RT "Architecture and self-assembly of the SARS-CoV-2 nucleocapsid protein.";
RL Protein Sci. 29:1890-1901(2020).
RN [4]
RP REVIEW.
RX PubMed=32974389; DOI=10.3389/fmolb.2020.00219;
RA Nikolakaki E., Giannakouros T.;
RT "SR/RS Motifs as Critical Determinants of Coronavirus Life Cycle.";
RL Front. Mol. Biosci. 7:219-219(2020).
RN [5]
RP VARIANTS LEU-3 AND PHE-235.
RC STRAIN=20B/501Y.V1, B.1.1.7, VOC-202012/01, and VUI-202012/01;
RX PubMed=33413740; DOI=10.2807/1560-7917.es.2020.26.1.2002106;
RA Leung K., Shum M.H., Leung G.M., Lam T.T., Wu J.T.;
RT "Early transmissibility assessment of the N501Y mutant strains of SARS-CoV-
RT 2 in the United Kingdom, October to November 2020.";
RL Eurosurveillance 26:0-0(2021).
RN [6]
RP FUNCTION, INTERACTION WITH HOST NLRP3, AND SUBCELLULAR LOCATION.
RX PubMed=34341353; DOI=10.1038/s41467-021-25015-6;
RA Pan P., Shen M., Yu Z., Ge W., Chen K., Tian M., Xiao F., Wang Z., Wang J.,
RA Jia Y., Wang W., Wan P., Zhang J., Chen W., Lei Z., Chen X., Luo Z.,
RA Zhang Q., Xu M., Li G., Li Y., Wu J.;
RT "SARS-CoV-2 N protein promotes NLRP3 inflammasome activation to induce
RT hyperinflammation.";
RL Nat. Commun. 12:4664-4664(2021).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 41-174, AND MUTAGENESIS OF
RP TYR-109.
RX PubMed=32363136; DOI=10.1016/j.apsb.2020.04.009;
RA Kang S., Yang M., Hong Z., Zhang L., Huang Z., Chen X., He S., Zhou Z.,
RA Zhou Z., Chen Q., Yan Y., Zhang C., Shan H., Chen S.;
RT "Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain
RT reveals potential unique drug targeting sites.";
RL Acta Pharmacol. Sin. 10:1228-1238(2020).
RN [8] {ECO:0007744|PDB:6YI3, ECO:0007744|PDB:7ACS, ECO:0007744|PDB:7ACT}
RP STRUCTURE BY NMR OF 44-180, FUNCTION, AND MUTAGENESIS OF ARG-68; ARG-92;
RP ILE-94; ARG-107; GLN-163; TYR-172 AND GLU-174.
RX PubMed=33264373; DOI=10.1371/journal.ppat.1009100;
RA Dinesh D.C., Chalupska D., Silhan J., Koutna E., Nencka R., Veverka V.,
RA Boura E.;
RT "Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid
RT phosphoprotein.";
RL PLoS Pathog. 16:1-16(2020).
RN [9]
RP MUTAGENESIS OF SER-188 AND SER-206, AND PHOSPHORYLATION AT SER-206.
RX PubMed=34593624; DOI=10.1073/pnas.2113401118;
RA Liu X., Verma A., Garcia G. Jr., Ramage H., Lucas A., Myers R.L.,
RA Michaelson J.J., Coryell W., Kumar A., Charney A.W., Kazanietz M.G.,
RA Rader D.J., Ritchie M.D., Berrettini W.H., Schultz D.C., Cherry S.,
RA Damoiseaux R., Arumugaswami V., Klein P.S.;
RT "Targeting the coronavirus nucleocapsid protein through GSK-3 inhibition.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:1-9(2021).
RN [10]
RP CLEAVAGE.
RX PubMed=35922005; DOI=10.1038/s41586-022-05148-4;
RA Chu H., Hou Y., Yang D., Wen L., Shuai H., Yoon C., Shi J., Chai Y.,
RA Yuen T.T., Hu B., Li C., Zhao X., Wang Y., Huang X., Lee K.S., Luo C.,
RA Cai J.P., Poon V.K., Chan C.C., Zhang A.J., Yuan S., Sit K.Y., Foo D.C.,
RA Au W.K., Wong K.K., Zhou J., Kok K.H., Jin D.Y., Chan J.F., Yuen K.Y.;
RT "Coronaviruses exploit a host cysteine-aspartic protease for replication.";
RL Nature 0:0-0(2022).
