ID STXB4_MOUSE Reviewed; 557 AA.
AC Q9WV89; Q5SUA6; Q5SUA8; Q5SUA9; Q8CFL1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 01-MAY-2013, entry version 93.
DE RecName: Full=Syntaxin-binding protein 4;
DE AltName: Full=Syntaxin 4-interacting protein;
DE Short=STX4-interacting protein;
DE Short=Synip;
GN Name=Stxbp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, INTERACTION WITH STX4A, AND TISSUE SPECIFICITY.
RX PubMed=10394363; DOI=10.1016/S1097-2765(01)80007-1;
RA Min J., Okada S., Kanzaki M., Elmendorf J.S., Coker K.J., Ceresa B.P.,
RA Syu L.-J., Noda Y., Saltiel A.R., Pessin J.E.;
RT "Synip: a novel insulin-regulated syntaxin 4-binding protein mediating
RT GLUT4 translocation in adipocytes.";
RL Mol. Cell 3:751-760(1999).
RN [2]
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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-557 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12855681; DOI=10.1074/jbc.M305114200;
RA Saito T., Okada S., Yamada E., Ohshima K., Shimizu H., Shimomura K.,
RA Sato M., Pessin J.E., Mori M.;
RT "Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate
RT insulin secretion in the pancreatic beta HC-9 cell.";
RL J. Biol. Chem. 278:36718-36725(2003).
RN [6]
RP PHOSPHORYLATION AT SER-99, AND MUTAGENESIS OF SER-97 AND SER-99.
RX PubMed=15753124; DOI=10.1083/jcb.200408182;
RA Yamada E., Okada S., Saito T., Ohshima K., Sato M., Tsuchiya T.,
RA Uehara Y., Shimizu H., Mori M.;
RT "Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-
RT containing vesicles.";
RL J. Cell Biol. 168:921-928(2005).
RN [7]
RP STRUCTURE BY NMR OF 12-107.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of syntaxin binding protein 4.";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the translocation of transport vesicles
CC from the cytoplasm to the plasma membrane. Inhibits the
CC translocation of SLC2A4 from intracellular vesicles to the plasma
CC membrane by STX4A binding and preventing the interaction between
CC STX4A and VAMP2. Stimulation with insulin disrupts the interaction
CC with STX4A, leading to increased levels of SLC2A4 at the plasma
CC membrane. May also play a role in the regulation of insulin
CC release by pancreatic beta cells after stimulation by glucose.
CC -!- SUBUNIT: Interacts with STX4A.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9WV89-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WV89-2; Sequence=VSP_017183;
CC Name=3;
CC IsoId=Q9WV89-3; Sequence=VSP_017179, VSP_017180;
CC Note=Gene prediction based on EST data;
CC Name=4;
CC IsoId=Q9WV89-4; Sequence=VSP_017184, VSP_017185;
CC Note=Gene prediction based on EST data;
CC Name=5;
CC IsoId=Q9WV89-5; Sequence=VSP_017181, VSP_017182;
CC Note=Gene prediction based on EST data;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart, testis,
CC adipocytes and pancreatic islet cells.
CC -!- PTM: Phosphorylated on Ser-99 by PKB/AKT2 after insulin treatment.
CC Phosphorylation on Ser-99 abolishes the interaction with STX4A.
CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC -!- SIMILARITY: Contains 1 WW domain.
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DR EMBL; AF152924; AAD43533.1; -; mRNA.
DR EMBL; AL646046; CAI23907.1; -; Genomic_DNA.
DR EMBL; AL646046; CAI23908.1; -; Genomic_DNA.
DR EMBL; AL646046; CAI23909.1; -; Genomic_DNA.
DR EMBL; AL646046; CAI23910.1; -; Genomic_DNA.
DR EMBL; AL646046; CAI23911.1; -; Genomic_DNA.
DR EMBL; BC032881; AAH32881.1; -; mRNA.
DR EMBL; AK138499; BAE23686.1; -; mRNA.
DR IPI; IPI00125455; -.
DR IPI; IPI00461639; -.
DR IPI; IPI00515178; -.
DR IPI; IPI00648170; -.
DR IPI; IPI00648897; -.
DR RefSeq; NP_035635.1; NM_011505.2.
DR UniGene; Mm.207203; -.
DR PDB; 1WI4; NMR; -; A=12-107.
DR PDBsum; 1WI4; -.
DR ProteinModelPortal; Q9WV89; -.
DR SMR; Q9WV89; 13-113, 502-534.
DR PhosphoSite; Q9WV89; -.
DR PRIDE; Q9WV89; -.
DR Ensembl; ENSMUST00000020858; ENSMUSP00000020858; ENSMUSG00000020546.
DR Ensembl; ENSMUST00000107872; ENSMUSP00000103504; ENSMUSG00000020546.
DR Ensembl; ENSMUST00000107875; ENSMUSP00000103507; ENSMUSG00000020546.
