STX7_HUMAN
ID STX7_HUMAN Reviewed; 261 AA.
AC O15400; E1P579; Q5SZW2; Q96ES9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Syntaxin-7;
GN Name=STX7;
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] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9358037; DOI=10.1016/s0378-1119(97)00343-0;
RA Wang H., Frelin L., Pevsner J.;
RT "Human syntaxin 7: a Pep12p/Vps6p homologue implicated in vesicle
RT trafficking to lysosomes.";
RL Gene 199:39-48(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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 [5]
RP PROTEIN SEQUENCE OF 2-17, AND ACETYLATION AT SER-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10564279; DOI=10.1091/mbc.10.11.3891;
RA Prekeris R., Yang B., Oorschot V., Klumperman J., Scheller R.H.;
RT "Differential roles of syntaxin 7 and syntaxin 8 in endosomal
RT trafficking.";
RL Mol. Biol. Cell 10:3891-3908(1999).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10692457; DOI=10.1074/jbc.275.9.6523;
RA Nakamura N., Yamamoto A., Wada Y., Futai M.;
RT "Syntaxin 7 mediates endocytic trafficking to late endosomes.";
RL J. Biol. Chem. 275:6523-6529(2000).
RN [8]
RP INTERACTION WITH VPS11; VPS16; VPS18 AND VPS33A.
RX PubMed=11382755; DOI=10.1074/jbc.m101778200;
RA Kim B.Y., Kraemer H., Yamamoto A., Kominami E., Kohsaka S., Akazawa C.;
RT "Molecular characterization of mammalian homologues of class C Vps proteins
RT that interact with syntaxin-7.";
RL J. Biol. Chem. 276:29393-29402(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4; SER-45; SER-75; SER-126
RP AND SER-129, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: May be involved in protein trafficking from the plasma
CC membrane to the early endosome (EE) as well as in homotypic fusion of
CC endocytic organelles. Mediates the endocytic trafficking from early
CC endosomes to late endosomes and lysosomes.
CC -!- SUBUNIT: Forms a SNARE complex with VTI1B, STX8 and VAMP8 which
CC functions in the homotypic fusion of late endosomes. Component of the
CC SNARE complex composed of STX7, STX8, VAMP7 and VTI1B that is required
CC for heterotypic fusion of late endosomes with lysosomes (By
CC similarity). Interacts with VPS11, VPS16 and VPS18. Interacts with
CC VPS33A. Interacts with TPC1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O70439, ECO:0000269|PubMed:11382755}.
CC -!- INTERACTION:
CC O15400; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-3221827, EBI-7054139;
CC O15400; Q13520: AQP6; NbExp=3; IntAct=EBI-3221827, EBI-13059134;
CC O15400; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-3221827, EBI-11343438;
CC O15400; Q9HA82: CERS4; NbExp=3; IntAct=EBI-3221827, EBI-2622997;
CC O15400; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-3221827, EBI-1045797;
CC O15400; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-3221827, EBI-6942903;
CC O15400; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-3221827, EBI-8637742;
CC O15400; Q15125: EBP; NbExp=3; IntAct=EBI-3221827, EBI-3915253;
CC O15400; Q9NYP7: ELOVL5; NbExp=3; IntAct=EBI-3221827, EBI-11037623;
CC O15400; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-3221827, EBI-18636064;
CC O15400; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-3221827, EBI-18938272;
CC O15400; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-3221827, EBI-3918971;
CC O15400; Q8NFK1: GJC3; NbExp=3; IntAct=EBI-3221827, EBI-20110678;
CC O15400; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-3221827, EBI-1052304;
CC O15400; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-3221827, EBI-18053395;
CC O15400; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-3221827, EBI-10266796;
CC O15400; Q9H400: LIME1; NbExp=3; IntAct=EBI-3221827, EBI-2830566;
CC O15400; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-3221827, EBI-10264855;
CC O15400; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-3221827, EBI-11956541;
CC O15400; O14880: MGST3; NbExp=3; IntAct=EBI-3221827, EBI-724754;
CC O15400; Q6IN84: MRM1; NbExp=3; IntAct=EBI-3221827, EBI-5454865;
CC O15400; Q9ULD2-3: MTUS1; NbExp=3; IntAct=EBI-3221827, EBI-18051665;
CC O15400; Q9H902: REEP1; NbExp=3; IntAct=EBI-3221827, EBI-1644241;
CC O15400; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-3221827, EBI-10192441;
CC O15400; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-3221827, EBI-12375429;
CC O15400; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-3221827, EBI-3920694;
CC O15400; Q14973: SLC10A1; NbExp=3; IntAct=EBI-3221827, EBI-3923031;
CC O15400; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-3221827, EBI-18159983;
CC O15400; Q16623: STX1A; NbExp=3; IntAct=EBI-3221827, EBI-712466;
CC O15400; P32856-2: STX2; NbExp=3; IntAct=EBI-3221827, EBI-11956649;
CC O15400; Q12846: STX4; NbExp=7; IntAct=EBI-3221827, EBI-744942;
CC O15400; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-3221827, EBI-6448756;
CC O15400; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-3221827, EBI-6269551;
CC O15400; Q24JQ0: TMEM241; NbExp=3; IntAct=EBI-3221827, EBI-18172866;
CC O15400; Q0VDI3: TMEM267; NbExp=3; IntAct=EBI-3221827, EBI-17555467;
CC O15400; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-3221827, EBI-11742770;
CC O15400; O15393-2: TMPRSS2; NbExp=4; IntAct=EBI-3221827, EBI-12345267;
CC O15400; Q9Y320: TMX2; NbExp=3; IntAct=EBI-3221827, EBI-6447886;
CC O15400; Q9BV40: VAMP8; NbExp=2; IntAct=EBI-3221827, EBI-727028;
CC O15400; Q9H270: VPS11; NbExp=2; IntAct=EBI-3221827, EBI-373380;
CC O15400; Q9P253: VPS18; NbExp=2; IntAct=EBI-3221827, EBI-1053363;
CC O15400; Q5T4F4: ZFYVE27; NbExp=3; IntAct=EBI-3221827, EBI-3892947;
CC -!- SUBCELLULAR LOCATION: Early endosome membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15400-2; Sequence=VSP_012938;
CC -!- TISSUE SPECIFICITY: Highest expression is found in placenta followed by
CC heart, skeletal muscle, kidney and brain. Low expression is found in
CC pancreas, lung and liver.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U77942; AAC51851.1; -; mRNA.
