STXB1_BOVIN
ID STXB1_BOVIN Reviewed; 594 AA.
AC P61763; Q28208; Q62759; Q64320; Q96TG8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Syntaxin-binding protein 1;
DE AltName: Full=N-Sec1;
DE AltName: Full=Protein unc-18 homolog 1;
DE Short=Unc18-1;
DE AltName: Full=Protein unc-18 homolog A;
DE Short=Unc-18A;
DE AltName: Full=p67;
GN Name=STXBP1; Synonyms=UNC18A;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=8247129; DOI=10.1038/366347a0;
RA Hata Y., Slaughter C.A., Suedhof T.C.;
RT "Synaptic vesicle fusion complex contains unc-18 homologue bound to
RT syntaxin.";
RL Nature 366:347-351(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Adrenal medulla;
RA Wang G.-T., Gillis K.D.;
RT "Bovine chromaffin cell munc18-1 cDNA deduced amino acid sequence is
RT identical to that of rat munc18-1.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH CABP5, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=22039235; DOI=10.1167/iovs.11-8246;
RA Sokal I., Haeseleer F.;
RT "Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.";
RL Invest. Ophthalmol. Vis. Sci. 52:9131-9141(2011).
CC -!- FUNCTION: Participates in the regulation of synaptic vesicle docking
CC and fusion through interaction with GTP-binding proteins (By
CC similarity). Essential for neurotransmission and binds syntaxin, a
CC component of the synaptic vesicle fusion machinery probably in a 1:1
CC ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May
CC play a role in determining the specificity of intracellular fusion
CC reactions (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61765}.
CC -!- SUBUNIT: Interacts with SYTL4 (By similarity). Interacts with STX1A (By
CC similarity). Interacts with alpha-synuclein/SNCA; this interaction
CC controls SNCA self-replicating aggregation (By similarity). Interacts
CC with RAB3A; this interaction promotes RAB3A dissociation from the
CC vesicle membrane (By similarity). Interacts with CABP5
CC (PubMed:22039235). {ECO:0000250|UniProtKB:P61764,
CC ECO:0000250|UniProtKB:P61765, ECO:0000269|PubMed:22039235}.
CC -!- INTERACTION:
CC P61763; Q17QQ3: SNAP25; NbExp=3; IntAct=EBI-7335973, EBI-7336080;
CC P61763; P32850: STX1A; NbExp=3; IntAct=EBI-7335973, EBI-7336000;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P61764}. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC {ECO:0000269|PubMed:22039235}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
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DR EMBL; L26088; AAB41112.1; -; mRNA.
DR EMBL; AF153327; AAD37018.1; -; mRNA.
DR PIR; S39346; S39346.
DR RefSeq; NP_777044.1; NM_174619.3.
DR AlphaFoldDB; P61763; -.
DR SMR; P61763; -.
DR IntAct; P61763; 3.
DR MINT; P61763; -.
DR STRING; 9913.ENSBTAP00000050665; -.
DR iPTMnet; P61763; -.
DR PaxDb; P61763; -.
DR PRIDE; P61763; -.
DR Ensembl; ENSBTAT00000004589; ENSBTAP00000004589; ENSBTAG00000003525.
DR GeneID; 282378; -.
DR KEGG; bta:282378; -.
DR CTD; 6812; -.
DR VEuPathDB; HostDB:ENSBTAG00000003525; -.
DR VGNC; VGNC:35445; STXBP1.
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000155127; -.
DR HOGENOM; CLU_009210_2_0_1; -.
DR InParanoid; P61763; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000003525; Expressed in prefrontal cortex and 103 other tissues.
DR ExpressionAtlas; P61763; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:0007412; P:axon target recognition; ISS:AgBase.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; ISS:AgBase.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..594
FT /note="Syntaxin-binding protein 1"
FT /id="PRO_0000206276"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61765"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08599"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61765"
FT CONFLICT 291
FT /note="L -> V (in Ref. 1; AAB41112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 67569 MW; 2DD0715F875CE0F3 CRC64;
MAPIGLKAVV GEKIMHDVIK KVKKKGEWKV LVVDQLSMRM LSSCCKMTDI MTEGITIVED
INKRREPLPS LEAVYLITPS EKSVHSLISD FKDPPTAKYR AAHVFFTDSC PDALFNELVK
SRAAKVIKTL TEINIAFLPY ESQVYSLDSA DSFQSFYSPH KAQMKNPILE RLAEQIATLC
ATLKEYPAVR YRGEYKDNAL LAQLIQDKLD AYKADDPTMG EGPDKARSQL LILDRGFDPS
SPVLHELTFQ AMSYDLLPIE NDVYKYETSG IGEARVKEVL LDEDDDLWIA LRHKHIAEVS
QEVTRSLKDF SSSKRMNTGE KTTMRDLSQM LKKMPQYQKE LSKYSTHLHL AEDCMKHYQG
TVDKLCRVEQ DLAMGTDAEG EKIKDPMRAI VPILLDANVS TYDKIRIILL YIFLKNGITE
ENLNKLIQHA QIPPEDSEII TNMAHLGVPI VTDSTLRRRS KPERKERISE QTYQLSRWTP
IIKDIMEDTI EDKLDTKHYP YISTRSSASF STTAVSARYG HWHKNKAPGE YRSGPRLIIF
ILGGVSLNEM RCAYEVTQAN GKWEVLIGST HILTPQKLLD TLKKLNKTDE EISS