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   27-MAR-2024, entry version 147.
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; 3.
DR   MINT; P61265; -.
DR   STRING; 10116.ENSRNOP00000026063; -.
DR   iPTMnet; P61265; -.
DR   PhosphoSitePlus; P61265; -.
DR   SwissPalm; P61265; -.
DR   jPOST; P61265; -.
DR   PaxDb; 10116-ENSRNOP00000026063; -.
DR   Ensembl; ENSRNOT00000026063.5; ENSRNOP00000026063.2; ENSRNOG00000019193.5.
DR   Ensembl; ENSRNOT00055051517; ENSRNOP00055042461; ENSRNOG00055029735.
DR   Ensembl; ENSRNOT00060041807; ENSRNOP00060034664; ENSRNOG00060024103.
DR   Ensembl; ENSRNOT00065025135; ENSRNOP00065019675; ENSRNOG00065015178.
DR   GeneID; 24923; -.
DR   KEGG; rno:24923; -.
DR   UCSC; RGD:3784; rat.
DR   AGR; RGD:3784; -.
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   OrthoDB; 2876074at2759; -.
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 cell types or tissues.
DR   GO; GO:0012505; C:endomembrane system; 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: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:0019904; F:protein domain specific binding; IPI: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:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IMP:SynGO.
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: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:0072657; P:protein localization to membrane; IDA:ParkinsonsUK-UCL.
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: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; 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; P61265; RN.
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
//