DR EMBL; AL357034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL589691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48029.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48030.1; -; Genomic_DNA.
DR EMBL; BC011975; AAH11975.1; -; mRNA.
DR CCDS; CCDS5153.1; -. [O15400-1]
DR CCDS; CCDS87441.1; -. [O15400-2]
DR RefSeq; NP_001313507.1; NM_001326578.1. [O15400-1]
DR RefSeq; NP_001313508.1; NM_001326579.1. [O15400-1]
DR RefSeq; NP_001313509.1; NM_001326580.1. [O15400-2]
DR RefSeq; NP_003560.2; NM_003569.2. [O15400-1]
DR RefSeq; XP_011534480.1; XM_011536178.1.
DR AlphaFoldDB; O15400; -.
DR SMR; O15400; -.
DR BioGRID; 114003; 638.
DR CORUM; O15400; -.
DR DIP; DIP-57384N; -.
DR IntAct; O15400; 122.
DR MINT; O15400; -.
DR STRING; 9606.ENSP00000356918; -.
DR iPTMnet; O15400; -.
DR PhosphoSitePlus; O15400; -.
DR SwissPalm; O15400; -.
DR BioMuta; STX7; -.
DR OGP; O15400; -.
DR EPD; O15400; -.
DR jPOST; O15400; -.
DR MassIVE; O15400; -.
DR MaxQB; O15400; -.
DR PaxDb; O15400; -.
DR PeptideAtlas; O15400; -.
DR PRIDE; O15400; -.
DR ProteomicsDB; 48639; -. [O15400-1]
DR ProteomicsDB; 48640; -. [O15400-2]
DR TopDownProteomics; O15400-1; -. [O15400-1]
DR Antibodypedia; 729; 174 antibodies from 28 providers.
DR DNASU; 8417; -.
DR Ensembl; ENST00000367937.4; ENSP00000356914.4; ENSG00000079950.14. [O15400-2]
DR Ensembl; ENST00000367941.7; ENSP00000356918.1; ENSG00000079950.14. [O15400-1]
DR GeneID; 8417; -.
DR KEGG; hsa:8417; -.
DR MANE-Select; ENST00000367941.7; ENSP00000356918.1; NM_003569.3; NP_003560.2.
DR UCSC; uc003qdg.3; human. [O15400-1]
DR CTD; 8417; -.
DR DisGeNET; 8417; -.
DR GeneCards; STX7; -.
DR HGNC; HGNC:11442; STX7.
DR HPA; ENSG00000079950; Low tissue specificity.
DR MIM; 603217; gene.
DR neXtProt; NX_O15400; -.
DR OpenTargets; ENSG00000079950; -.
DR PharmGKB; PA36239; -.
DR VEuPathDB; HostDB:ENSG00000079950; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_059257_1_1_1; -.
DR InParanoid; O15400; -.
DR OMA; HMENGLN; -.
DR OrthoDB; 1204812at2759; -.
DR PhylomeDB; O15400; -.
DR TreeFam; TF315607; -.
DR PathwayCommons; O15400; -.
DR SignaLink; O15400; -.
DR BioGRID-ORCS; 8417; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; STX7; human.
DR GeneWiki; STX7; -.
DR GenomeRNAi; 8417; -.
DR Pharos; O15400; Tbio.
DR PRO; PR:O15400; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O15400; protein.
DR Bgee; ENSG00000079950; Expressed in cortical plate and 207 other tissues.
DR Genevisible; O15400; HS.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0070820; C:tertiary granule; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0019869; F:chloride channel inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IDA:MGI.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0070925; P:organelle assembly; IDA:UniProtKB.
DR GO; GO:0051640; P:organelle localization; IDA:UniProtKB.
DR GO; GO:1902685; P:positive regulation of receptor localization to synapse; IMP:UniProtKB.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd00179; SynN; 1.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF14523; Syntaxin_2; 1.
DR SMART; SM00503; SynN; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Direct protein sequencing;
KW Endosome; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT CHAIN 2..261
FT /note="Syntaxin-7"
FT /id="PRO_0000210213"
FT TOPO_DOM 2..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..261
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 165..227
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 129..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 47..69
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O70439"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70439"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 232..261
FT /note="RKSRKTLCIIILILVIGVAIISLIIWGLNH -> KKDSCMLM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_012938"
FT CONFLICT 12
FT /note="A -> T (in Ref. 1; AAC51851)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 29816 MW; 42AC173F0233ACDA CRC64;
MSYTPGVGGD PAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ QLQQKQQYTN
QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKVQRQ AAEREKEFVA
RVRASSRVSG SFPEDSSKER NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
DIMDINEIFK DLGMMIHEQG DVIDSIEANV ENAEVHVQQA NQQLSRAADY QRKSRKTLCI
IILILVIGVA IISLIIWGLN H