RN [11]
RP MUTAGENESIS OF 203-ARG-GLY-204 AND ARG-203, AND PHOSPHORYLATION.
RX PubMed=35728038; DOI=10.1371/journal.ppat.1010627;
RA Johnson B.A., Zhou Y., Lokugamage K.G., Vu M.N., Bopp N.,
RA Crocquet-Valdes P.A., Kalveram B., Schindewolf C., Liu Y., Scharton D.,
RA Plante J.A., Xie X., Aguilar P., Weaver S.C., Shi P.Y., Walker D.H.,
RA Routh A.L., Plante K.S., Menachery V.D.;
RT "Nucleocapsid mutations in SARS-CoV-2 augment replication and
RT pathogenesis.";
RL PLoS Pathog. 18:e1010627-e1010627(2022).
RN [12]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=35921414; DOI=10.1126/sciadv.abp9770;
RA Lopez-Munoz A.D., Kosik I., Holly J., Yewdell J.W.;
RT "Cell surface SARS-CoV-2 nucleocapsid protein modulates innate and adaptive
RT immunity.";
RL Sci. Adv. 8:eabp9770-eabp9770(2022).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=34901782; DOI=10.1016/j.isci.2021.103562;
RA Nabeel-Shah S., Lee H., Ahmed N., Burke G.L., Farhangmehr S., Ashraf K.,
RA Pu S., Braunschweig U., Zhong G., Wei H., Tang H., Yang J., Marcon E.,
RA Blencowe B.J., Zhang Z., Greenblatt J.F.;
RT "SARS-CoV-2 nucleocapsid protein binds host mRNAs and attenuates stress
RT granules to impair host stress response.";
RL IScience 25:103562-103562(2022).
RN [14]
RP FUNCTION.
RX PubMed=36534661; DOI=10.1371/journal.ppat.1011041;
RA Dolliver S.M., Kleer M., Bui-Marinos M.P., Ying S., Corcoran J.A.,
RA Khaperskyy D.A.;
RT "Nsp1 proteins of human coronaviruses HCoV-OC43 and SARS-CoV2 inhibit
RT stress granule formation.";
RL PLoS Pathog. 18:e1011041-e1011041(2022).
RN [15] {ECO:0007744|PDB:7PKU}
RP STRUCTURE BY NMR OF 191-263, AND INTERACTION WITH NSP3.
RX PubMed=35044811; DOI=10.1126/sciadv.abm4034;
RA Bessa L.M., Guseva S., Camacho-Zarco A.R., Salvi N., Maurin D., Perez L.M.,
RA Botova M., Malki A., Nanao M., Jensen M.R., Ruigrok R.W.H., Blackledge M.;
RT "The intrinsically disordered SARS-CoV-2 nucleoprotein in dynamic complex
RT with its viral partner nsp3a.";
RL Sci. Adv. 8:4034-4034(2022).
CC -!- FUNCTION: Packages the positive strand viral genome RNA into a helical
CC ribonucleocapsid (RNP) and plays a fundamental role during virion
CC assembly through its interactions with the viral genome and membrane
CC protein M (PubMed:33264373). Plays an important role in enhancing the
CC efficiency of subgenomic viral RNA transcription as well as viral
CC replication. Attenuates the stress granules formation by reducing host
CC G3BP1 access to host mRNAs under stress conditions (PubMed:34901782,
CC PubMed:36534661). {ECO:0000269|PubMed:32974389,
CC ECO:0000269|PubMed:33264373, ECO:0000269|PubMed:34901782,
CC ECO:0000269|PubMed:36534661}.
CC -!- FUNCTION: May block host chemokine function in vivo, facilitating viral
CC replication and transmission (PubMed:35921414). Acts by being secreted
CC into the extracellular space where it competes to host chemokines for
CC binding to host glycosaminoglycans (GAG) (PubMed:35921414).
CC {ECO:0000269|PubMed:35921414}.
CC -!- FUNCTION: May induce inflammasome responses in cultured cells and mice.
CC Acts by interacting with host NLRP3 to facilitate inflammasome
CC assembly, which induces cytokine release that may play a role in COVID
CC lung injury. {ECO:0000269|PubMed:34341353}.
