STX4_HUMAN
ID STX4_HUMAN Reviewed; 297 AA.
AC Q12846; A8MXY0; Q15525; Q6FHE8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Syntaxin-4;
DE AltName: Full=Renal carcinoma antigen NY-REN-31;
GN Name=STX4; Synonyms=STX4A;
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=Placenta;
RX PubMed=8206394; DOI=10.1016/0378-1119(94)90117-1;
RA Li H., Hodge D.R., Pei G.K., Seth A.;
RT "Isolation and sequence analysis of the human syntaxin-encoding gene.";
RL Gene 143:303-304(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=8760387; DOI=10.1042/bj3170945;
RA Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H.,
RA Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J.,
RA Ward C.W.;
RT "Insulin-responsive tissues contain the core complex protein SNAP-25
RT (synaptosomal-associated protein 25) A and B isoforms in addition to
RT syntaxin 4 and synaptobrevins 1 and 2.";
RL Biochem. J. 317:945-954(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood neutrophil;
RX PubMed=10080545; DOI=10.1002/jlb.65.3.397;
RA Martin-Martin B., Nabokina S.M., Lazo P.A., Mollinedo F.;
RT "Co-expression of several human syntaxin genes in neutrophils and
RT differentiating HL-60 cells: variant isoforms and detection of syntaxin
RT 1.";
RL J. Leukoc. Biol. 65:397-406(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zhang Z., Loh E., Low S.H., Li X., Miura M., An F., Weimbs T.;
RT "Expression of syntaxins in kidney MDCK cells.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [10]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [12]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-15 AND SER-117, AND
RP IDENTIFICATION BY 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-15, AND
RP IDENTIFICATION BY 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; SER-36 AND SER-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-15, AND
RP IDENTIFICATION BY 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 [19]
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).
CC -!- FUNCTION: Plasma membrane t-SNARE that mediates docking of transport
CC vesicles (By similarity). Necessary for the translocation of SLC2A4
CC from intracellular vesicles to the plasma membrane (By similarity). In
CC neurons, recruited at neurite tips to membrane domains rich in the
CC phospholipid 1-oleoyl-2-palmitoyl-PC (OPPC) which promotes neurite tip
CC surface expression of the dopamine transporter SLC6A3/DAT by
CC facilitating fusion of SLC6A3-containing transport vesicles with the
CC plasma membrane (By similarity). Together with STXB3 and VAMP2, may
CC also play a role in docking/fusion of intracellular GLUT4-containing
CC vesicles with the cell surface in adipocytes and in docking of synaptic
CC vesicles at presynaptic active zones (By similarity).
CC {ECO:0000250|UniProtKB:P70452, ECO:0000250|UniProtKB:Q08850}.
CC -!- SUBUNIT: Component of the SNARE complex composed of STX4, SNAP23 and
CC VAMP7 that interacts with SYT7 during lysosomal exocytosis. Found in a
CC complex with VAMP8 and SNAP23. Detected in a complex with SNAP23 and
CC STXBP4. Interacts with VAMP2. Interacts with SNAP23 and SNAPIN.
CC Interacts with LLGL1. Interacts (via C-terminus) with CENPF. Interacts
CC with DOC2B. Interacts with STXBP6. Interacts with STXBP3; excludes
CC interaction with DOC2B and SNAP25. Interacts with STXBP4; excludes
CC interaction with VAMP2 (By similarity). Interacts with STXBP5L (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q12846; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-744942, EBI-11096309;
CC Q12846; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-744942, EBI-12109402;
CC Q12846; O15155: BET1; NbExp=6; IntAct=EBI-744942, EBI-749204;
CC Q12846; Q53TN4: CYBRD1; NbExp=7; IntAct=EBI-744942, EBI-8637742;
CC Q12846; P50402: EMD; NbExp=3; IntAct=EBI-744942, EBI-489887;
CC Q12846; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-744942, EBI-12142299;
CC Q12846; Q96F15: GIMAP5; NbExp=3; IntAct=EBI-744942, EBI-6166686;
CC Q12846; O14653: GOSR2; NbExp=6; IntAct=EBI-744942, EBI-4401517;
CC Q12846; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-744942, EBI-13345167;
