STXB1_MOUSE
ID STXB1_MOUSE Reviewed; 594 AA.
AC O08599; A2ARS2; A2ARS3; A2ARS4; Q5WAC6; Q8VD51;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Syntaxin-binding protein 1;
DE AltName: Full=Protein unc-18 homolog 1;
DE Short=Unc18-1;
DE AltName: Full=Protein unc-18 homolog A;
DE Short=Unc-18A;
GN Name=Stxbp1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=8824310; DOI=10.1523/jneurosci.16-21-06695.1996;
RA Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.;
RT "A murine neural-specific homolog corrects cholinergic defects in
RT Caenorhabditis elegans unc-18 mutants.";
RL J. Neurosci. 16:6695-6702(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=9705297; DOI=10.1074/jbc.273.34.21642;
RA Gotoh K., Yokota H., Kikuya E., Watanabe T., Oishi M.;
RT "Genomic structure of MUNC18-1 protein, which is involved in docking and
RT fusion of synaptic vesicles in brain.";
RL J. Biol. Chem. 273:21642-21647(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RA Fehr C., Buck K.J.;
RT "Characterization of candidate genes for multiple ethanol influenced traits
RT on mouse chromosome 2.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [6]
RP PROTEIN SEQUENCE OF 30-39; 47-98; 101-120; 162-184; 193-225; 228-235;
RP 266-275; 278-314; 326-332; 344-356; 368-382; 389-425; 468-518 AND 537-594.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-511 AND SER-516, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=22039235; DOI=10.1167/iovs.11-8246;
RA Sokal I., Haeseleer F.;
RT "Insight into the role of Ca2+-binding protein 5 in vesicle exocytosis.";
RL Invest. Ophthalmol. Vis. Sci. 52:9131-9141(2011).
CC -!- FUNCTION: Participates in the regulation of synaptic vesicle docking
CC and fusion through interaction with GTP-binding proteins (By
CC similarity). Essential for neurotransmission and binds syntaxin, a
CC component of the synaptic vesicle fusion machinery probably in a 1:1
CC ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May
CC play a role in determining the specificity of intracellular fusion
CC reactions (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61765}.
CC -!- SUBUNIT: Interacts with SYTL4 (By similarity). Interacts with STX1A (By
CC similarity). Interacts with alpha-synuclein/SNCA; this interaction
CC controls SNCA self-replicating aggregation (By similarity). Interacts
CC with RAB3A; this interaction promotes RAB3A dissociation from the
CC vesicle membrane (By similarity). Interacts with CABP5 (By similarity).
CC {ECO:0000250|UniProtKB:P61763, ECO:0000250|UniProtKB:P61764,
CC ECO:0000250|UniProtKB:P61765}.
CC -!- INTERACTION:
CC O08599-1; P31423: Grm4; Xeno; NbExp=2; IntAct=EBI-15809216, EBI-7974891;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P61764}. Membrane; Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O08599-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O08599-2; Sequence=VSP_010496;
CC -!- TISSUE SPECIFICITY: Expressed in the inner and outer plexiform layers
CC of the retina (at protein level). {ECO:0000269|PubMed:22039235}.
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM20726.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D45903; BAA19479.1; -; mRNA.
DR EMBL; AB012697; BAA32486.1; -; Genomic_DNA.
DR EMBL; AF326545; AAL37391.1; -; mRNA.
DR EMBL; AF326563; AAL37409.1; -; mRNA.
DR EMBL; AL845471; CAM20726.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL845471; CAM20727.1; -; Genomic_DNA.
DR EMBL; AL845471; CAM20728.1; -; Genomic_DNA.
DR EMBL; BC031728; AAH31728.1; -; mRNA.
DR CCDS; CCDS15933.1; -. [O08599-1]
DR CCDS; CCDS50572.1; -. [O08599-2]
DR RefSeq; NP_001107041.1; NM_001113569.1. [O08599-2]
DR RefSeq; NP_033321.2; NM_009295.2. [O08599-1]
DR AlphaFoldDB; O08599; -.
DR SMR; O08599; -.
DR BioGRID; 203564; 30.
DR DIP; DIP-31951N; -.
DR IntAct; O08599; 18.
DR MINT; O08599; -.
DR STRING; 10090.ENSMUSP00000089051; -.
DR iPTMnet; O08599; -.
DR PhosphoSitePlus; O08599; -.
DR SwissPalm; O08599; -.
DR EPD; O08599; -.
DR jPOST; O08599; -.
DR MaxQB; O08599; -.
DR PaxDb; O08599; -.
DR PeptideAtlas; O08599; -.
DR PRIDE; O08599; -.
DR ProteomicsDB; 254770; -. [O08599-1]
DR ProteomicsDB; 254771; -. [O08599-2]
DR Antibodypedia; 2191; 517 antibodies from 41 providers.
DR DNASU; 20910; -.
