ID   ORF9B_SARS2             Reviewed;          97 AA.
AC   P0DTD2;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 1.
DT   10-FEB-2021, entry version 6.
DE   RecName: Full=ORF9b protein;
DE            Short=ORF9b;
DE   AltName: Full=Accessory protein 9b;
DE   AltName: Full=ORF-9b;
DE   AltName: Full=Protein 9b;
GN   ORFNames=9b;
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.
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   INTERACTION WITH HUMAN TOMM70, AND 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).
CC   -!- FUNCTION: Plays a role in the inhibition of host innate immune response
CC       by targeting the mitochondrial-associated adapter MAVS.
CC       Mechanistically, usurps the E3 ligase ITCH to trigger the degradation
CC       of MAVS, TRAF3, and TRAF6. In addition, causes mitochondrial elongation
CC       by triggering ubiquitination and proteasomal degradation of dynamin-
CC       like protein 1/DNM1L. {ECO:0000250|UniProtKB:P59636}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with host TOMM70
CC       (PubMed:33060197). Interacts with host MAVS. Interacts with ORF6
CC       protein (By similarity). {ECO:0000250|UniProtKB:P59636,
CC       ECO:0000269|PubMed:33060197}.
CC   -!- INTERACTION:
CC       P0DTD2; O94826: TOMM70; Xeno; NbExp=16; IntAct=EBI-25475909, EBI-2800236;
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:33060197}.
CC       Host mitochondrion {ECO:0000269|PubMed:33060197}.
CC   -!- MISCELLANEOUS: The open reading frame (ORF) encoding for this protein
CC       overlaps with the N ORF. {ECO:0000269|PubMed:32015508}.
CC   -!- SIMILARITY: Belongs to the coronavirus group 2 protein 9b family.
CC       {ECO:0000305}.
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DR   EMBL; MN908947; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PDB; 6Z4U; X-ray; 1.95 A; A/B=1-97.
DR   PDB; 7KDT; EM; 3.05 A; B=1-97.
DR   PDBsum; 6Z4U; -.
DR   PDBsum; 7KDT; -.
DR   SMR; P0DTD2; -.
DR   BioGRID; 4383874; 400.
DR   ComplexPortal; CPX-6100; SARS-CoV-2 9b complex.
DR   IntAct; P0DTD2; 35.
DR   Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR   PRO; PR:P0DTD2; -.
DR   Proteomes; UP000464024; Genome.
DR   GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019012; C:virion; IEA:UniProtKB-SubCell.
DR   GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
DR   InterPro; IPR018542; Protein_9b_Betacoronavirus.
DR   InterPro; IPR037223; Protein_9b_SARS.
DR   Pfam; PF09399; bCoV_lipid_BD; 1.
DR   SUPFAM; SSF141666; SSF141666; 1.
DR   PROSITE; PS51920; SARS_9B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host cytoplasm; Host mitochondrion; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host MAVS by virus; Inhibition of host RLR pathway by virus;
KW   Reference proteome; Viral immunoevasion.
FT   CHAIN           1..97
FT                   /note="ORF9b protein"
FT                   /evidence="ECO:0000250|UniProtKB:P59636"
FT                   /id="PRO_0000449657"
FT   DOMAIN          8..97
FT                   /note="9b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01268"
FT   MOTIF           45..53
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000250|UniProtKB:P59636"
FT   HELIX           5..7
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          12..15
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          19..23
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          40..42
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          44..50
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          52..61
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          64..66
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          68..74
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   HELIX           84..86
FT                   /evidence="ECO:0000244|PDB:6Z4U"
FT   STRAND          89..96
FT                   /evidence="ECO:0000244|PDB:6Z4U"
SQ   SEQUENCE   97 AA;  10797 MW;  62CFB65C1804545E CRC64;
     MDPKISEMHP ALRLVDPQIQ LAVTRMENAV GRDQNNVGPK VYPIILRLGS PLSLNMARKT
     LNSLEDKAFQ LTPIAVQMTK LATTEELPDE FVVVTVK
//