ID   STX1B_MOUSE             Reviewed;         288 AA.
AC   P61264; A2RSB4; O35525; P32853;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   27-MAR-2024, entry version 151.
DE   RecName: Full=Syntaxin-1B;
GN   Name=Stx1b; Synonyms=Stx1b1, Stx1b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Fujiwara T., Genda M., Nagai A., Okazaki M., Watanabe T., Nagamatsu S.,
RA   Akagawa K.;
RT   "Cloning and sequence analysis of the various species HPC-1/syntaxin
RT   cDNA.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RA   Horikawa H.P.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 10-40; 46-69; 94-107; 125-139; 151-181; 189-197 AND
RP   232-245, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   FUNCTION, AND INTERACTION WITH SYT6 AND SYT8.
RX   PubMed=15774481; DOI=10.1074/jbc.m412920200;
RA   Hutt D.M., Baltz J.M., Ngsee J.K.;
RT   "Synaptotagmin VI and VIII and syntaxin 2 are essential for the mouse sperm
RT   acrosome reaction.";
RL   J. Biol. Chem. 280:20197-20203(2005).
RN   [7]
RP   INTERACTION WITH OTOF.
RC   STRAIN=BALB/cJ; TISSUE=Cochlea;
RX   PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
RA   Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C., Bahloul A.,
RA   Perfettini I., Le Gall M., Rostaing P., Hamard G., Triller A., Avan P.,
RA   Moser T., Petit C.;
RT   "Otoferlin, defective in a human deafness form, is essential for exocytosis
RT   at the auditory ribbon synapse.";
RL   Cell 127:277-289(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-14, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC       presynaptic active zones (By similarity). May mediate Ca(2+)-regulation
CC       of exocytosis acrosomal reaction in sperm. {ECO:0000250,
CC       ECO:0000269|PubMed:15774481}.
CC   -!- SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the
CC       interaction is Ca(2+)-dependent. {ECO:0000269|PubMed:15774481,
CC       ECO:0000269|PubMed:17055430}.
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; D45207; BAA25986.1; -; mRNA.
DR   EMBL; D29743; BAA06162.1; -; mRNA.
DR   EMBL; AC149222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132042; AAI32043.1; -; mRNA.
DR   EMBL; BC132068; AAI32069.1; -; mRNA.
DR   CCDS; CCDS40146.1; -.
DR   RefSeq; NP_077725.1; NM_024414.2.
DR   AlphaFoldDB; P61264; -.
DR   SMR; P61264; -.
DR   BioGRID; 207850; 14.
DR   IntAct; P61264; 6.
DR   MINT; P61264; -.
DR   STRING; 10090.ENSMUSP00000101874; -.
DR   GlyGen; P61264; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61264; -.
DR   MetOSite; P61264; -.
DR   PhosphoSitePlus; P61264; -.
DR   SwissPalm; P61264; -.
DR   MaxQB; P61264; -.
DR   PaxDb; 10090-ENSMUSP00000101874; -.
DR   PeptideAtlas; P61264; -.
DR   ProteomicsDB; 257504; -.
DR   Antibodypedia; 67397; 81 antibodies from 19 providers.
DR   DNASU; 56216; -.
DR   Ensembl; ENSMUST00000106267.5; ENSMUSP00000101874.4; ENSMUSG00000030806.7.
DR   GeneID; 56216; -.
DR   KEGG; mmu:56216; -.
DR   UCSC; uc009jwx.1; mouse.
DR   AGR; MGI:1930705; -.
DR   CTD; 112755; -.
DR   MGI; MGI:1930705; Stx1b.
DR   VEuPathDB; HostDB:ENSMUSG00000030806; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   GeneTree; ENSGT01030000234627; -.
DR   HOGENOM; CLU_042423_2_2_1; -.
DR   InParanoid; P61264; -.
DR   OMA; ANIEQKG; -.
DR   OrthoDB; 2876074at2759; -.
DR   PhylomeDB; P61264; -.
DR   TreeFam; TF313763; -.
DR   Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR   BioGRID-ORCS; 56216; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Stx1b; mouse.
DR   PRO; PR:P61264; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P61264; Protein.
DR   Bgee; ENSMUSG00000030806; Expressed in superior frontal gyrus and 131 other cell types or tissues.
DR   ExpressionAtlas; P61264; baseline and differential.
DR   GO; GO:0030424; C:axon; IDA:SynGO-UCL.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR   GO; GO:0005652; C:nuclear lamina; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0098793; C:presynapse; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0048787; C:presynaptic active zone membrane; ISO:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0048791; P:calcium ion-regulated exocytosis of neurotransmitter; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; ISO:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:1905302; P:negative regulation of macropinocytosis; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; ISS:ParkinsonsUK-UCL.
DR   GO; GO:1903422; P:negative regulation of synaptic vesicle recycling; IMP:ParkinsonsUK-UCL.
DR   GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IGI:ParkinsonsUK-UCL.
DR   GO; GO:1904050; P:positive regulation of spontaneous neurotransmitter secretion; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0072657; P:protein localization to membrane; ISO:MGI.
DR   GO; GO:0017157; P:regulation of exocytosis; ISO:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0060025; P:regulation of synaptic activity; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0010807; P:regulation of synaptic vesicle priming; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0061669; P:spontaneous neurotransmitter secretion; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0016081; P:synaptic vesicle docking; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:SynGO.
DR   GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR   CDD; cd15880; SNARE_syntaxin1; 1.
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:SF334; SYNTAXIN-1B; 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.
DR   Genevisible; P61264; MM.
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_0000210193"
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:0007744|PubMed:21183079"
FT   MOD_RES         14
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CONFLICT        3..4
FT                   /note="DR -> EW (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        8
FT                   /note="L -> R (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="D -> A (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        30
FT                   /note="D -> A (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51..55
FT                   /note="EQVKK -> GRVGG (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="N -> K (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        98
FT                   /note="S -> G (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        114..116
FT                   /note="IRK -> YRT (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="L -> V (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="K -> N (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="Q -> K (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        148
FT                   /note="I -> L (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191
FT                   /note="L -> R (in Ref. 1; BAA25986)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   288 AA;  33245 MW;  2733497E02978BEB CRC64;
     MKDRTQELRS AKDSDDEEEV VHVDRDHFMD EFFEQVEEIR GCIEKLSEDV EQVKKQHSAI
     LAAPNPDEKT KQELEDLTAD IKKTANKVRS KLKAIEQSIE QEEGLNRSSA DLRIRKTQHS
     TLSRKFVEVM TEYNATQSKY RDRCKDRIQR QLEITGRTTT NEELEDMLES GKLAIFTDDI
     KMDSQMTKQA LNEIETRHNE IIKLETSIRE LHDMFVDMAM LVESQGEMID RIEYNVEHSV
     DYVERAVSDT KKAVKYQSKA RRKKIMIIIC CVVLGVVLAS SIGGTLGL
//