ID SNP29_HUMAN Reviewed; 258 AA.
AC O95721;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JUL-2024, entry version 206.
DE RecName: Full=Synaptosomal-associated protein 29 {ECO:0000312|HGNC:HGNC:11133};
DE Short=SNAP-29 {ECO:0000312|HGNC:HGNC:11133};
DE AltName: Full=Soluble 29 kDa NSF attachment protein {ECO:0000312|HGNC:HGNC:11133};
DE AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN Name=SNAP29 {ECO:0000312|HGNC:HGNC:11133};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9852078; DOI=10.1074/jbc.273.51.34171;
RA Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
RA Scheller R.H.;
RT "Three novel proteins of the syntaxin/SNAP-25 family.";
RL J. Biol. Chem. 273:34171-34179(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Schardt A., Kraemer E.-M., Werner H., Nave K.-A.;
RT "Genomic organization of the human SNAP29 gene.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INVOLVEMENT IN CEDNIK.
RX PubMed=15968592; DOI=10.1086/432556;
RA Sprecher E., Ishida-Yamamoto A., Mizrahi-Koren M., Rapaport D.,
RA Goldsher D., Indelman M., Topaz O., Chefetz I., Keren H., O'brien T.J.,
RA Bercovich D., Shalev S., Geiger D., Bergman R., Horowitz M., Mandel H.;
RT "A mutation in SNAP29, coding for a SNARE protein involved in intracellular
RT trafficking, causes a novel neurocutaneous syndrome characterized by
RT cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar
RT keratoderma.";
RL Am. J. Hum. Genet. 77:242-251(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION IN AUTOPHAGY, AND INTERACTION WITH VAMP8 AND STX17.
RX PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA Itakura E., Kishi-Itakura C., Mizushima N.;
RT "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes
RT for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-78; SER-114; THR-130;
RP THR-137; SER-163; SER-182; SER-185; SER-204 AND SER-210, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25686250; DOI=10.1038/ncb3109;
RA Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J., Baxa U.,
RA Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
RA Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
RT "Early steps in primary cilium assembly require EHD1/EHD3-dependent ciliary
RT vesicle formation.";
RL Nat. Cell Biol. 17:228-240(2015).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP INTERACTION WITH STX17.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
RN [14]
RP INTERACTION WITH HANTAAN HANTAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061;
RA Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L.,
RA Zhang F.;
RT "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate
RT Autophagy Flux to Restrain Host Innate Immune Responses.";
RL Cell Rep. 27:2075-2091.e5(2019).
RN [15]
RP INTERACTION WITH EIPR1.
RX PubMed=27440922; DOI=10.1091/mbc.e16-04-0209;
RA Gershlick D.C., Schindler C., Chen Y., Bonifacino J.S.;
RT "TSSC1 is novel component of the endosomal retrieval machinery.";
RL Mol. Biol. Cell 27:2867-2878(2016).
RN [16]
RP INTERACTION WITH STX17 (MICROBIAL INFECTION).
RX PubMed=33422265; DOI=10.1016/j.devcel.2020.12.010;
RA Miao G., Zhao H., Li Y., Ji M., Chen Y., Shi Y., Bi Y., Wang P., Zhang H.;
RT "ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
RT assembly of the SNARE complex required for autolysosome formation.";
RL Dev. Cell 56:427-442(2020).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 39-116 AND 194-258 IN COMPLEX WITH
RP STX17 AND VAMP8, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25686604; DOI=10.1038/nature14147;
RA Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M.,
RA Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.;
RT "ATG14 promotes membrane tethering and fusion of autophagosomes to
RT endolysosomes.";
RL Nature 520:563-566(2015).
CC -!- FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment
CC protein receptors, are essential proteins for fusion of cellular
CC membranes. SNAREs localized on opposing membranes assemble to form a
CC trans-SNARE complex, an extended, parallel four alpha-helical bundle
CC that drives membrane fusion. SNAP29 is a SNARE involved in autophagy
CC through the direct control of autophagosome membrane fusion with the
CC lysososome membrane. Also plays a role in ciliogenesis by regulating
CC membrane fusions. {ECO:0000269|PubMed:23217709,
CC ECO:0000269|PubMed:25686250, ECO:0000269|PubMed:25686604}.
