ID   STX4_BOVIN              Reviewed;         297 AA.
AC   Q3SWZ3;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-NOV-2023, entry version 117.
DE   RecName: Full=Syntaxin-4;
GN   Name=STX4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC104588; AAI04589.1; -; mRNA.
DR   RefSeq; NP_001030236.1; NM_001035064.1.
DR   AlphaFoldDB; Q3SWZ3; -.
DR   SMR; Q3SWZ3; -.
DR   STRING; 9913.ENSBTAP00000009899; -.
DR   PaxDb; 9913-ENSBTAP00000009899; -.
DR   GeneID; 508675; -.
DR   KEGG; bta:508675; -.
DR   CTD; 6810; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   HOGENOM; CLU_042423_2_1_1; -.
DR   InParanoid; Q3SWZ3; -.
DR   OrthoDB; 2876074at2759; -.
DR   TreeFam; TF313763; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005901; C:caveola; IDA:AgBase.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0032589; C:neuron projection membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0034394; P:protein localization to cell surface; ISS: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   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:SF97; SYNTAXIN-4; 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; t-snare proteins; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Coiled coil; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..297
FT                   /note="Syntaxin-4"
FT                   /id="PRO_0000282875"
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   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:0000250|UniProtKB:Q12846"
FT   MOD_RES         15
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12846"
FT   MOD_RES         31
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12846"
FT   MOD_RES         36
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12846"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12846"
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"
SQ   SEQUENCE   297 AA;  34400 MW;  5CAE09860DD5C422 CRC64;
     MRDRTHELRQ GDDSSDDEDK ERVALVVHPG TARLGSPDDE FFQKVRTIRQ TIVKLENKVR
     ELEKQQVTIL ATPLPEESMK QDLQNLRDEI KQLGRDIRAQ LKAIEPQKEE ADENYNSVNT
     RMRKTQHGVL SQQFVELINK CNLMQSEYRE KNVERIRRQL KITNAGMVSD KELEQMLDSG
     QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HEIFTFLATE VEMQGEMINR
     IEKNILSSAD YVERGQEHVK VALENQKKAR KKKVFIAICL SITVLILVVI IVISTLV
//