STXB5_RAT
ID STXB5_RAT Reviewed; 1152 AA.
AC Q9WU70; Q9WU71; Q9Z152;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Syntaxin-binding protein 5;
DE AltName: Full=Lethal(2) giant larvae protein homolog 3;
DE AltName: Full=Tomosyn-1;
GN Name=Stxbp5; Synonyms=Llgl3;
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] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP INTERACTION WITH STX1A AND STX1B, IDENTIFICATION IN A COMPLEX WITH STX1A;
RP SNAP25 AND SYT1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9620695; DOI=10.1016/s0896-6273(00)80472-9;
RA Fujita Y., Shirataki H., Sakisaka T., Asakura T., Ohya T., Kotani H.,
RA Yokoyama S., Nishioka H., Matsuura Y., Mizoguchi A., Scheller R.H.,
RA Takai Y.;
RT "Tomosyn: a syntaxin-1-binding protein that forms a novel complex in the
RT neurotransmitter release process.";
RL Neuron 20:905-915(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), INTERACTION WITH STX1A,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=10066450; DOI=10.1006/bbrc.1999.0300;
RA Yokoyama S., Shirataki H., Sakisaka T., Takai Y.;
RT "Three splicing variants of tomosyn and identification of their syntaxin-
RT binding region.";
RL Biochem. Biophys. Res. Commun. 256:218-222(1999).
RN [3]
RP MUTAGENESIS OF SER-724, AND PHOSPHORYLATION AT SER-724.
RX PubMed=16186257; DOI=10.1083/jcb.200504055;
RA Baba T., Sakisaka T., Mochida S., Takai Y.;
RT "PKA-catalyzed phosphorylation of tomosyn and its implication in Ca2+-
RT dependent exocytosis of neurotransmitter.";
RL J. Cell Biol. 170:1113-1125(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-783, AND
RP IDENTIFICATION BY 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1010-1145 IN COMPLEX WITH STX1A
RP AND SNAP25.
RX PubMed=15316007; DOI=10.1074/jbc.m408767200;
RA Pobbati A.V., Razeto A., Boeddener M., Becker S., Fasshauer D.;
RT "Structural basis for the inhibitory role of tomosyn in exocytosis.";
RL J. Biol. Chem. 279:47192-47200(2004).
CC -!- FUNCTION: Inhibits translocation of GLUT4 from intracellular vesicles
CC to the plasma membrane (By similarity). Plays a regulatory role in
CC calcium-dependent exocytosis and neurotransmitter release. Inhibits
CC membrane fusion between transport vesicles and the plasma membrane. May
CC modulate the assembly of trans-SNARE complexes between transport
CC vesicles and the plasma membrane. Competes with STXBP1 for STX1
CC binding. {ECO:0000250, ECO:0000269|PubMed:9620695}.
CC -!- SUBUNIT: Part of a complex that contains STXBP5, STX4A and SNAP23 (By
CC similarity). Interacts with STX1A and STX4A via its v-SNARE homology
CC domain. Part of a complex that contains STX1, STXBP5, SNAP25 and SYT1.
CC {ECO:0000250, ECO:0000269|PubMed:10066450, ECO:0000269|PubMed:15316007,
CC ECO:0000269|PubMed:9620695}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9620695}. Cell
CC membrane {ECO:0000269|PubMed:9620695}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9620695}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:9620695}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9620695}. Synapse {ECO:0000269|PubMed:9620695}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000269|PubMed:9620695}. Note=Cytoplasmic, and associated with
CC vesicular membranes and the plasma membrane. Detected at synapses and
CC on synaptic vesicles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=B-tomosyn;
CC IsoId=Q9WU70-1; Sequence=Displayed;
CC Name=2; Synonyms=M-tomosyn;
CC IsoId=Q9WU70-2; Sequence=VSP_016477;
CC Name=3; Synonyms=S-tomosyn;
CC IsoId=Q9WU70-3; Sequence=VSP_016476;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in heart, brain, lung, liver,
CC skeletal muscle, kidney and testis. Isoform 2 is detected in brain and
CC in testis. Isoform 3 is detected in testis.
