STX1A_BOVIN
ID STX1A_BOVIN Reviewed; 288 AA.
AC P32850;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Syntaxin-1A;
DE AltName: Full=Neuron-specific antigen HPC-1;
DE AltName: Full=Synaptotagmin-associated 35 kDa protein;
DE Short=P35A;
GN Name=STX1A;
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].
RC TISSUE=Brain;
RX PubMed=1530610; DOI=10.1016/0006-291x(92)91316-i;
RA Inoue A., Akagawa K.;
RT "Neuron-specific antigen HPC-1 from bovine brain reveals strong homology to
RT epimorphin, an essential factor involved in epithelial morphogenesis:
RT identification of a novel protein family.";
RL Biochem. Biophys. Res. Commun. 187:1144-1150(1992).
RN [2]
RP PROTEIN SEQUENCE OF 29-40; 43-55; 97-106; 160-166 AND 213-224.
RX PubMed=8455717; DOI=10.1038/362318a0;
RA Soellner T., Whiteheart S.W., Brunner M., Erdjument-Bromage H.,
RA Geromanos S., Tempst P., Rothman J.E.;
RT "SNAP receptors implicated in vesicle targeting and fusion.";
RL Nature 362:318-324(1993).
RN [3]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM NEUROTOXIN TYPE
RP C.
RC TISSUE=Chromaffin cell;
RX PubMed=8611567; DOI=10.1021/bi9519009;
RA Foran P., Lawrence G.W., Shone C.C., Foster K.A., Dolly J.O.;
RT "Botulinum neurotoxin C1 cleaves both syntaxin and SNAP-25 in intact and
RT permeabilized chromaffin cells: correlation with its blockade of
RT catecholamine release.";
RL Biochemistry 35:2630-2636(1996).
CC -!- FUNCTION: Plays an essential role in hormone and neurotransmitter
CC calcium-dependent exocytosis and endocytosis. Part of the SNARE
CC (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and
CC VAMP2 which mediates the fusion of synaptic vesicles with the
CC presynaptic plasma membrane. STX1A and SNAP25 are localized on the
CC plasma membrane while VAMP2 resides in synaptic vesicles. The pairing
CC of the three SNAREs from the N-terminal SNARE motifs to the C-terminal
CC anchors leads to the formation of the SNARE complex, which brings
CC membranes into close proximity and results in final fusion (By
CC similarity). Participates in the calcium-dependent regulation of
CC acrosomal exocytosis in sperm. Also plays an important role in the
CC exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-
CC 1) (By similarity). {ECO:0000250|UniProtKB:O35526,
CC ECO:0000250|UniProtKB:P32851}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A; this complex constitutes the basic catalytic machinery of the
CC complex neurotransmitter release apparatus. The SNARE complex interacts
CC with CPLX1. Interacts with STXBP1. Interacts (via C-terminus) with
CC KCNB1 (via C-terminus); the interaction increases in a calcium-
CC dependent manner and induces a pore-independent enhancement of
CC exocytosis in neuroendocrine cells, chromaffin cells, pancreatic beta
CC cells and from the soma of dorsal root ganglia (DRG) neurons (By
CC similarity). Interacts with SYTL4 (By similarity). Interacts with
CC STXBP6. Interacts with PLCL1 (via C2 domain) (By similarity). Interacts
CC with OTOF. Interacts with LGI3 (By similarity). Interacts with SLC6A4
CC (By similarity). Interacts with SYT6 and SYT8; the interaction is
CC Ca(2+)-dependent (By similarity). Interacts with VAMP8. Interacts with
CC SNAP23 (By similarity). Interacts with VAPA and SYBU (By similarity).
CC Interacts with PRRT2 (By similarity). Interacts with SEPT8 (By
CC similarity). Interacts with STXBP5L (By similarity). Interacts with
CC synaptotagmin-1/SYT1 (By similarity). Interacts with SEPTIN5; in the
CC cerebellar cortex (By similarity). Interacts with SEPTIN4; in the
CC striatum (By similarity). {ECO:0000250|UniProtKB:O35526,
CC ECO:0000250|UniProtKB:P32851, ECO:0000250|UniProtKB:Q16623}.
CC -!- INTERACTION:
CC P32850; P61763: STXBP1; NbExp=3; IntAct=EBI-7336000, EBI-7335973;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:O35526}; Single-pass type IV
CC membrane protein {ECO:0000250|UniProtKB:O35526}. Synapse, synaptosome
CC {ECO:0000250|UniProtKB:O35526}. Cell membrane
CC {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell
CC membrane. {ECO:0000250|UniProtKB:P32851}.
CC -!- PTM: Phosphorylated by CK2. Phosphorylation at Ser-188 by DAPK1
CC significantly decreases its interaction with STXBP1 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Sumoylated, sumoylation is required for regulation of synaptic
CC vesicle endocytosis. {ECO:0000250|UniProtKB:Q16623}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type C (BoNT/C) which inhibits neurotransmitter release
CC (PubMed:8611567). Probably hydrolyzes the 253-Lys-|-Ala-254 bond.
CC {ECO:0000305|PubMed:8611567}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR PIR; JQ1615; JQ1615.
DR RefSeq; XP_005225301.1; XM_005225244.2.
DR AlphaFoldDB; P32850; -.
DR BMRB; P32850; -.
DR SMR; P32850; -.
DR CORUM; P32850; -.
DR IntAct; P32850; 2.
DR MINT; P32850; -.
DR PRIDE; P32850; -.
DR Ensembl; ENSBTAT00000084274; ENSBTAP00000064870; ENSBTAG00000017075.
DR GeneID; 788566; -.
DR CTD; 6804; -.
DR VEuPathDB; HostDB:ENSBTAG00000017075; -.
DR VGNC; VGNC:35436; STX1A.
DR GeneTree; ENSGT01030000234627; -.
DR InParanoid; P32850; -.
DR OMA; RWICFIL; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000017075; Expressed in Ammon's horn and 104 other tissues.
DR ExpressionAtlas; P32850; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
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:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; ISS:UniProtKB.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB.
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; IPR028669; STX1.
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 PANTHER; PTHR19957:SF84; PTHR19957:SF84; 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; Coiled coil; Cytoplasmic vesicle; Direct protein sequencing;
KW Exocytosis; Isopeptide bond; Membrane; Neurotransmitter transport;
KW Phosphoprotein; Reference proteome; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation.
FT CHAIN 1..288
FT /note="Syntaxin-1A"
FT /id="PRO_0000210185"
FT TOPO_DOM 1..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..288
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 192..254
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..109
FT /evidence="ECO:0000255"
FT SITE 253..254
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type C (BoNT/C)"
FT /evidence="ECO:0000305|PubMed:8611567"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35526"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32851"
FT MOD_RES 188
FT /note="Phosphoserine; by DAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:Q16623"
SQ SEQUENCE 288 AA; 33091 MW; 97ED781DE0EBB409 CRC64;
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKISEN VEEVKRKHSA
ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH
STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG
IIMDSSISKQ ALSEIETRHS EIIKLENSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHS
VDYVERAVSD TKKAVKYQSK ARRKKIMIVI CCVVLGIVIA STFGGIFG
