STX1B_MOUSE
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 03-AUG-2022, entry version 143.
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; 7.
DR IntAct; P61264; 6.
DR MINT; P61264; -.
DR STRING; 10090.ENSMUSP00000101874; -.
DR iPTMnet; P61264; -.
DR PhosphoSitePlus; P61264; -.
DR SwissPalm; P61264; -.
DR MaxQB; P61264; -.
DR PaxDb; P61264; -.
DR PeptideAtlas; P61264; -.
DR PRIDE; P61264; -.
DR ProteomicsDB; 257504; -.
DR Antibodypedia; 67397; 55 antibodies from 18 providers.
DR DNASU; 56216; -.
DR Ensembl; ENSMUST00000106267; ENSMUSP00000101874; ENSMUSG00000030806.
DR GeneID; 56216; -.
DR KEGG; mmu:56216; -.
DR UCSC; uc009jwx.1; mouse.
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; ARRWKWY; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; P61264; -.
DR TreeFam; TF313763; -.
DR Reactome; R-MMU-5682910; LGI-ADAM interactions.
DR BioGRID-ORCS; 56216; 2 hits in 73 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 130 other tissues.
DR ExpressionAtlas; P61264; baseline and differential.
DR Genevisible; P61264; MM.
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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IC:SynGO-UCL.
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:0008021; C:synaptic vesicle; 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:0006887; P:exocytosis; IBA:GO_Central.
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:0015031; P:protein transport; 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; 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_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
