STX1B_BOVIN
ID STX1B_BOVIN Reviewed; 288 AA.
AC P61267; A6QR58; P41414;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Syntaxin-1B;
DE AltName: Full=Synaptocanalin I;
DE AltName: Full=Syntaxin-1B2;
GN Name=STX1B; Synonyms=STX1B2;
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;
RA Morita T., Mori H., Sakimura K., Mishina M., Sekine Y., Tsugita A.,
RA Odani S., Horikawa H.P., Saisu H., Abe T.;
RT "Synaptocanalin I, a protein associated with brain omega-conotoxin-
RT sensitive calcium channels.";
RL Biomed. Res. 13:357-364(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 46-81; 125-137 AND 158-181.
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 [4]
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: Potentially involved in docking of synaptic vesicles at
CC presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis
CC acrosomal reaction in sperm (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the
CC interaction is Ca(2+)-dependent (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}.
CC -!- PTM: Phosphorylated by CK2. {ECO:0000250}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type C (BoNT/C); cleavage by BoNT/C inhibits
CC neurotransmitter release (PubMed:8611567). Probably hydrolyzes the 252-
CC Lys-|-Ala-253 bond. {ECO:0000305|PubMed:8611567}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; D14133; BAA03188.1; -; mRNA.
DR EMBL; BC150124; AAI50125.1; -; mRNA.
DR PIR; JU0136; JU0136.
DR RefSeq; NP_777043.1; NM_174618.2.
DR AlphaFoldDB; P61267; -.
DR SMR; P61267; -.
DR CORUM; P61267; -.
DR STRING; 9913.ENSBTAP00000022704; -.
DR PaxDb; P61267; -.
DR PRIDE; P61267; -.
DR Ensembl; ENSBTAT00000022704; ENSBTAP00000022704; ENSBTAG00000002349.
DR GeneID; 282377; -.
DR KEGG; bta:282377; -.
DR CTD; 112755; -.
DR VEuPathDB; HostDB:ENSBTAG00000002349; -.
DR VGNC; VGNC:35437; STX1B.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; P61267; -.
DR OMA; ARRWKWY; -.
DR OrthoDB; 1033833at2759; -.
DR TreeFam; TF313763; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000002349; Expressed in prefrontal cortex and 63 other tissues.
DR ExpressionAtlas; P61267; baseline.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048787; C:presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; 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:0017157; P:regulation of exocytosis; IEA:InterPro.
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:SF334; PTHR19957:SF334; 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 Coiled coil; Direct protein sequencing; Membrane;
KW Neurotransmitter transport; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..288
FT /note="Syntaxin-1B"
FT /id="PRO_0000210191"
FT TOPO_DOM 1..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..288
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 191..253
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 29..104
FT /evidence="ECO:0000255"
FT SITE 252..253
FT /note="(Microbial infection) Cleavage; by C.botulinum
FT neurotoxin type C (BoNT/C)"
FT /evidence="ECO:0000305|PubMed:8611567"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61264"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61266"
FT CONFLICT 79
FT /note="T -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 288 AA; 33275 MW; C66D4785F63C851F CRC64;
MKDRTQELRS AKDSDDEEEV VHVDRDHFMD EFFEQVEEIR GCIEKLSEDV EQVKKQHSAI
LAAPNPDEKT KQELEDLTTD IKKTANKVRS KLKAIEQSIE QEEGLNRSSA DLRIRKTQHS
TLSRKFVEVM TEYNATQSKY RDRCKDRIQR QLEITGRTTT NEELEDMLES GKLAIFTDDI
KMDSQMTKQA LNEIETRHNE IIKLETSIRE LHDMFVDMAM LVESQGEMID RIEYNVEHSV
DYVERAVSDT KKAVKYQSKA RRKKIMIIIC CVVLGVVLAS SIGGTLGL