CC -!- SUBUNIT: Homodimer, homotetramer, homooligomer with RNA
CC (PubMed:32654247). Both monomeric and oligomeric forms interact with
CC RNA. Interacts with protein M (By similarity). Interacts with protein E
CC (By similarity). Interacts with NSP3; this interaction serves to tether
CC the genome to the newly translated replicase-transcriptase complex at a
CC very early stage of infection (PubMed:35044811). May interact with host
CC NLRP3 (PubMed:34341353). {ECO:0000250|UniProtKB:P59595,
CC ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:32654247,
CC ECO:0000269|PubMed:34341353, ECO:0000269|PubMed:35044811}.
CC -!- INTERACTION:
CC P0DTC9; P0DTC4: E; NbExp=3; IntAct=EBI-25475856, EBI-25475850;
CC P0DTC9; P0DTC5: M; NbExp=6; IntAct=EBI-25475856, EBI-25475853;
CC P0DTC9; P0DTC9: N; NbExp=101; IntAct=EBI-25475856, EBI-25475856;
CC P0DTC9; PRO_0000449621 [P0DTD1]: rep; NbExp=13; IntAct=EBI-25475856, EBI-25492388;
CC P0DTC9; P78563: ADARB1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-2967304;
CC P0DTC9; O15145: ARPC3; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-351829;
CC P0DTC9; Q13895: BYSL; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-358049;
CC P0DTC9; Q16543: CDC37; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-295634;
CC P0DTC9; Q92793: CREBBP; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-81215;
CC P0DTC9; Q92499: DDX1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-358474;
CC P0DTC9; Q9NR30: DDX21; Xeno; NbExp=12; IntAct=EBI-25475856, EBI-357942;
CC P0DTC9; P26196: DDX6; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-351257;
CC P0DTC9; Q08426: EHHADH; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-2339219;
CC P0DTC9; P19525: EIF2AK2; Xeno; NbExp=8; IntAct=EBI-25475856, EBI-640775;
CC P0DTC9; Q14241: ELOA; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-742350;
CC P0DTC9; Q13283: G3BP1; Xeno; NbExp=71; IntAct=EBI-25475856, EBI-1047359;
CC P0DTC9; Q9UN86: G3BP2; Xeno; NbExp=37; IntAct=EBI-25475856, EBI-1044298;
CC P0DTC9; P57764: GSDMD; Xeno; NbExp=13; IntAct=EBI-25475856, EBI-2798865;
CC P0DTC9; P49841: GSK3B; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-373586;
CC P0DTC9; P10412: H1-4; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-358163;
CC P0DTC9; O14920: IKBKB; Xeno; NbExp=7; IntAct=EBI-25475856, EBI-81266;
CC P0DTC9; Q92830: KAT2A; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-477622;
CC P0DTC9; Q92831: KAT2B; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-477430;
CC P0DTC9; Q07866: KLC1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-721019;
CC P0DTC9; Q9H0B6: KLC2; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-726994;
CC P0DTC9; Q9NSK0: KLC4; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-949319;
CC P0DTC9; Q9NX58: LYAR; Xeno; NbExp=6; IntAct=EBI-25475856, EBI-713507;
CC P0DTC9; O43318: MAP3K7; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-358684;
CC P0DTC9; Q9UBU8: MORF4L1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-399246;
CC P0DTC9; Q15014: MORF4L2; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-399257;
CC P0DTC9; Q9HCE1: MOV10; Xeno; NbExp=11; IntAct=EBI-25475856, EBI-1055820;
CC P0DTC9; Q9HC36: MRM3; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-1045440;
CC P0DTC9; O15226: NKRF; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-766011;
CC P0DTC9; Q96P20: NLRP3; Xeno; NbExp=18; IntAct=EBI-25475856, EBI-6253230;
CC P0DTC9; O15118: NPC1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-2368710;
CC P0DTC9; Q96HA8: NTAQ1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-741158;
CC P0DTC9; P11940: PABPC1; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-81531;
CC P0DTC9; P62937: PPIA; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-437708;
CC P0DTC9; O75569: PRKRA; Xeno; NbExp=8; IntAct=EBI-25475856, EBI-713955;
CC P0DTC9; Q99873: PRMT1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-78738;
CC P0DTC9; P61289: PSME3; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-355546;
CC P0DTC9; P26022: PTX3; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-11574553;
CC P0DTC9; P54727: RAD23B; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-954531;
CC P0DTC9; O95786: RIGI; Xeno; NbExp=15; IntAct=EBI-25475856, EBI-995350;
CC P0DTC9; P62899: RPL31; Xeno; NbExp=6; IntAct=EBI-25475856, EBI-1053664;
CC P0DTC9; P62753: RPS6; Xeno; NbExp=6; IntAct=EBI-25475856, EBI-356625;
CC P0DTC9; P37840: SNCA; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-985879;
CC P0DTC9; Q96SB4: SRPK1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-539478;
CC P0DTC9; P78362: SRPK2; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-593303;
CC P0DTC9; P42224: STAT1; Xeno; NbExp=6; IntAct=EBI-25475856, EBI-1057697;
CC P0DTC9; P52630: STAT2; Xeno; NbExp=7; IntAct=EBI-25475856, EBI-1546963;
CC P0DTC9; Q15633: TARBP2; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-978581;
CC P0DTC9; Q14258: TRIM25; Xeno; NbExp=13; IntAct=EBI-25475856, EBI-2341129;
CC P0DTC9; O60763: USO1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-356164;
CC P0DTC9; Q93008: USP9X; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-302524;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34341353}.
