STX4_MOUSE
ID STX4_MOUSE Reviewed; 298 AA.
AC P70452; Q3TSL5; Q3UKQ8; Q80WT8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Syntaxin-4;
GN Name=Stx4; Synonyms=Stx4a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH STXB3, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Adipocyte;
RX PubMed=9045631; DOI=10.1074/jbc.272.10.6179;
RA Tellam J.T., Macaulay S.L., McIntosh S., Hewish D.R., Ward C.W.,
RA James D.E.;
RT "Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative
RT role in insulin-dependent movement of GLUT-4.";
RL J. Biol. Chem. 272:6179-6186(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [4]
RP FUNCTION, AND INTERACTION WITH STXBP4; SNAP23 AND VAMP2.
RX PubMed=10394363; DOI=10.1016/s1097-2765(01)80007-1;
RA Min J., Okada S., Kanzaki M., Elmendorf J.S., Coker K.J., Ceresa B.P.,
RA Syu L.-J., Noda Y., Saltiel A.R., Pessin J.E.;
RT "Synip: a novel insulin-regulated syntaxin 4-binding protein mediating
RT GLUT4 translocation in adipocytes.";
RL Mol. Cell 3:751-760(1999).
RN [5]
RP INTERACTION WITH SNAP23 AND SNAPIN.
RX PubMed=12877659; DOI=10.1042/bj20030427;
RA Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I., Manickam E.,
RA Rowe T.;
RT "Identification and characterization of Snapin as a ubiquitously expressed
RT SNARE-binding protein that interacts with SNAP23 in non-neuronal cells.";
RL Biochem. J. 375:433-440(2003).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND SNAP23.
RX PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.;
RT "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar
RT cells.";
RL Dev. Cell 7:359-371(2004).
RN [7]
RP INTERACTION WITH LLGL1.
RX PubMed=11809830; DOI=10.1091/mbc.01-10-0496;
RA Musch A., Cohen D., Yeaman C., Nelson W.J., Rodriguez-Boulan E.,
RA Brennwald P.J.;
RT "Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae
RT interacts with basolateral exocytic machinery in Madin-Darby canine kidney
RT cells.";
RL Mol. Biol. Cell 13:158-168(2002).
RN [8]
RP INTERACTION WITH STXBP3 AND VAMP2.
RX PubMed=17548353; DOI=10.1074/jbc.m701661200;
RA Ke B., Oh E., Thurmond D.C.;
RT "Doc2beta is a novel Munc18c-interacting partner and positive effector of
RT syntaxin 4-mediated exocytosis.";
RL J. Biol. Chem. 282:21786-21797(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [10]
RP FUNCTION, INTERACTION WITH CENPF, AND SUBCELLULAR LOCATION.
RX PubMed=18827011; DOI=10.1242/jcs.032847;
RA Pooley R.D., Moynihan K.L., Soukoulis V., Reddy S., Francis R., Lo C.,
RA Ma L.-J., Bader D.M.;
RT "Murine CENPF interacts with syntaxin 4 in the regulation of vesicular
RT transport.";
RL J. Cell Sci. 121:3413-3421(2008).
RN [11]
RP INTERACTION WITH DOC2B.
RX PubMed=19033398; DOI=10.2337/db08-0303;
RA Fukuda N., Emoto M., Nakamori Y., Taguchi A., Miyamoto S., Uraki S.,
RA Oka Y., Tanizawa Y.;
RT "DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated
RT GLUT4 vesicle fusion in adipocytes.";
RL Diabetes 58:377-384(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-29 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-117 AND SER-208, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP INTERACTION WITH STXBP5L.
RX PubMed=21998599; DOI=10.1371/journal.pgen.1002323;
RA Bhatnagar S., Oler A.T., Rabaglia M.E., Stapleton D.S., Schueler K.L.,
RA Truchan N.A., Worzella S.L., Stoehr J.P., Clee S.M., Yandell B.S.,
RA Keller M.P., Thurmond D.C., Attie A.D.;
RT "Positional cloning of a type 2 diabetes quantitative trait locus; tomosyn-
RT 2, a negative regulator of insulin secretion.";
RL PLoS Genet. 7:E1002323-E1002323(2011).
