STX4_RAT
ID STX4_RAT Reviewed; 298 AA.
AC Q08850; G3V8I4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Syntaxin-4;
GN Name=Stx4; Synonyms=Stx4a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=7690687; DOI=10.1016/0092-8674(93)90466-4;
RA Bennett M.K., Garcia-Arraras J.E., Elferink L.A., Peterson K.E.,
RA Fleming A.M., Hazuka C.D., Scheller R.H.;
RT "The syntaxin family of vesicular transport receptors.";
RL Cell 74:863-873(1993).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3] {ECO:0000312|EMBL:EDM17224.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH STXBP6.
RX PubMed=12145319; DOI=10.1074/jbc.m204929200;
RA Scales S.J., Hesser B.A., Masuda E.S., Scheller R.H.;
RT "Amisyn, a novel syntaxin-binding protein that may regulate SNARE complex
RT assembly.";
RL J. Biol. Chem. 277:28271-28279(2002).
RN [5]
RP SNARE COMPLEX CHARACTERIZATION.
RX PubMed=14993220; DOI=10.1074/jbc.m400798200;
RA Rao S.K., Huynh C., Proux-Gillardeaux V., Galli T., Andrews N.W.;
RT "Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal
RT exocytosis.";
RL J. Biol. Chem. 279:20471-20479(2004).
RN [6]
RP TISSUE SPECIFICITY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-35 AND SER-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SITE, AND MUTAGENESIS OF ILE-290.
RX PubMed=32963038; DOI=10.1194/jlr.ra120001087;
RA Kuge H., Miyamoto I., Yagyu K.I., Honke K.;
RT "PLRP2 selectively localizes synaptic membrane proteins via acyl-chain
RT remodeling of phospholipids.";
RL J. Lipid Res. 61:1747-1763(2020).
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 (PubMed:32963038). 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:0000269|PubMed:32963038}.
CC -!- SUBUNIT: Found in a complex with VAMP8 and SNAP23. Detected in a
CC complex with SNAP23 and STXBP4. Interacts with SNAP23 and SNAPIN.
CC Interacts with VAMP2. Interacts with LLGL1. Interacts (via C-terminus)
CC with CENPF. Interacts with DOC2B. Interacts with STXBP3; excludes
CC interaction with DOC2B and SNAP25. Interacts with STXBP4; excludes
CC interaction with VAMP2 (By similarity). Component of the SNARE complex
CC composed of STX4, SNAP23 and VAMP7 that interacts with SYT7 during
CC lysosomal exocytosis. Interacts with STXBP6. Interacts with STXBP5L (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12145319}.
CC -!- INTERACTION:
CC Q08850; P63045: Vamp2; NbExp=8; IntAct=EBI-918243, EBI-520880;
CC Q08850; O09044: Snap23; Xeno; NbExp=4; IntAct=EBI-918243, EBI-1812522;
CC Q08850; Q60770: Stxbp3; Xeno; NbExp=4; IntAct=EBI-918243, EBI-8430169;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32963038};
CC Single-pass type IV membrane protein {ECO:0000305}. Cell projection,
CC neuron projection {ECO:0000269|PubMed:32963038}. Note=Localizes to
CC neurite tips in neuronal cells. {ECO:0000269|PubMed:32963038}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested including adipose,
CC brain, testis, intestine, liver, heart, spleen, skeletal muscle and
CC kidney. {ECO:0000269|PubMed:18827011, ECO:0000269|PubMed:7690687}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; L20821; AAA03046.1; -; mRNA.
DR EMBL; AC111812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473956; EDM17224.1; -; Genomic_DNA.
DR EMBL; CH473956; EDM17226.1; -; Genomic_DNA.
DR PIR; E48213; E48213.
DR RefSeq; NP_112387.1; NM_031125.1.
DR AlphaFoldDB; Q08850; -.
DR SMR; Q08850; -.
DR BioGRID; 249661; 2.
DR CORUM; Q08850; -.
DR DIP; DIP-373N; -.
DR IntAct; Q08850; 12.
DR MINT; Q08850; -.
DR STRING; 10116.ENSRNOP00000026224; -.
DR iPTMnet; Q08850; -.
DR PhosphoSitePlus; Q08850; -.
DR PaxDb; Q08850; -.
DR GeneID; 81803; -.
DR KEGG; rno:81803; -.
DR UCSC; RGD:621019; rat.
DR CTD; 6810; -.
DR RGD; 621019; Stx4.
DR VEuPathDB; HostDB:ENSRNOG00000019302; -.
DR eggNOG; KOG0810; Eukaryota.
DR InParanoid; Q08850; -.
DR OMA; KVWIAIC; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; Q08850; -.
DR TreeFam; TF313763; -.
DR Reactome; R-RNO-114516; Disinhibition of SNARE formation.
DR Reactome; R-RNO-1236974; ER-Phagosome pathway.
DR Reactome; R-RNO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-RNO-449836; Other interleukin signaling.
DR PRO; PR:Q08850; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000019302; Expressed in ovary and 20 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; ISO:RGD.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043219; C:lateral loop; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0035749; C:myelin sheath adaxonal region; ISO:RGD.
DR GO; GO:0032589; C:neuron projection membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; ISO:RGD.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0036477; C:somatodendritic compartment; ISO:RGD.
DR GO; GO:0042581; C:specific granule; ISO:RGD.
DR GO; GO:0000322; C:storage vacuole; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0000149; F:SNARE binding; IPI:RGD.
DR GO; GO:0030507; F:spectrin binding; IPI:RGD.
DR GO; GO:0016230; F:sphingomyelin phosphodiesterase activator activity; ISO:RGD.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:1903575; P:cornified envelope assembly; ISO:RGD.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0046907; P:intracellular transport; NAS:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR GO; GO:0061025; P:membrane fusion; IDA:RGD.
DR GO; GO:0048284; P:organelle fusion; ISO:RGD.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:RGD.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISO:RGD.
DR GO; GO:0043311; P:positive regulation of eosinophil degranulation; ISO:RGD.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; ISO:RGD.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:RGD.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:RGD.
DR GO; GO:0016081; P:synaptic vesicle docking; IDA:RGD.
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; IDA:SynGO.
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 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_0000210204"
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:0000250"
FT COILED 38..163
FT /evidence="ECO:0000255"
FT SITE 290
FT /note="Required for neurite tip localization"
FT /evidence="ECO:0000269|PubMed:32963038"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70452"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:22673903"
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 MUTAGEN 290
FT /note="I->F: Mislocalization in neurons from neurite tips
FT to perinuclear region."
FT /evidence="ECO:0000269|PubMed:32963038"
FT CONFLICT 216
FT /note="S -> T (in Ref. 1; AAA03046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 34195 MW; E98547758FE6CEC6 CRC64;
MRDRTHELRQ GDNISDDEDE VRVALVVHSG AARLSSPDDE 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