CC Secreted {ECO:0000269|PubMed:35921414}. Host extracellular space
CC {ECO:0000269|PubMed:35921414}. Note=Probably associates with ER-derived
CC membranes where it participates in viral RNA synthesis and virus
CC budding. When located inside the virion, complexed with the viral RNA.
CC Can be secreted by unconventional protein secretion (UPS)
CC (PubMed:35921414). When secreted, can bind to host glycosaminoglycans
CC on infected and non infected cells (PubMed:35921414). Found in host
CC cytoplasmic stress granules (PubMed:34901782). {ECO:0000255|HAMAP-
CC Rule:MF_04096, ECO:0000269|PubMed:34901782,
CC ECO:0000269|PubMed:35921414}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- PTM: Phosphorylated on serine residues by host GSK3A and GSK3B
CC (PubMed:34593624, PubMed:35728038). This promotes the solubility of
CC homodimers that would otherwise aggregate (PubMed:32974389). Host
CC phosphatase would dephosphorylate the protein during assembly at M
CC bound membranes (PubMed:32974389). {ECO:0000269|PubMed:34593624,
CC ECO:0000269|PubMed:35728038, ECO:0000305|PubMed:32974389}.
CC -!- PTM: Proteolytically cleaved by host CASP6. The cleavage leads to two
CC fragments and facilitates viral replication by inhibiting host IFN
CC signaling. The two fragments may interact with IRF3 inhibiting its
CC nuclear translocation after activation and reduce the expression of
CC IFNB and IFN-stimulated genes. {ECO:0000269|PubMed:35922005}.
CC -!- POLYMORPHISM: Variant Alpha/B.1.1.7 belongs to a lineage isolated first
CC in United Kingdom (December 2020). It is also called Variant of Concern
CC (VOC) 202012/01, Variant Under Investigation (VUI) 202012/01, 501Y.V1
CC or 20B/501Y.V1. {ECO:0000305|PubMed:33413740}.
CC -!- POLYMORPHISM: Variant Omicron/BA.1 and BA.2 belong to a lineage first
CC isolated in South Africa (November 2021). {ECO:0000305}.
CC -!- POLYMORPHISM: Variant Omicron/BQ.1.1 belongs to a lineage first
CC isolated in Nigeria (November 2022). {ECO:0000305}.
CC -!- POLYMORPHISM: Variant Omicron/XBB.1.5 belongs to a lineage first
CC isolated in United States (November 2022). It is the result of
CC recombination between omicron BJ.1 and BM.1.1. Moreover XBB.1.5 do not
CC express ORF8. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MN908947; QHD43423.2; -; Genomic_RNA.
DR PDB; 6M3M; X-ray; 2.70 A; A/B/C/D=41-174.
DR PDB; 6VYO; X-ray; 1.70 A; A/B/C/D=47-173.
DR PDB; 6WJI; X-ray; 2.05 A; A/B/C/D/E/F=257-364.
DR PDB; 6WKP; X-ray; 2.67 A; A/B/C/D=47-173.
DR PDB; 6WZO; X-ray; 1.42 A; A/B/C/D=247-364.
DR PDB; 6WZQ; X-ray; 1.45 A; A/B/C/D=247-364.