CC {ECO:0000269|PubMed:10066450, ECO:0000269|PubMed:9620695}.
CC -!- PTM: Phosphorylation by PKA reduces interaction with STX1A and enhances
CC synaptic neurotransmitter release. {ECO:0000269|PubMed:16186257}.
CC -!- SIMILARITY: Belongs to the WD repeat L(2)GL family. {ECO:0000305}.
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DR EMBL; U92072; AAD04756.1; -; mRNA.
DR EMBL; AF118889; AAD27818.1; -; mRNA.
DR EMBL; AF118890; AAD27819.1; -; mRNA.
DR PIR; T42213; T42213.
DR RefSeq; NP_110470.1; NM_030843.2. [Q9WU70-2]
DR RefSeq; NP_848035.1; NM_178345.1. [Q9WU70-1]
DR RefSeq; NP_848036.1; NM_178346.1. [Q9WU70-3]
DR PDB; 1URQ; X-ray; 2.00 A; A=1086-1145.
DR PDBsum; 1URQ; -.
DR AlphaFoldDB; Q9WU70; -.
DR SMR; Q9WU70; -.
DR BioGRID; 249498; 2.
DR CORUM; Q9WU70; -.
DR IntAct; Q9WU70; 1.
DR STRING; 10116.ENSRNOP00000049322; -.
DR iPTMnet; Q9WU70; -.
DR PhosphoSitePlus; Q9WU70; -.
DR SwissPalm; Q9WU70; -.
DR PaxDb; Q9WU70; -.
DR PRIDE; Q9WU70; -.
DR Ensembl; ENSRNOT00000049699; ENSRNOP00000049322; ENSRNOG00000013351. [Q9WU70-1]
DR GeneID; 81022; -.
DR KEGG; rno:81022; -.
DR UCSC; RGD:708517; rat. [Q9WU70-1]
DR CTD; 134957; -.
DR RGD; 708517; Stxbp5.
DR eggNOG; KOG1983; Eukaryota.
DR GeneTree; ENSGT00950000182906; -.
DR HOGENOM; CLU_002808_0_0_1; -.
DR InParanoid; Q9WU70; -.
DR OMA; VSSFHFC; -.
DR OrthoDB; 84844at2759; -.
DR PhylomeDB; Q9WU70; -.
DR EvolutionaryTrace; Q9WU70; -.
DR PRO; PR:Q9WU70; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013351; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q9WU70; RN.
DR GO; GO:0005892; C:acetylcholine-gated channel complex; ISO:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0098674; C:extrinsic component of neuronal dense core vesicle membrane; ISO:RGD.
DR GO; GO:0098888; C:extrinsic component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0030141; C:secretory granule; TAS:BHF-UCL.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IDA:SynGO.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0045159; F:myosin II binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; ISO:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:RGD.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
DR GO; GO:0050708; P:regulation of protein secretion; IBA:GO_Central.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; ISO:RGD.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISO:RGD.
DR GO; GO:0099504; P:synaptic vesicle cycle; IDA:SynGO.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR000664; Lethal2_giant.
DR InterPro; IPR013905; Lgl_C_dom.
DR InterPro; IPR013577; LLGL2.
DR InterPro; IPR042855; V_SNARE_CC.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF08596; Lgl_C; 1.
DR Pfam; PF08366; LLGL; 1.
DR Pfam; PF00400; WD40; 1.
DR PRINTS; PR00962; LETHAL2GIANT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50892; V_SNARE; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Exocytosis; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Synapse;
KW Transport; WD repeat.