CC -!- SUBUNIT: Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17,
CC involved in fusion of autophagosome with lysosome (PubMed:23217709,
CC PubMed:25686604). Interacts with multiple syntaxins including STX6 (By
CC similarity). Interacts with EIPR1 (PubMed:27440922). Interacts with
CC STX17; this interaction is increased in the absence of TMEM39A
CC (PubMed:31806350, PubMed:33422265). {ECO:0000250|UniProtKB:Q9Z2P6,
CC ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604,
CC ECO:0000269|PubMed:27440922, ECO:0000269|PubMed:31806350,
CC ECO:0000269|PubMed:33422265}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hantaan hantavirus
CC nucleoprotein; this interaction prevents the breakdown of the viral
CC glycoprotein N by virus-triggered autophagy.
CC {ECO:0000269|PubMed:31091447}.
CC -!- SUBUNIT: (Microbial infection) The interaction with STX17 is decreased
CC in presence of SARS coronavirus-2/SARS-CoV-2 ORF3A protein.
CC {ECO:0000269|PubMed:33422265}.
CC -!- INTERACTION:
CC O95721; P54253: ATXN1; NbExp=3; IntAct=EBI-490676, EBI-930964;
CC O95721; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-490676, EBI-3866319;
CC O95721; Q9H4M9: EHD1; NbExp=3; IntAct=EBI-490676, EBI-490691;
CC O95721; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-490676, EBI-10175124;
CC O95721; Q8IZT9: FAM9C; NbExp=3; IntAct=EBI-490676, EBI-2870039;
CC O95721; P42858: HTT; NbExp=3; IntAct=EBI-490676, EBI-466029;
CC O95721; Q9H115: NAPB; NbExp=8; IntAct=EBI-490676, EBI-3921185;
CC O95721; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-490676, EBI-741158;
CC O95721; O15294: OGT; NbExp=2; IntAct=EBI-490676, EBI-539828;
CC O95721; Q86Y82: STX12; NbExp=5; IntAct=EBI-490676, EBI-2691717;
CC O95721; O14662-5: STX16; NbExp=3; IntAct=EBI-490676, EBI-9089968;
CC O95721; P56962: STX17; NbExp=10; IntAct=EBI-490676, EBI-2797775;
CC O95721; P61266: STX1B; NbExp=3; IntAct=EBI-490676, EBI-9071709;
CC O95721; P32856-2: STX2; NbExp=3; IntAct=EBI-490676, EBI-11956649;
CC O95721; Q13277: STX3; NbExp=3; IntAct=EBI-490676, EBI-1394295;
CC O95721; O43752: STX6; NbExp=3; IntAct=EBI-490676, EBI-2695795;
CC O95721; Q13114: TRAF3; NbExp=4; IntAct=EBI-490676, EBI-357631;
CC O95721; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-490676, EBI-12003468;
CC O95721; Q6F5E7: TXNRD3NB; NbExp=3; IntAct=EBI-490676, EBI-18122152;
CC O95721; P23763: VAMP1; NbExp=3; IntAct=EBI-490676, EBI-10201335;
CC O95721; P63027: VAMP2; NbExp=3; IntAct=EBI-490676, EBI-520113;
CC O95721; Q15836: VAMP3; NbExp=3; IntAct=EBI-490676, EBI-722343;
CC O95721; O75379-2: VAMP4; NbExp=3; IntAct=EBI-490676, EBI-10187996;
CC O95721; O95183: VAMP5; NbExp=9; IntAct=EBI-490676, EBI-10191195;
CC O95721; Q9BV40: VAMP8; NbExp=6; IntAct=EBI-490676, EBI-727028;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23217709}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:25686604}; Peripheral membrane protein
CC {ECO:0000305}. Cell projection, cilium membrane
CC {ECO:0000269|PubMed:25686250}; Peripheral membrane protein
CC {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via
CC interaction with syntaxins, but a significant portion is cytoplasmic.
CC Localizes to the ciliary pocket from where the cilium protrudes.
CC {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250}.
CC -!- TISSUE SPECIFICITY: Found in brain, heart, kidney, liver, lung,
CC placenta, skeletal muscle, spleen and pancreas.
CC {ECO:0000269|PubMed:9852078}.
CC -!- DISEASE: Cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar
CC keratoderma syndrome (CEDNIK) [MIM:609528]: A neurocutaneous syndrome
CC characterized by cerebral dysgenesis, neuropathy, ichthyosis and
CC palmoplantar keratoderma. {ECO:0000269|PubMed:15968592}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; AF115436; AAD11436.1; -; mRNA.
DR EMBL; AF278704; AAF91421.1; -; Genomic_DNA.
DR EMBL; CR456582; CAG30468.1; -; mRNA.
DR EMBL; BT007357; AAP36021.1; -; mRNA.
DR EMBL; BC009715; AAH09715.1; -; mRNA.
DR CCDS; CCDS13784.1; -.
DR RefSeq; NP_004773.1; NM_004782.3.