DR Ensembl; ENSMUST00000143203; ENSMUSP00000116191; ENSMUSG00000020546.
DR GeneID; 20913; -.
DR KEGG; mmu:20913; -.
DR UCSC; uc007kwu.2; mouse.
DR UCSC; uc007kwx.2; mouse.
DR UCSC; uc007kwy.2; mouse.
DR CTD; 252983; -.
DR MGI; MGI:1342296; Stxbp4.
DR eggNOG; NOG72384; -.
DR GeneTree; ENSGT00390000002226; -.
DR HOGENOM; HOG000015395; -.
DR HOVERGEN; HBG058016; -.
DR InParanoid; Q9WV89; -.
DR KO; K15302; -.
DR OMA; PAFQMIT; -.
DR ChiTaRS; STXBP4; mouse.
DR EvolutionaryTrace; Q9WV89; -.
DR NextBio; 299809; -.
DR ArrayExpress; Q9WV89; -.
DR Bgee; Q9WV89; -.
DR CleanEx; MM_STXBP4; -.
DR Genevestigator; Q9WV89; -.
DR GermOnline; ENSMUSG00000020546; Mus musculus.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Compara.
DR GO; GO:0005634; C:nucleus; IEA:Compara.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015758; P:glucose transport; IDA:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR Gene3D; 1.10.238.10; -; 1.
DR InterPro; IPR011992; EF-hand-like_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR001202; WW_dom.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF50156; PDZ; 1.
DR SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 557 Syntaxin-binding protein 4.
FT /FTId=PRO_0000076331.
FT DOMAIN 19 105 PDZ.
FT DOMAIN 500 533 WW.
FT COILED 298 408 Potential.
FT MOD_RES 10 10 Phosphoserine (By similarity).
FT MOD_RES 99 99 Phosphoserine; by PKB/AKT2.
FT VAR_SEQ 195 226 DIAPAWTDDDSGPQGKISLNPSVRLKAEKLEM -> AHMER
FT KKRHESSGQSKMWHWSCSMMKVEVFIP (in isoform
FT 3).
FT /FTId=VSP_017179.
FT VAR_SEQ 227 557 Missing (in isoform 3).
FT /FTId=VSP_017180.
FT VAR_SEQ 227 258 ALNYLGIQPTKEQREALREQVQADSKGTVSFG -> VNPLK
FT KNHFLHKTAGKNCLVLGEEDIGESLVS (in isoform
FT 5).
FT /FTId=VSP_017181.
FT VAR_SEQ 259 557 Missing (in isoform 5).
FT /FTId=VSP_017182.
FT VAR_SEQ 502 557 LPYGWEEAYTADGIKYFINHVTQTTSWIHPVMSALNLSCAE
FT ESEEDCPRELTDPKS -> KLSLSSSSSPSSSSSFSSSSSC
FT NLLNKAEERP (in isoform 2).
FT /FTId=VSP_017183.
FT VAR_SEQ 520 520 N -> K (in isoform 4).
FT /FTId=VSP_017184.
FT VAR_SEQ 521 557 Missing (in isoform 4).
FT /FTId=VSP_017185.
FT MUTAGEN 97 97 S->F: No effect.
FT MUTAGEN 99 99 S->F: Abolishes phosphorylation by
FT PKB/AKT2.
FT STRAND 20 25
FT STRAND 33 37
FT STRAND 39 43
FT STRAND 45 52
FT HELIX 57 61
FT STRAND 69 73
FT HELIX 83 92
FT STRAND 96 99
FT STRAND 101 106
SQ SEQUENCE 557 AA; 61689 MW; 9211A8B02AF8EC86 CRC64;
MSDGTASARS SSPLDRDPAF RVITVTKETG LGLKILGGIN RNEGPLVYIH EVIPGGDCYK
DGRLKPGDQL VSINKESMIG VSFEEAKSII TRAKLRSESP WEIAFIRQKS YCGHPGNICC
PSPQVSEDCG PQTSTFTLLS SPSETLLPKT SSTPQTQDST FPSCKAIQTK PEHDKTEHSP
ITSLDNSPAD TSNADIAPAW TDDDSGPQGK ISLNPSVRLK AEKLEMALNY LGIQPTKEQR
EALREQVQAD SKGTVSFGDF VQVARSLFCL QLDEVNVGVH EIPSILDSQL LPCDSLEADE
VGKLRQERNA ALEERNVLKE KLLESEKHRK QLIEELQNVK QEAKAVAEET RALRSRIHLA
EAAQRQAHGM EMDYEEVIRL LEAEVSELKA QLADYSDQNK ESVQDLRKRV TVLDCQLRKS
EMARKAFKAS TERLLGFIEA IQEVLLDSSA PLSTLSERRA VLASQTSLPL LARNGRSFPA
TLLLESKELV RSVRAILDMD CLPYGWEEAY TADGIKYFIN HVTQTTSWIH PVMSALNLSC
AEESEEDCPR ELTDPKS
//