CC Q12846; P54920: NAPA; NbExp=3; IntAct=EBI-744942, EBI-749652;
CC Q12846; Q9H115: NAPB; NbExp=6; IntAct=EBI-744942, EBI-3921185;
CC Q12846; P60201-2: PLP1; NbExp=3; IntAct=EBI-744942, EBI-12188331;
CC Q12846; P25788: PSMA3; NbExp=3; IntAct=EBI-744942, EBI-348380;
CC Q12846; P78317: RNF4; NbExp=3; IntAct=EBI-744942, EBI-2340927;
CC Q12846; Q96IW7: SEC22A; NbExp=6; IntAct=EBI-744942, EBI-8652744;
CC Q12846; O75396: SEC22B; NbExp=4; IntAct=EBI-744942, EBI-1058865;
CC Q12846; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-744942, EBI-10329948;
CC Q12846; O95470: SGPL1; NbExp=3; IntAct=EBI-744942, EBI-1046170;
CC Q12846; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-744942, EBI-10244848;
CC Q12846; O60499-2: STX10; NbExp=3; IntAct=EBI-744942, EBI-12094584;
CC Q12846; O75558: STX11; NbExp=3; IntAct=EBI-744942, EBI-714135;
CC Q12846; Q86Y82: STX12; NbExp=8; IntAct=EBI-744942, EBI-2691717;
CC Q12846; O14662: STX16; NbExp=3; IntAct=EBI-744942, EBI-2853548;
CC Q12846; O14662-5: STX16; NbExp=3; IntAct=EBI-744942, EBI-9089968;
CC Q12846; Q16623: STX1A; NbExp=3; IntAct=EBI-744942, EBI-712466;
CC Q12846; P61266: STX1B; NbExp=3; IntAct=EBI-744942, EBI-9071709;
CC Q12846; P32856-2: STX2; NbExp=4; IntAct=EBI-744942, EBI-11956649;
CC Q12846; Q13277: STX3; NbExp=8; IntAct=EBI-744942, EBI-1394295;
CC Q12846; Q13190: STX5; NbExp=6; IntAct=EBI-744942, EBI-714206;
CC Q12846; O43752: STX6; NbExp=8; IntAct=EBI-744942, EBI-2695795;
CC Q12846; O15400: STX7; NbExp=7; IntAct=EBI-744942, EBI-3221827;
CC Q12846; Q9UNK0: STX8; NbExp=6; IntAct=EBI-744942, EBI-727240;
CC Q12846; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-744942, EBI-11955057;
CC Q12846; Q8N511: TMEM199; NbExp=3; IntAct=EBI-744942, EBI-10265825;
CC Q12846; Q969S6: TMEM203; NbExp=3; IntAct=EBI-744942, EBI-12274070;
CC Q12846; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-744942, EBI-765817;
CC Q12846; Q9NZ43: USE1; NbExp=3; IntAct=EBI-744942, EBI-742842;
CC Q12846; P23763: VAMP1; NbExp=3; IntAct=EBI-744942, EBI-10201335;
CC Q12846; P23763-3: VAMP1; NbExp=3; IntAct=EBI-744942, EBI-12097582;
CC Q12846; P63027: VAMP2; NbExp=6; IntAct=EBI-744942, EBI-520113;
CC Q12846; Q15836: VAMP3; NbExp=9; IntAct=EBI-744942, EBI-722343;
CC Q12846; O75379: VAMP4; NbExp=7; IntAct=EBI-744942, EBI-744953;
CC Q12846; O75379-2: VAMP4; NbExp=4; IntAct=EBI-744942, EBI-10187996;
CC Q12846; O95183: VAMP5; NbExp=7; IntAct=EBI-744942, EBI-10191195;
CC Q12846; Q9UEU0: VTI1B; NbExp=6; IntAct=EBI-744942, EBI-723716;
CC Q12846; O95159: ZFPL1; NbExp=3; IntAct=EBI-744942, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q08850};
CC Single-pass type IV membrane protein {ECO:0000305}. Cell projection,
CC neuron projection {ECO:0000250|UniProtKB:Q08850}. Note=Localizes to
CC neurite tips in neuronal cells. {ECO:0000250|UniProtKB:Q08850}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12846-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12846-2; Sequence=VSP_054603;
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils and neutrophil-
CC differentiated HL-60 cells. Expression in neutrophils increases with
CC differentiation. {ECO:0000269|PubMed:10080545}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U07158; AAA20967.1; -; mRNA.
DR EMBL; X85784; CAA59769.1; -; mRNA.
DR EMBL; AJ000541; CAA04174.1; -; mRNA.
DR EMBL; AF026007; AAB88810.1; -; mRNA.
DR EMBL; AF318489; AAG40313.1; -; Transcribed_RNA.
DR EMBL; BT007326; AAP35990.1; -; mRNA.
DR EMBL; AK091833; BAG52424.1; -; mRNA.
DR EMBL; AK315716; BAG38075.1; -; mRNA.
DR EMBL; CR541806; CAG46605.1; -; mRNA.
DR EMBL; AC135050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471192; EAW52176.1; -; Genomic_DNA.
DR EMBL; CH471192; EAW52177.1; -; Genomic_DNA.
DR EMBL; BC002436; AAH02436.1; -; mRNA.
DR CCDS; CCDS10700.1; -. [Q12846-1]
DR CCDS; CCDS61916.1; -. [Q12846-2]
DR PIR; I38517; I38517.
DR PIR; S52726; S52726.
DR RefSeq; NP_001259025.1; NM_001272096.1. [Q12846-2]
DR RefSeq; NP_004595.2; NM_004604.4. [Q12846-1]
DR AlphaFoldDB; Q12846; -.
DR SMR; Q12846; -.
DR BioGRID; 112679; 419.
DR CORUM; Q12846; -.
DR IntAct; Q12846; 80.
DR MINT; Q12846; -.