CC -!- FUNCTION: Plasma membrane t-SNARE that mediates docking of transport
CC vesicles. Necessary for the translocation of SLC2A4 from intracellular
CC vesicles to the plasma membrane. In neurons, recruited at neurite tips
CC to membrane domains rich in the phospholipid 1-oleoyl-2-palmitoyl-PC
CC (OPPC) which promotes neurite tip surface expression of the dopamine
CC transporter SLC6A3/DAT by facilitating fusion of SLC6A3-containing
CC transport vesicles with the plasma membrane (By similarity). Together
CC with STXB3 and VAMP2, may also play a role in docking/fusion of
CC intracellular GLUT4-containing vesicles with the cell surface in
CC adipocytes and in docking of synaptic vesicles at presynaptic active
CC zones. {ECO:0000250|UniProtKB:Q08850, ECO:0000269|PubMed:10394363,
CC ECO:0000269|PubMed:18827011, ECO:0000269|PubMed:9045631}.
CC -!- SUBUNIT: Interacts with STXBP6. Component of the SNARE complex composed
CC of STX4, SNAP23 and VAMP7 that interacts with SYT7 during lysosomal
CC exocytosis (By similarity). Found in a complex with VAMP8 and SNAP23.
CC Detected in a complex with SNAP23 and STXBP4. Interacts with VAMP2.
CC Interacts with SNAP23 and SNAPIN. Interacts with LLGL1. Interacts (via
CC C-terminus) with CENPF. Interacts with DOC2B. Interacts with STXBP3;
CC excludes interaction with DOC2B and SNAP25. Interacts with STXBP4;
CC excludes interaction with VAMP2. Interacts with STXBP5L. {ECO:0000250,
CC ECO:0000269|PubMed:10394363, ECO:0000269|PubMed:11809830,
CC ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:15363411,
CC ECO:0000269|PubMed:17548353, ECO:0000269|PubMed:18827011,
CC ECO:0000269|PubMed:19033398, ECO:0000269|PubMed:21998599,
CC ECO:0000269|PubMed:9045631}.
CC -!- INTERACTION:
CC P70452; Q155P7: Cenpf; NbExp=9; IntAct=EBI-645716, EBI-2211248;
CC P70452; Q60770-1: Stxbp3; NbExp=3; IntAct=EBI-645716, EBI-15639434;
CC P70452; P61765: Stxbp1; Xeno; NbExp=2; IntAct=EBI-645716, EBI-1029097;
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 -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; U76832; AAB18991.1; -; mRNA.
DR EMBL; AK145909; BAE26743.1; -; mRNA.
DR EMBL; AK161971; BAE36660.1; -; mRNA.
DR EMBL; BC005791; AAH05791.1; -; mRNA.
DR EMBL; BC011491; AAH11491.1; -; mRNA.
DR EMBL; BC052023; AAH52023.1; -; mRNA.
DR CCDS; CCDS21880.1; -.
DR RefSeq; NP_033320.1; NM_009294.3.
DR PDB; 3PUJ; X-ray; 3.31 A; C/D=1-10.
DR PDB; 3PUK; X-ray; 3.05 A; C/D=1-10.
DR PDBsum; 3PUJ; -.
DR PDBsum; 3PUK; -.
DR AlphaFoldDB; P70452; -.
DR SMR; P70452; -.
DR BioGRID; 203563; 13.
DR CORUM; P70452; -.
DR DIP; DIP-41399N; -.
DR IntAct; P70452; 7.
DR MINT; P70452; -.
DR STRING; 10090.ENSMUSP00000033075; -.
DR iPTMnet; P70452; -.
DR PhosphoSitePlus; P70452; -.
DR SwissPalm; P70452; -.
DR EPD; P70452; -.
DR jPOST; P70452; -.
DR MaxQB; P70452; -.