DR PDB; 6YI3; NMR; -; A=44-180.
DR PDB; 6YUN; X-ray; 1.44 A; A/B=249-364.
DR PDB; 6ZCO; X-ray; 1.36 A; A=247-364.
DR PDB; 7ACS; NMR; -; A=44-180.
DR PDB; 7ACT; NMR; -; A=44-180.
DR PDB; 7C22; X-ray; 2.00 A; A/B/C/D=248-364.
DR PDB; 7CDZ; X-ray; 1.80 A; A/B/C/D=44-174.
DR PDB; 7CE0; X-ray; 1.50 A; A/B/C/D=255-364.
DR PDB; 7CR5; X-ray; 2.08 A; A=41-174.
DR PDB; 7DE1; X-ray; 2.00 A; A/B=250-364.
DR PDB; 7F2B; X-ray; 2.00 A; A/B=257-362.
DR PDB; 7F2E; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=255-362.
DR PDB; 7KGO; X-ray; 2.15 A; C=351-359.
DR PDB; 7KGP; X-ray; 1.40 A; C=316-324.
DR PDB; 7KGQ; X-ray; 1.34 A; C=222-230.
DR PDB; 7KGR; X-ray; 1.55 A; C=159-167.
DR PDB; 7KGS; X-ray; 1.58 A; C=138-146.
DR PDB; 7KGT; X-ray; 1.90 A; C=226-234.
DR PDB; 7LGD; X-ray; 2.88 A; E/F=105-113.
DR PDB; 7LTU; X-ray; 1.12 A; A/B=217-222.
DR PDB; 7LUX; X-ray; 1.30 A; A=217-222.
DR PDB; 7LUZ; X-ray; 1.10 A; A=243-248.
DR PDB; 7LV2; X-ray; 1.30 A; A=179-184.
DR PDB; 7N0I; X-ray; 2.20 A; A/B/C/D/E/F/G/H=269-364.
DR PDB; 7N0R; X-ray; 1.42 A; A/B=49-174.
DR PDB; 7N3C; X-ray; 1.82 A; C=47-173.
DR PDB; 7N3D; X-ray; 1.53 A; C=47-173.
DR PDB; 7O05; X-ray; 1.94 A; A/B/C/D=247-364.
DR PDB; 7O35; X-ray; 1.80 A; A/B/C/D=247-364.
DR PDB; 7O36; X-ray; 2.00 A; A/B/C/D=247-364.
DR PDB; 7PKU; NMR; -; B=191-263.
DR PDB; 7QIK; X-ray; 2.01 A; E/F=193-200.
DR PDB; 7QIP; X-ray; 2.65 A; C/D=201-210.
DR PDB; 7R98; X-ray; 2.51 A; A/B/C=49-174.
DR PDB; 7SD4; NMR; -; A=40-174.
DR PDB; 7STR; X-ray; 1.50 A; C=47-173.
DR PDB; 7STS; X-ray; 2.16 A; C/D=47-173.
DR PDB; 7SUE; X-ray; 2.90 A; C/D/J/K=47-173.
DR PDB; 7SUO; X-ray; 2.35 A; C/D=12-22.
DR PDB; 7UW3; X-ray; 1.70 A; A/B/C/D=40-174.
DR PDB; 7UXX; X-ray; 1.85 A; AAA/BBB/CCC/DDD/EEE/FFF=251-364.
DR PDB; 7UXZ; X-ray; 1.73 A; AAA/BBB/CCC/DDD/EEE/FFF=251-364.
DR PDB; 7VBD; X-ray; 1.94 A; A/B/C/D=48-174.
DR PDB; 7VBE; X-ray; 1.59 A; A/B=257-364.
DR PDB; 7VBF; X-ray; 1.30 A; A/B=255-364.
DR PDB; 7VNU; X-ray; 1.95 A; A/B/C/D=47-174.
DR PDB; 7WKJ; X-ray; 1.50 A; C=361-369.
DR PDB; 7WZO; X-ray; 2.64 A; A=47-174.
DR PDB; 7XWX; X-ray; 3.00 A; A/B/C/D/E/F/G/H=269-367.
DR PDB; 7XWZ; X-ray; 2.25 A; A/B=48-172.
DR PDB; 7XX1; X-ray; 1.90 A; A/B/C/D=49-173.