DR Ensembl; ENSMUST00000050000; ENSMUSP00000052440; ENSMUSG00000026797. [O08599-1]
DR Ensembl; ENSMUST00000077458; ENSMUSP00000089051; ENSMUSG00000026797. [O08599-2]
DR GeneID; 20910; -.
DR KEGG; mmu:20910; -.
DR UCSC; uc008jha.2; mouse. [O08599-1]
DR UCSC; uc008jhb.2; mouse. [O08599-2]
DR CTD; 6812; -.
DR MGI; MGI:107363; Stxbp1.
DR VEuPathDB; HostDB:ENSMUSG00000026797; -.
DR eggNOG; KOG1300; Eukaryota.
DR GeneTree; ENSGT00940000155127; -.
DR HOGENOM; CLU_009210_2_0_1; -.
DR InParanoid; O08599; -.
DR OMA; ITDRTMD; -.
DR OrthoDB; 725424at2759; -.
DR PhylomeDB; O08599; -.
DR TreeFam; TF313242; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 20910; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Stxbp1; mouse.
DR PRO; PR:O08599; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O08599; protein.
DR Bgee; ENSMUSG00000026797; Expressed in retinal neural layer and 229 other tissues.
DR ExpressionAtlas; O08599; baseline and differential.
DR Genevisible; O08599; MM.
DR GO; GO:0030424; C:axon; IDA:SynGO-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098891; C:extrinsic component of presynaptic active zone membrane; IC:SynGO-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:SynGO-UCL.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043274; F:phospholipase binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007412; P:axon target recognition; IMP:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0003006; P:developmental process involved in reproduction; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IDA:MGI.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0002576; P:platelet degranulation; ISO:MGI.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:MGI.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:MGI.
DR GO; GO:1903296; P:positive regulation of glutamate secretion, neurotransmission; ISO:MGI.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; ISO:MGI.
DR GO; GO:0106022; P:positive regulation of vesicle docking; ISO:MGI.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IMP:SynGO.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:2000367; P:regulation of acrosomal vesicle exocytosis; ISO:MGI.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISO:MGI.
DR GO; GO:0031338; P:regulation of vesicle fusion; ISO:MGI.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0035493; P:SNARE complex assembly; ISO:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; TAS:ParkinsonsUK-UCL.
DR GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.40.50.1910; -; 1.
DR Gene3D; 3.40.50.2060; -; 1.
DR Gene3D; 3.90.830.10; -; 1.
DR InterPro; IPR043154; Sec-1-like_dom1.
DR InterPro; IPR043127; Sec-1-like_dom3a.
DR InterPro; IPR001619; Sec1-like.
DR InterPro; IPR027482; Sec1-like_dom2.
DR InterPro; IPR036045; Sec1-like_sf.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..594
FT /note="Syntaxin-binding protein 1"
FT /id="PRO_0000206278"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61765"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61765"
FT VAR_SEQ 576..594
FT /note="QKLLDTLKKLNKTDEEISS -> TKFLMDLRHPDFRESSRVSFEDQAPTME
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010496"
FT VARIANT 216
FT /note="D -> N (in strain: DBA/2J)"
FT CONFLICT 101
FT /note="A -> R (in Ref. 1; BAA19479)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="R -> H (in Ref. 2; BAA32486)"
FT /evidence="ECO:0000305"
FT CONFLICT 537
FT /note="L -> F (in Ref. 1; BAA19479)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="G -> A (in Ref. 1; BAA19479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 594 AA; 67569 MW; 2DD0715F875CE0F3 CRC64;
MAPIGLKAVV GEKIMHDVIK KVKKKGEWKV LVVDQLSMRM LSSCCKMTDI MTEGITIVED
INKRREPLPS LEAVYLITPS EKSVHSLISD FKDPPTAKYR AAHVFFTDSC PDALFNELVK
SRAAKVIKTL TEINIAFLPY ESQVYSLDSA DSFQSFYSPH KAQMKNPILE RLAEQIATLC
ATLKEYPAVR YRGEYKDNAL LAQLIQDKLD AYKADDPTMG EGPDKARSQL LILDRGFDPS
SPVLHELTFQ AMSYDLLPIE NDVYKYETSG IGEARVKEVL LDEDDDLWIA LRHKHIAEVS
QEVTRSLKDF SSSKRMNTGE KTTMRDLSQM LKKMPQYQKE LSKYSTHLHL AEDCMKHYQG
TVDKLCRVEQ DLAMGTDAEG EKIKDPMRAI VPILLDANVS TYDKIRIILL YIFLKNGITE
ENLNKLIQHA QIPPEDSEII TNMAHLGVPI VTDSTLRRRS KPERKERISE QTYQLSRWTP
IIKDIMEDTI EDKLDTKHYP YISTRSSASF STTAVSARYG HWHKNKAPGE YRSGPRLIIF
ILGGVSLNEM RCAYEVTQAN GKWEVLIGST HILTPQKLLD TLKKLNKTDE EISS