DR PaxDb; P70452; -.
DR PeptideAtlas; P70452; -.
DR PRIDE; P70452; -.
DR ProteomicsDB; 257472; -.
DR Antibodypedia; 732; 286 antibodies from 32 providers.
DR DNASU; 20909; -.
DR Ensembl; ENSMUST00000033075; ENSMUSP00000033075; ENSMUSG00000030805.
DR Ensembl; ENSMUST00000121705; ENSMUSP00000112927; ENSMUSG00000030805.
DR GeneID; 20909; -.
DR KEGG; mmu:20909; -.
DR UCSC; uc009jwy.1; mouse.
DR CTD; 20909; -.
DR MGI; MGI:893577; Stx4a.
DR VEuPathDB; HostDB:ENSMUSG00000030805; -.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_1_1; -.
DR InParanoid; P70452; -.
DR OMA; KVWIAIC; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; P70452; -.
DR TreeFam; TF313763; -.
DR Reactome; R-MMU-114516; Disinhibition of SNARE formation.
DR Reactome; R-MMU-1236974; ER-Phagosome pathway.
DR Reactome; R-MMU-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-MMU-449836; Other interleukin signaling.
DR BioGRID-ORCS; 20909; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Stx4a; mouse.
DR EvolutionaryTrace; P70452; -.
DR PRO; PR:P70452; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P70452; protein.
DR Bgee; ENSMUSG00000030805; Expressed in ileal epithelium and 266 other tissues.
DR ExpressionAtlas; P70452; baseline and differential.
DR Genevisible; P70452; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0043219; C:lateral loop; IDA:BHF-UCL.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0035749; C:myelin sheath adaxonal region; IDA:BHF-UCL.
DR GO; GO:0032589; C:neuron projection membrane; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:MGI.
DR GO; GO:0042581; C:specific granule; ISO:MGI.
DR GO; GO:0000322; C:storage vacuole; IDA:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0016230; F:sphingomyelin phosphodiesterase activator activity; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI.
DR GO; GO:1903575; P:cornified envelope assembly; ISO:MGI.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0061025; P:membrane fusion; ISO:MGI.
DR GO; GO:0048284; P:organelle fusion; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:MGI.
DR GO; GO:0043311; P:positive regulation of eosinophil degranulation; ISO:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:MGI.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0034394; P:protein localization to cell surface; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:BHF-UCL.
DR GO; GO:0016081; P:synaptic vesicle docking; ISO:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; TAS:MGI.
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 GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
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 3D-structure; Cell membrane; Cell projection; Coiled coil; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..298
FT /note="Syntaxin-4"
FT /id="PRO_0000210203"
FT TOPO_DOM 1..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..298
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 154..298
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000269|PubMed:18827011"
FT COILED 38..163
FT /evidence="ECO:0000255"
FT SITE 290
FT /note="Required for neurite tip localization"
FT /evidence="ECO:0000250|UniProtKB:Q08850"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12846"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 47
FT /note="T -> I (in Ref. 3; AAH52023)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="C -> Y (in Ref. 2; BAE36660)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="S -> Y (in Ref. 2; BAE26743)"
FT /evidence="ECO:0000305"
FT HELIX 5..8
FT /evidence="ECO:0007829|PDB:3PUK"
SQ SEQUENCE 298 AA; 34165 MW; FCD1477E1126CEC1 CRC64;
MRDRTHELRQ GDNISDDEDE VRVALVVHSG AARLGSPDDE FFQKVQTIRQ TMAKLESKVR
ELEKQQVTIL ATPLPEESMK QGLQNLREEI KQLGREVRAQ LKAIEPQKEE ADENYNSVNT
RMKKTQHGVL SQQFVELINK CNSMQSEYRE KNVERIRRQL KITNAGMVSD EELEQMLDSG
QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HEIFTFLATE VEMQGEMINR
IEKNILSSAD YVERGQEHVK IALENQKKAR KKKVMIAICV SVTVLILAVI IGITITVG
