STXB4_MOUSE
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 03-AUG-2022, entry version 151.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT 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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., 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 insulin
RT 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., Uehara Y.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
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 from
CC the cytoplasm to the plasma membrane. Inhibits the translocation of
CC SLC2A4 from intracellular vesicles to the plasma membrane by STX4A
CC binding and preventing the interaction between STX4A and VAMP2.
CC Stimulation with insulin disrupts the interaction with STX4A, leading
CC to increased levels of SLC2A4 at the plasma membrane. May also play a
CC role in the regulation of insulin release by pancreatic beta cells
CC after stimulation by glucose. {ECO:0000269|PubMed:10394363,
CC ECO:0000269|PubMed:12855681}.
CC -!- SUBUNIT: Interacts with STX4A. {ECO:0000269|PubMed:10394363}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10394363}.
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 Name=4;
CC IsoId=Q9WV89-4; Sequence=VSP_017184, VSP_017185;
CC Name=5;
CC IsoId=Q9WV89-5; Sequence=VSP_017181, VSP_017182;
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart, testis,
CC adipocytes and pancreatic islet cells. {ECO:0000269|PubMed:10394363,
CC ECO:0000269|PubMed:12855681}.
CC -!- PTM: Phosphorylated on Ser-99 by PKB/AKT2 after insulin treatment.
CC Phosphorylation on Ser-99 abolishes the interaction with STX4A.
CC {ECO:0000269|PubMed:15753124}.
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DR EMBL; AF152924; AAD43533.1; -; mRNA.
DR EMBL; AL646046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032881; AAH32881.1; -; mRNA.
DR EMBL; AK138499; BAE23686.1; -; mRNA.
DR CCDS; CCDS25242.1; -. [Q9WV89-1]
DR RefSeq; NP_035635.1; NM_011505.2. [Q9WV89-1]
DR PDB; 1WI4; NMR; -; A=12-107.
DR PDBsum; 1WI4; -.
DR AlphaFoldDB; Q9WV89; -.
DR SMR; Q9WV89; -.
DR BioGRID; 203567; 1.
DR STRING; 10090.ENSMUSP00000116191; -.
DR iPTMnet; Q9WV89; -.
DR PhosphoSitePlus; Q9WV89; -.
DR MaxQB; Q9WV89; -.
DR PaxDb; Q9WV89; -.
DR PeptideAtlas; Q9WV89; -.
DR PRIDE; Q9WV89; -.
DR ProteomicsDB; 254773; -. [Q9WV89-1]
DR ProteomicsDB; 254774; -. [Q9WV89-2]
DR ProteomicsDB; 254775; -. [Q9WV89-3]
DR ProteomicsDB; 254776; -. [Q9WV89-4]
DR ProteomicsDB; 254777; -. [Q9WV89-5]
DR Antibodypedia; 3574; 120 antibodies from 26 providers.
DR DNASU; 20913; -.
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 VEuPathDB; HostDB:ENSMUSG00000020546; -.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00390000002226; -.
DR HOGENOM; CLU_022133_1_0_1; -.
DR InParanoid; Q9WV89; -.
DR OMA; DQHQALR; -.
DR OrthoDB; 307920at2759; -.
DR PhylomeDB; Q9WV89; -.
DR TreeFam; TF331084; -.
DR BioGRID-ORCS; 20913; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Stxbp4; mouse.
DR EvolutionaryTrace; Q9WV89; -.
DR PRO; PR:Q9WV89; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9WV89; protein.
DR Bgee; ENSMUSG00000020546; Expressed in vas deferens and 235 other tissues.
DR ExpressionAtlas; Q9WV89; baseline and differential.
DR Genevisible; Q9WV89; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:MGI.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; IDA:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
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; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..557
FT /note="Syntaxin-binding protein 4"
FT /id="PRO_0000076331"
FT DOMAIN 19..105
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 500..533
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 142..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..408
FT /evidence="ECO:0000255"
FT COMPBIAS 142..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZWJ1"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZWJ1"
FT MOD_RES 99
FT /note="Phosphoserine; by PKB/AKT2"
FT /evidence="ECO:0000269|PubMed:15753124,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZWJ1"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZWJ1"
FT VAR_SEQ 195..226
FT /note="DIAPAWTDDDSGPQGKISLNPSVRLKAEKLEM -> AHMERKKRHESSGQSK
FT MWHWSCSMMKVEVFIP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017179"
FT VAR_SEQ 227..557
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017180"
FT VAR_SEQ 227..258
FT /note="ALNYLGIQPTKEQREALREQVQADSKGTVSFG -> VNPLKKNHFLHKTAGK
FT NCLVLGEEDIGESLVS (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_017181"
FT VAR_SEQ 259..557
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_017182"
FT VAR_SEQ 502..557
FT /note="LPYGWEEAYTADGIKYFINHVTQTTSWIHPVMSALNLSCAEESEEDCPRELT
FT DPKS -> KLSLSSSSSPSSSSSFSSSSSCNLLNKAEERP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017183"
FT VAR_SEQ 520
FT /note="N -> K (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017184"
FT VAR_SEQ 521..557
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017185"
FT MUTAGEN 97
FT /note="S->F: No effect."
FT /evidence="ECO:0000269|PubMed:15753124"
FT MUTAGEN 99
FT /note="S->F: Abolishes phosphorylation by PKB/AKT2."
FT /evidence="ECO:0000269|PubMed:15753124"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:1WI4"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1WI4"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1WI4"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:1WI4"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:1WI4"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1WI4"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1WI4"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:1WI4"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1WI4"
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
