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 27-MAR-2024, entry version 203. 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}. 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; 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; 662. DR CORUM; O15400; -. DR DIP; DIP-57384N; -. DR IntAct; O15400; 128. DR MINT; O15400; -. DR STRING; 9606.ENSP00000356918; -. DR GlyGen; O15400; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000356918; -. DR PeptideAtlas; O15400; -. DR ProteomicsDB; 48639; -. [O15400-1] DR ProteomicsDB; 48640; -. [O15400-2] DR TopDownProteomics; O15400-1; -. [O15400-1] DR Antibodypedia; 729; 196 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 AGR; HGNC:11442; -. 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; LMTYTKQ; -. DR OrthoDB; 200189at2759; -. DR PhylomeDB; O15400; -. DR TreeFam; TF315607; -. DR PathwayCommons; O15400; -. DR SignaLink; O15400; -. DR BioGRID-ORCS; 8417; 11 hits in 1158 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 209 other cell types or tissues. 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: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; cd15875; SNARE_syntaxin7; 1. DR CDD; cd00179; SynN; 1. DR Gene3D; 1.20.5.110; -; 1. DR Gene3D; 1.20.58.70; -; 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; SYNTAXIN; 1. DR PANTHER; PTHR19957:SF90; SYNTAXIN-7; 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; t-snare proteins; 1. DR PROSITE; PS00914; SYNTAXIN; 1. DR PROSITE; PS50192; T_SNARE; 1. DR Genevisible; O15400; HS. 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 //