FT CHAIN 1..1152
FT /note="Syntaxin-binding protein 5"
FT /id="PRO_0000051246"
FT REPEAT 62..95
FT /note="WD 1"
FT REPEAT 102..141
FT /note="WD 2"
FT REPEAT 146..182
FT /note="WD 3"
FT REPEAT 201..235
FT /note="WD 4"
FT REPEAT 241..273
FT /note="WD 5"
FT REPEAT 295..337
FT /note="WD 6"
FT REPEAT 345..379
FT /note="WD 7"
FT REPEAT 401..478
FT /note="WD 8"
FT REPEAT 506..620
FT /note="WD 9"
FT REPEAT 634..696
FT /note="WD 10"
FT REPEAT 795..852
FT /note="WD 11"
FT REPEAT 861..935
FT /note="WD 12"
FT REPEAT 940..984
FT /note="WD 13"
FT REPEAT 998..1021
FT /note="WD 14"
FT DOMAIN 1087..1147
FT /note="v-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00290"
FT REGION 14..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 675..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 724
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:16186257"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 763
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 785
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8K400"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K400"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K400"
FT MOD_RES 1040
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K400"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5T5C0"
FT VAR_SEQ 717..769
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10066450"
FT /id="VSP_016476"
FT VAR_SEQ 717..752
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10066450,
FT ECO:0000303|PubMed:9620695"
FT /id="VSP_016477"
FT MUTAGEN 724
FT /note="S->A: Strongly reduces phosphorylation."
FT /evidence="ECO:0000269|PubMed:16186257"
FT MUTAGEN 724
FT /note="S->D: Reduces interaction with STX1A."
FT /evidence="ECO:0000269|PubMed:16186257"
FT HELIX 1089..1143
FT /evidence="ECO:0007829|PDB:1URQ"
SQ SEQUENCE 1152 AA; 127659 MW; 1C07CABD8421CBD5 CRC64;
MRKFNIRKVL DGLTAGSSSA SQQQQQQQHP PGNREPEIQE TLQSEHFQLC KTVRHGFPYQ
PSALAFDPVQ KILAVGTQTG ALRLFGRPGV ECYCQHDSGA AVIQLQFLIN EGALVSALAD
DTLHLWNLRQ KRPAVLHSLK FCRERVTFCH LPFQSKWLYV GTERGNIHIV NVESFTLSGY
VIMWNKAIEL SSKSHPGPVV HISDNPMDEG KLLIGFESGT VVLWDLKSKK ADYRYTYDEA
IHSVAWHHEG KQFICSHSDG TLTIWNVRSP TKPVQTITPH GKQLKDGKKP EPCKPILKVE
FKTTRSGEPF IILSGGLSYD TVGRRPCLTV MHGKSTAVLE MDYSIVDFLT LCETPYPNDF
QEPYAVVVLL EKDLVLIDLA QNGYPIFENP YPLSIHESPV TCCEYFADCP VDLIPALYSV
GARQKRQGYS KKEWPINGGN WGLGAQSYPE IIITGHADGS IKFWDASAIT LQVLYKLKTS
KVFEKSRNKD DRQNTDIVDE DPYAIQIISW CPESRMLCIA GVSAHVIIYR FSKQEVVTEV
IPMLEVRLLY EINDVETPEG EQPPPLSTPV GSSTSQPIPP QSHPSTSSSS SDGLRDNVPC
LKVKNSPLKQ SPGYQTELVI QLVWVGGEPP QQITSLALNS SYGLVVFGNS NGIAMVDYLQ
KAVLLNLSTI ELYGSNDPYR REPRSPRKSR QPSGAGLCDI TEGTVVPEDR CKSPTSGSSS
PHNSDDEQKV NNFIEKVKTQ SRKFSKMVAS DLAKMSRKLS LPTDLKPDLD VKDNSFSRSR
SSSVTSIDKE SREAISALHF CETFTRKADS SPSPCLWVGT TVGTAFVITL NLPLGPEQRL
LQPVIVSPSG TILRLKGAIL RMAFLDAAGC LMPPAYEPWT EHNVPEEKDE KEKLKKRRPV
SVSPSSSQEI SENQYAVICS EKQAKVISLP TQNCAYKQNI TETSFVLRGD IVALSNSVCL
ACFCANGHIM TFSLPSLRPL LDVYYLPLTN MRIARTFCFA NSGQALYLVS PTEIQRLTYS
QETCENLQEM LGELFTPVET PEAPNRGFFK GLFGGGAQSL DREELFGESS SGKASRSLAQ
HIPGPGGIEG VKGAASGVVG ELARARLALD ERGQKLSDLE ERTAAMMSSA DSFSKHAHEM
MLKYKDKKWY QF