DR PDB; 7XXK; X-ray; 2.00 A; A/B/C/D/E/F=248-364.
DR PDB; 7YLB; X-ray; 2.41 A; A/B/C/D/G/H/J/K=247-364.
DR PDB; 7ZIT; X-ray; 1.79 A; C/D=194-200.
DR PDB; 8DNT; X-ray; 3.18 A; D/J/Q/X=222-230.
DR PDB; 8FD5; EM; 4.57 A; A=1-419.
DR PDB; 8FG2; EM; 6.00 A; A/B=1-419.
DR PDB; 8X1H; X-ray; 2.00 A; A/B/C/D=44-175.
DR PDBsum; 6M3M; -.
DR PDBsum; 6VYO; -.
DR PDBsum; 6WJI; -.
DR PDBsum; 6WKP; -.
DR PDBsum; 6WZO; -.
DR PDBsum; 6WZQ; -.
DR PDBsum; 6YI3; -.
DR PDBsum; 6YUN; -.
DR PDBsum; 6ZCO; -.
DR PDBsum; 7ACS; -.
DR PDBsum; 7ACT; -.
DR PDBsum; 7C22; -.
DR PDBsum; 7CDZ; -.
DR PDBsum; 7CE0; -.
DR PDBsum; 7CR5; -.
DR PDBsum; 7DE1; -.
DR PDBsum; 7F2B; -.
DR PDBsum; 7F2E; -.
DR PDBsum; 7KGO; -.
DR PDBsum; 7KGP; -.
DR PDBsum; 7KGQ; -.
DR PDBsum; 7KGR; -.
DR PDBsum; 7KGS; -.
DR PDBsum; 7KGT; -.
DR PDBsum; 7LGD; -.
DR PDBsum; 7LTU; -.
DR PDBsum; 7LUX; -.
DR PDBsum; 7LUZ; -.
DR PDBsum; 7LV2; -.
DR PDBsum; 7N0I; -.
DR PDBsum; 7N0R; -.
DR PDBsum; 7N3C; -.
DR PDBsum; 7N3D; -.
DR PDBsum; 7O05; -.
DR PDBsum; 7O35; -.
DR PDBsum; 7O36; -.
DR PDBsum; 7PKU; -.
DR PDBsum; 7QIK; -.
DR PDBsum; 7QIP; -.
DR PDBsum; 7R98; -.
DR PDBsum; 7SD4; -.
DR PDBsum; 7STR; -.
DR PDBsum; 7STS; -.
DR PDBsum; 7SUE; -.
DR PDBsum; 7SUO; -.
DR PDBsum; 7UW3; -.
DR PDBsum; 7UXX; -.
DR PDBsum; 7UXZ; -.
DR PDBsum; 7VBD; -.
DR PDBsum; 7VBE; -.
DR PDBsum; 7VBF; -.
DR PDBsum; 7VNU; -.
DR PDBsum; 7WKJ; -.
DR PDBsum; 7WZO; -.
DR PDBsum; 7XWX; -.
DR PDBsum; 7XWZ; -.
DR PDBsum; 7XX1; -.
DR PDBsum; 7XXK; -.
DR PDBsum; 7YLB; -.
DR PDBsum; 7ZIT; -.
DR PDBsum; 8DNT; -.
DR PDBsum; 8FD5; -.
DR PDBsum; 8FG2; -.
DR PDBsum; 8X1H; -.
DR BMRB; P0DTC9; -.
DR EMDB; EMD-29002; -.
DR EMDB; EMD-29072; -.
DR SASBDB; P0DTC9; -.
DR SMR; P0DTC9; -.
DR BioGRID; 4383847; 1315.
DR ComplexPortal; CPX-5686; SARS-CoV-2 nucleocapsid complex.
DR IntAct; P0DTC9; 608.
DR MINT; P0DTC9; -.
DR ChEMBL; CHEMBL5169223; -.
DR iPTMnet; P0DTC9; -.
DR ABCD; P0DTC9; 26 sequenced antibodies.
DR DNASU; 43740575; -.
DR AGR; RefSeq:YP_009724397; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-9694322; Virion Assembly and Release.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR Reactome; R-HSA-9694635; Translation of Structural Proteins.
DR Reactome; R-HSA-9694786; Transcription of SARS-CoV-2 sgRNAs.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9733458; Induction of Cell-Cell Fusion.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SIGNOR; P0DTC9; -.
