ID   STX1B_SHEEP             Reviewed;         288 AA.
AC   P61268; P41414;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Syntaxin-1B;
DE   AltName: Full=Syntaxin-1B2;
GN   Name=STX1B; Synonyms=STX1B2;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Helps C.R., Harbour D.A.;
RT   "Cloning and sequence analysis of sheep syntaxin 1B.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR   EMBL; AF081781; AAC31961.1; -; mRNA.
DR   RefSeq; NP_001009440.1; NM_001009440.1.
DR   AlphaFoldDB; P61268; -.
DR   SMR; P61268; -.
DR   STRING; 9940.ENSOARP00000008892; -.
DR   Ensembl; ENSOART00020036442; ENSOARP00020030128; ENSOARG00020023307.
DR   GeneID; 443479; -.
DR   KEGG; oas:443479; -.
DR   CTD; 112755; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   OrthoDB; 1033833at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0000149; F:SNARE binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Coiled coil; Membrane; Neurotransmitter transport; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..288
FT                   /note="Syntaxin-1B"
FT                   /id="PRO_0000210195"
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   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"
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