STX1B_RAT
ID STX1B_RAT Reviewed; 288 AA.
AC P61265; P32853;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Syntaxin-1B;
DE AltName: Full=P35B;
DE AltName: Full=Syntaxin-1B2;
GN Name=Stx1b; Synonyms=Stx1b2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-16 AND 31-55.
RC TISSUE=Brain;
RX PubMed=1321498; DOI=10.1126/science.1321498;
RA Bennett M.K., Calakos N., Scheller R.H.;
RT "Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at
RT presynaptic active zones.";
RL Science 257:255-259(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7690687; DOI=10.1016/0092-8674(93)90466-4;
RA Bennett M.K., Garcia-Arraras J.E., Elferink L.A., Peterson K.E.,
RA Fleming A.M., Hazuka C.D., Scheller R.H.;
RT "The syntaxin family of vesicular transport receptors.";
RL Cell 74:863-873(1993).
RN [3]
RP PROTEIN SEQUENCE OF 189-197; 204-209 AND 232-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPE C.
RX PubMed=7901002; DOI=10.1002/j.1460-2075.1993.tb06171.x;
RA Blasi J., Chapman E.R., Yamasaki S., Binz T., Niemann H., Jahn R.;
RT "Botulinum neurotoxin C1 blocks neurotransmitter release by means of
RT cleaving HPC-1/syntaxin.";
RL EMBO J. 12:4821-4828(1993).
RN [5]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION) BY C.BOTULINUM
RP NEUROTOXIN TYPE C.
RX PubMed=7737992; DOI=10.1074/jbc.270.18.10566;
RA Schiavo G., Shone C.C., Bennett M.K., Scheller R.H., Montecucco C.;
RT "Botulinum neurotoxin type C cleaves a single Lys-Ala bond within the
RT carboxyl-terminal region of syntaxins.";
RL J. Biol. Chem. 270:10566-10570(1995).
RN [6]
RP PHOSPHORYLATION AT SER-14.
RX PubMed=12692561; DOI=10.1038/nbt819;
RA Wu C.C., MacCoss M.J., Howell K.E., Yates J.R. III;
RT "A method for the comprehensive proteomic analysis of membrane proteins.";
RL Nat. Biotechnol. 21:532-538(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC presynaptic active zones (PubMed:7901002). May mediate Ca(2+)-
CC regulation of exocytosis acrosomal reaction in sperm (By similarity).
CC {ECO:0000250, ECO:0000305|PubMed:7901002}.
CC -!- SUBUNIT: Interacts with OTOF. Interacts with SYT6 and SYT8; the
CC interaction is Ca(2+)-dependent (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P61265; Q8CJB9: Rnf40; NbExp=4; IntAct=EBI-2255905, EBI-6110162;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type IV
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Cerebral cortex, hippocampus, cerebellum, and
CC adrenal medulla.
CC -!- PTM: Phosphorylated by CK2. {ECO:0000269|PubMed:12692561}.
CC -!- PTM: (Microbial infection) Targeted and hydrolyzed by C.botulinum
CC neurotoxin type C (BoNT/C), which hydrolyzes the 252-Lys-|-Ala-253 bond
CC (PubMed:7737992). Cleavage inhibits neurotransmitter release
CC (PubMed:7901002). {ECO:0000269|PubMed:7737992,
CC ECO:0000269|PubMed:7901002}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; M95735; AAA42197.1; -; mRNA.
DR PIR; B48213; B48213.
DR RefSeq; NP_036832.1; NM_012700.2.
DR AlphaFoldDB; P61265; -.
DR SMR; P61265; -.
DR BioGRID; 247029; 5.
DR CORUM; P61265; -.
DR IntAct; P61265; 2.
DR MINT; P61265; -.
DR STRING; 10116.ENSRNOP00000026063; -.
DR iPTMnet; P61265; -.
DR PhosphoSitePlus; P61265; -.
DR SwissPalm; P61265; -.
DR jPOST; P61265; -.
DR PaxDb; P61265; -.
DR PRIDE; P61265; -.
DR Ensembl; ENSRNOT00000026063; ENSRNOP00000026063; ENSRNOG00000019193.
DR GeneID; 24923; -.
DR KEGG; rno:24923; -.
DR UCSC; RGD:3784; rat.
DR CTD; 112755; -.
DR RGD; 3784; Stx1b.
DR eggNOG; KOG0810; Eukaryota.
DR GeneTree; ENSGT01030000234627; -.
DR HOGENOM; CLU_042423_2_2_1; -.
DR InParanoid; P61265; -.
DR OMA; ARRWKWY; -.
DR OrthoDB; 1033833at2759; -.
DR PhylomeDB; P61265; -.
DR TreeFam; TF313763; -.
DR Reactome; R-RNO-5682910; LGI-ADAM interactions.
DR PRO; PR:P61265; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019193; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; P61265; RN.
DR GO; GO:0030424; C:axon; ISO:RGD.
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:0016020; C:membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0048787; C:presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0042734; C:presynaptic membrane; IDA:ParkinsonsUK-UCL.
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; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IMP:SynGO.
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; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:ParkinsonsUK-UCL.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:1904050; P:positive regulation of spontaneous neurotransmitter secretion; ISO:RGD.
DR GO; GO:0072657; P:protein localization to membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISS:ParkinsonsUK-UCL.
DR GO; GO:0060025; P:regulation of synaptic activity; ISS:ParkinsonsUK-UCL.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISS:ParkinsonsUK-UCL.
DR GO; GO:0061669; P:spontaneous neurotransmitter secretion; ISO:RGD.
DR GO; GO:0016081; P:synaptic vesicle docking; ISS:ParkinsonsUK-UCL.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; ISO:RGD.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:ParkinsonsUK-UCL.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:RGD.
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_0000210194"
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:0000269|PubMed:7737992"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61264"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12692561,
FT ECO:0007744|PubMed:22673903"
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