DR PRO; PR:P0DTC9; -.
DR Proteomes; UP000464024; Genome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0044177; C:host cell Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0043655; C:host extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IDA:DisProt.
DR GO; GO:0042612; C:MHC class I protein complex; EXP:DisProt.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IPI:ComplexPortal.
DR GO; GO:0019013; C:viral nucleocapsid; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042288; F:MHC class I protein binding; EXP:DisProt.
DR GO; GO:0140693; F:molecular condensate scaffold activity; IDA:DisProt.
DR GO; GO:0042803; F:protein homodimerization activity; EXP:DisProt.
DR GO; GO:0140311; F:protein sequestering activity; IDA:UniProt.
DR GO; GO:0003723; F:RNA binding; IDA:UniProt.
DR GO; GO:0035613; F:RNA stem-loop binding; IDA:DisProt.
DR GO; GO:0039709; P:cytoplasmic capsid assembly; IDA:UniProt.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:ComplexPortal.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0052572; P:response to host immune response; IDA:DisProt.
DR GO; GO:0019074; P:viral RNA genome packaging; NAS:ComplexPortal.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
DR HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR043505; NCAP_bCoV.
DR InterPro; IPR001218; Nucleocap_CoV.
DR InterPro; IPR037179; Nucleocapsid_C.
DR InterPro; IPR037195; Nucleocapsid_N.
DR Pfam; PF00937; CoV_nucleocap; 1.
DR PIRSF; PIRSF003888; Corona_nucleocap; 1.
DR SUPFAM; SSF110304; Coronavirus RNA-binding domain; 1.
DR SUPFAM; SSF103068; Nucleocapsid protein dimerization domain; 1.
DR PROSITE; PS51929; COV_N_CTD; 1.
DR PROSITE; PS51928; COV_N_NTD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Host cytoplasm; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Secreted;
KW Transcription; Transcription regulation; Viral nucleoprotein; Virion.
FT CHAIN 1..419
FT /note="Nucleoprotein"
FT /id="PRO_0000449656"
FT DOMAIN 48..174
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276,
FT ECO:0000269|PubMed:32363136"
FT DOMAIN 247..364
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..186
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..206
FT /note="SR region"
FT /evidence="ECO:0000305|PubMed:32974389"
FT REGION 233..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..361
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 260..340
FT /note="Putative NLRP3 binding"
FT /evidence="ECO:0000269|PubMed:34341353"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..419
FT /note="Tetramerization"
FT /evidence="ECO:0000269|PubMed:32654247"
FT MOTIF 256..264
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:P59595"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 92
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000269|PubMed:33264373,
FT ECO:0007744|PDB:7ACS, ECO:0007744|PDB:7ACT"
FT BINDING 107
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000269|PubMed:33264373,
FT ECO:0007744|PDB:7ACS, ECO:0007744|PDB:7ACT"
FT BINDING 149
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000269|PubMed:33264373,
FT ECO:0007744|PDB:7ACS, ECO:0007744|PDB:7ACT"
FT SITE 399..402
FT /note="Cleavage (by host CASP6)"
FT /evidence="ECO:0000250|UniProtKB:P59595"
FT MOD_RES 176
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 206
FT /note="Phosphoserine; by host GSK3-alpha and GSK3-beta"
FT /evidence="ECO:0000269|PubMed:34593624"
FT VARIANT 2..3
FT /note="SD -> Y (in strain: Eta/B.1.525)"
FT /evidence="ECO:0000305"
FT VARIANT 3
FT /note="D -> L (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 12
FT /note="A -> G (in strain: Eta/B.1.525)"
FT VARIANT 13
FT /note="P -> L (in strain: Lambda/C.37, Omicron/BA.1,
FT Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/
FT BA.4, Omicron/BA.5, Omicron/BQ.1.1, Omicron/XBB.1.5,
FT Omicron/EG.5.1)"
FT /evidence="ECO:0000305"
FT VARIANT 31..33
FT /note="Missing (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/
FT BA.5, Omicron/BQ.1.1, Omicron/XBB.1.5, Omicron/EG.5.1)"
FT /evidence="ECO:0000305"
FT VARIANT 63
FT /note="D -> G (in strain: Delta/B.1.617.2)"
FT /evidence="ECO:0000305"
FT VARIANT 80
FT /note="P -> R (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 119
FT /note="A -> S (in strain: Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 136
FT /note="E -> D (in strain: Omicron/BQ.1.1)"
FT /evidence="ECO:0000305"
FT VARIANT 151