DR PDB; 4WY4; X-ray; 1.40 A; C=39-116, D=194-258.
DR PDB; 7BV6; X-ray; 3.05 A; C/G/K/O/S/W=40-130, D/H/L/P/T/X=191-258.
DR PDBsum; 4WY4; -.
DR PDBsum; 7BV6; -.
DR AlphaFoldDB; O95721; -.
DR SMR; O95721; -.
DR BioGRID; 114748; 263.
DR CORUM; O95721; -.
DR DIP; DIP-56475N; -.
DR IntAct; O95721; 113.
DR MINT; O95721; -.
DR STRING; 9606.ENSP00000215730; -.
DR GlyCosmos; O95721; 4 sites, 1 glycan.
DR GlyGen; O95721; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; O95721; -.
DR MetOSite; O95721; -.
DR PhosphoSitePlus; O95721; -.
DR BioMuta; SNAP29; -.
DR jPOST; O95721; -.
DR MassIVE; O95721; -.
DR PaxDb; 9606-ENSP00000215730; -.
DR PeptideAtlas; O95721; -.
DR ProteomicsDB; 51014; -.
DR Pumba; O95721; -.
DR Antibodypedia; 23352; 205 antibodies from 29 providers.
DR DNASU; 9342; -.
DR Ensembl; ENST00000215730.12; ENSP00000215730.6; ENSG00000099940.12.
DR GeneID; 9342; -.
DR KEGG; hsa:9342; -.
DR MANE-Select; ENST00000215730.12; ENSP00000215730.6; NM_004782.4; NP_004773.1.
DR UCSC; uc011ahw.3; human.
DR AGR; HGNC:11133; -.
DR CTD; 9342; -.
DR DisGeNET; 9342; -.
DR GeneCards; SNAP29; -.
DR HGNC; HGNC:11133; SNAP29.
DR HPA; ENSG00000099940; Low tissue specificity.
DR MalaCards; SNAP29; -.
DR MIM; 604202; gene.
DR MIM; 609528; phenotype.
DR neXtProt; NX_O95721; -.
DR OpenTargets; ENSG00000099940; -.
DR Orphanet; 66631; CEDNIK syndrome.
DR PharmGKB; PA35981; -.
DR VEuPathDB; HostDB:ENSG00000099940; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR InParanoid; O95721; -.
DR OMA; NLDEMCD; -.
DR OrthoDB; 4213488at2759; -.
DR PhylomeDB; O95721; -.
DR TreeFam; TF320226; -.
DR PathwayCommons; O95721; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR SignaLink; O95721; -.
DR SIGNOR; O95721; -.
DR BioGRID-ORCS; 9342; 64 hits in 1166 CRISPR screens.
DR ChiTaRS; SNAP29; human.
DR EvolutionaryTrace; O95721; -.
DR GeneWiki; SNAP29; -.
DR GenomeRNAi; 9342; -.
DR Pharos; O95721; Tbio.
DR PRO; PR:O95721; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O95721; Protein.
DR Bgee; ENSG00000099940; Expressed in left testis and 206 other cell types or tissues.
DR ExpressionAtlas; O95721; baseline and differential.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0020018; C:ciliary pocket membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IDA:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR CDD; cd15856; SNARE_SNAP29C; 1.
DR CDD; cd15887; SNARE_SNAP29N; 1.
DR Gene3D; 1.20.5.110; -; 2.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR19305:SF9; SYNAPTOSOMAL-ASSOCIATED PROTEIN 29; 1.
DR SMART; SM00397; t_SNARE; 2.
DR SUPFAM; SSF58038; SNARE fusion complex; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Ichthyosis; Membrane; Neuropathy;
KW Palmoplantar keratoderma; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..258
FT /note="Synaptosomal-associated protein 29"
FT /id="PRO_0000213601"
FT DOMAIN 196..258
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..107
FT /evidence="ECO:0000255"
FT COMPBIAS 10..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT HELIX 40..113
FT /evidence="ECO:0007829|PDB:4WY4"
FT HELIX 195..255
FT /evidence="ECO:0007829|PDB:4WY4"
SQ SEQUENCE 258 AA; 28970 MW; 7E1CDBA22D6F5A3C CRC64;
MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL RRAEATAAST
SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ DLKISQKHIN SIKSVFGGLV
NYFKSKPVET PPEQNGTLTS QPNNRLKEAI STSKEQEAKY QASHPNLRKL DDTDPVPRGA
GSAMSTDAYP KNPHLRAYHQ KIDSNLDELS MGLGRLKDIA LGMQTEIEEQ DDILDRLTTK
VDKLDVNIKS TERKVRQL
//