DR STRING; 9606.ENSP00000317714; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR TCDB; 8.A.91.1.12; the syntaxin (syntaxin) family.
DR GlyGen; Q12846; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12846; -.
DR PhosphoSitePlus; Q12846; -.
DR SwissPalm; Q12846; -.
DR BioMuta; STX4; -.
DR DMDM; 3041737; -.
DR OGP; Q12846; -.
DR EPD; Q12846; -.
DR jPOST; Q12846; -.
DR MassIVE; Q12846; -.
DR MaxQB; Q12846; -.
DR PaxDb; Q12846; -.
DR PeptideAtlas; Q12846; -.
DR PRIDE; Q12846; -.
DR ProteomicsDB; 2361; -.
DR ProteomicsDB; 58981; -. [Q12846-1]
DR Antibodypedia; 732; 286 antibodies from 32 providers.
DR DNASU; 6810; -.
DR Ensembl; ENST00000313843.8; ENSP00000317714.3; ENSG00000103496.15. [Q12846-1]
DR Ensembl; ENST00000394998.5; ENSP00000378447.1; ENSG00000103496.15. [Q12846-2]
DR GeneID; 6810; -.
DR KEGG; hsa:6810; -.
DR MANE-Select; ENST00000313843.8; ENSP00000317714.3; NM_004604.5; NP_004595.2.
DR UCSC; uc002eak.5; human. [Q12846-1]
DR CTD; 6810; -.
DR DisGeNET; 6810; -.
DR GeneCards; STX4; -.
DR HGNC; HGNC:11439; STX4.
DR HPA; ENSG00000103496; Low tissue specificity.
DR MIM; 186591; gene.
DR neXtProt; NX_Q12846; -.
DR OpenTargets; ENSG00000103496; -.
DR PharmGKB; PA36236; -.
DR VEuPathDB; HostDB:ENSG00000103496; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; Q12846; -.
DR OMA; KVWIAIC; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; Q12846; -.
DR TreeFam; TF313763; -.
DR PathwayCommons; Q12846; -.
DR Reactome; R-HSA-114516; Disinhibition of SNARE formation.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR SignaLink; Q12846; -.
DR SIGNOR; Q12846; -.
DR BioGRID-ORCS; 6810; 218 hits in 1081 CRISPR screens.
DR ChiTaRS; STX4; human.
DR GeneWiki; STX4; -.
DR GenomeRNAi; 6810; -.
DR Pharos; Q12846; Tbio.
DR PRO; PR:Q12846; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q12846; protein.
DR Bgee; ENSG00000103496; Expressed in C1 segment of cervical spinal cord and 193 other tissues.
DR ExpressionAtlas; Q12846; baseline and differential.
DR Genevisible; Q12846; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; 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:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0043219; C:lateral loop; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
DR GO; GO:0032589; C:neuron projection membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0000322; C:storage vacuole; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:0005773; C:vacuole; TAS:HGNC-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0016230; F:sphingomyelin phosphodiesterase activator activity; IMP:UniProtKB.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
DR GO; GO:1903575; P:cornified envelope assembly; IDA:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060291; P:long-term synaptic potentiation; IDA:UniProtKB.
DR GO; GO:0048284; P:organelle fusion; IDA:UniProtKB.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:UniProtKB.
DR GO; GO:0043311; P:positive regulation of eosinophil degranulation; IMP:UniProtKB.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:UniProtKB.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR GO; GO:0035493; P:SNARE complex assembly; IEA:Ensembl.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
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; PF00804; Syntaxin; 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 Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW Membrane; Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..297
FT /note="Syntaxin-4"
FT /id="PRO_0000210202"
FT TOPO_DOM 1..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 200..262
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..297
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT COILED 43..163
FT /evidence="ECO:0000255"
FT SITE 290
FT /note="Required for neurite tip localization"
FT /evidence="ECO:0000250|UniProtKB:Q08850"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 31
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70452"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70452"
FT VAR_SEQ 1..44
FT /note="MRDRTHELRQGDDSSDEEDKERVALVVHPGTARLGSPDEEFFHK -> MGMT
FT ARTKRTRSGSRWWCTRARHGWGARTRSSSTSPLGHPPQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054603"
FT CONFLICT 174
FT /note="E -> D (in Ref. 1; AAA20967)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="A -> V (in Ref. 1; AAA20967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 34180 MW; 5084FD1C49A86BAA CRC64;
MRDRTHELRQ GDDSSDEEDK ERVALVVHPG TARLGSPDEE FFHKVRTIRQ TIVKLGNKVQ
ELEKQQVTIL ATPLPEESMK QELQNLRDEI KQLGREIRLQ LKAIEPQKEE ADENYNSVNT
RMRKTQHGVL SQQFVELINK CNSMQSEYRE KNVERIRRQL KITNAGMVSD EELEQMLDSG
QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HDIFTFLATE VEMQGEMINR
IEKNILSSAD YVERGQEHVK TALENQKKAR KKKVLIAICV SITVVLLAVI IGVTVVG