FT /note="P -> S (in strain: Omicron/BA.4)"
FT /evidence="ECO:0000305"
FT VARIANT 203..204
FT /note="RG -> KR (in strain: Alpha/B.1.1.7, Gamma/P.1, Zeta/
FT P.2, Theta/P.3, Lambda/C.37, Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.2.75, Omicron/BA.4, Omicron/
FT BA.5, Omicron/BQ.1.1, Omicron/XBB.1.5, Omicron/EG.5.1)"
FT /evidence="ECO:0000305"
FT VARIANT 203
FT /note="R -> M (in strain: Delta/B.1.617.2, Kappa/
FT B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 205
FT /note="T -> I (in strain: Beta/B.1.351, Epsilon/B.1.429,
FT Eta/B.1.525 and Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 214
FT /note="G -> C (in strain: Lambda/C.37)"
FT VARIANT 234
FT /note="M -> I (in strain: Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 235
FT /note="S -> F (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 377
FT /note="D -> Y (in strain: Delta/B.1.617.2, Kappa/
FT B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 413
FT /note="S -> R (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.2.75, Omicron/BA.4, Omicron/BA.5, Omicron/
FT BQ.1.1, Omicron/XBB.1.5, Omicron/EG.5.1)"
FT /evidence="ECO:0000305"
FT MUTAGEN 68
FT /note="R->E: No effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 92
FT /note="R->E: Complete loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 94
FT /note="I->A: Partial loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 107
FT /note="R->E: Complete loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 109
FT /note="Y->A: Significant decrease of RNA binding capacity."
FT /evidence="ECO:0000269|PubMed:32363136"
FT MUTAGEN 163
FT /note="Q->A: Partial loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 172
FT /note="Y->A: Partial loss of RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 174
FT /note="E->R: Significant increase of RNA-binding."
FT /evidence="ECO:0000269|PubMed:33264373"
FT MUTAGEN 188
FT /note="S->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:34593624"
FT MUTAGEN 203..204
FT /note="RG->KR: Partial increase of pathogenesis and fitness
FT in vivo. No effect on virus replication ex vivo."
FT /evidence="ECO:0000269|PubMed:35728038"
FT MUTAGEN 203
FT /note="R->M: No effect on virus replication ex vivo."
FT /evidence="ECO:0000269|PubMed:35728038"
FT MUTAGEN 206
FT /note="S->A: Partial loss of phosphorylation."
FT /evidence="ECO:0000269|PubMed:34593624"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7STR"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7N0R"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:7SD4"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:7N0R"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:7ACT"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7N3D"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:7N0R"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:7N0R"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7ACT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7VNU"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:7ACT"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:7PKU"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:7PKU"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:7LTU"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:7VBF"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:7CE0"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:7VBF"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:7F2E"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:7VBF"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7VBF"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:7VBF"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:7VBF"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:7VBF"
FT STRAND 328..338
FT /evidence="ECO:0007829|PDB:7VBF"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:7VBF"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:7VBF"
SQ SEQUENCE 419 AA; 45626 MW; 56688DB785414E81 CRC64;
MSDNGPQNQR NAPRITFGGP SDSTGSNQNG ERSGARSKQR RPQGLPNNTA SWFTALTQHG
KEDLKFPRGQ GVPINTNSSP DDQIGYYRRA TRRIRGGDGK MKDLSPRWYF YYLGTGPEAG
LPYGANKDGI IWVATEGALN TPKDHIGTRN PANNAAIVLQ LPQGTTLPKG FYAEGSRGGS
QASSRSSSRS RNSSRNSTPG SSRGTSPARM AGNGGDAALA LLLLDRLNQL ESKMSGKGQQ
QQGQTVTKKS AAEASKKPRQ KRTATKAYNV TQAFGRRGPE QTQGNFGDQE LIRQGTDYKH
WPQIAQFAPS ASAFFGMSRI GMEVTPSGTW LTYTGAIKLD DKDPNFKDQV ILLNKHIDAY
KTFPPTEPKK DKKKKADETQ ALPQRQKKQQ TVTLLPAADL DDFSKQLQQS MSSADSTQA
//