GenomeNet

Database: UniProt
Entry: Q9WV89
LinkDB: Q9WV89
Original site: Q9WV89 
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   19-MAR-2014, entry version 100.
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   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   BioGrid; 203567; 1.
DR   PhosphoSite; Q9WV89; -.
DR   PRIDE; Q9WV89; -.
DR   Ensembl; ENSMUST00000020858; ENSMUSP00000020858; ENSMUSG00000020546. [Q9WV89-2]
DR   Ensembl; ENSMUST00000107872; ENSMUSP00000103504; ENSMUSG00000020546. [Q9WV89-3]
DR   Ensembl; ENSMUST00000107875; ENSMUSP00000103507; ENSMUSG00000020546. [Q9WV89-5]
DR   Ensembl; ENSMUST00000143203; ENSMUSP00000116191; ENSMUSG00000020546. [Q9WV89-1]
DR   GeneID; 20913; -.
DR   KEGG; mmu:20913; -.
DR   UCSC; uc007kwu.2; mouse. [Q9WV89-1]
DR   UCSC; uc007kwx.2; mouse. [Q9WV89-2]
DR   UCSC; uc007kwy.2; mouse. [Q9WV89-5]
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; CLQLDEV; -.
DR   OrthoDB; EOG7B5WVP; -.
DR   TreeFam; TF331084; -.
DR   ChiTaRS; STXBP4; mouse.
DR   EvolutionaryTrace; Q9WV89; -.
DR   NextBio; 299809; -.
DR   PRO; PR:Q9WV89; -.
DR   ArrayExpress; Q9WV89; -.
DR   Bgee; Q9WV89; -.
DR   CleanEx; MM_STXBP4; -.
DR   Genevestigator; Q9WV89; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045111; C:intermediate filament cytoskeleton; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
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-dom_pair.
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; SSF50156; 1.
DR   SUPFAM; SSF51045; SSF51045; 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
//
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