VINEX_MOUSE
ID VINEX_MOUSE Reviewed; 733 AA.
AC Q9R1Z8; Q62423;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vinexin;
DE AltName: Full=SH3 domain-containing protein SH3P3;
DE AltName: Full=SH3-containing adapter molecule 1;
DE Short=SCAM-1;
DE AltName: Full=Sorbin and SH3 domain-containing protein 3;
GN Name=Sorbs3; Synonyms=Scam1, Sh3d4;
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].
RC TISSUE=Embryo;
RX PubMed=9885244; DOI=10.1083/jcb.144.1.59;
RA Kioka N., Sakata S., Kawauchi T., Amachi T., Akiyama S.K., Okazaki K.,
RA Yaen C., Yamada K.M., Aota S.;
RT "Vinexin: a novel vinculin-binding protein with multiple SH3 domains
RT enhances actin cytoskeletal organization.";
RL J. Cell Biol. 144:59-69(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 559-733.
RC TISSUE=Embryo;
RX PubMed=9630982; DOI=10.1038/nbt0696-741;
RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT "Cloning of ligand targets: systematic isolation of SH3 domain-containing
RT proteins.";
RL Nat. Biotechnol. 14:741-744(1996).
RN [3]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DLG5.
RX PubMed=12657639; DOI=10.1074/jbc.m211004200;
RA Wakabayashi M., Ito T., Mitsushima M., Aizawa S., Ueda K., Amachi T.,
RA Kioka N.;
RT "Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase
RT family protein, with vinexin and beta-catenin at sites of cell-cell
RT contact.";
RL J. Biol. Chem. 278:21709-21714(2003).
RN [4]
RP PHOSPHORYLATION AT SER-594, INTERACTION WITH MAPK1/ERK2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15184391; DOI=10.1074/jbc.m402304200;
RA Mitsushima M., Suwa A., Amachi T., Ueda K., Kioka N.;
RT "Extracellular signal-regulated kinase activated by epidermal growth factor
RT and cell adhesion interacts with and phosphorylates vinexin.";
RL J. Biol. Chem. 279:34570-34577(2004).
RN [5]
RP INTERACTION WITH SOCS7.
RX PubMed=15242778; DOI=10.1016/j.yexcr.2004.04.002;
RA Martens N., Wery M., Wang P., Braet F., Gertler A., Hooghe R.,
RA Vandenhaute J., Hooghe-Peters E.L.;
RT "The suppressor of cytokine signaling (SOCS)-7 interacts with the actin
RT cytoskeleton through vinexin.";
RL Exp. Cell Res. 298:239-248(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-459, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
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).
CC -!- FUNCTION: Promotes up-regulation of actin stress fiber formation.
CC -!- SUBUNIT: Interacts with vinculin by the first two SH3 domains and the
CC proline rich region of vinculin. Binds to SOS (guanine nucleotide
CC exchange factor of RAS and RAC), through its third SH3 domain. The
CC formation of this complex is down-regulated by phosphorylation of SOS.
CC Interacts with SAFB2, INPPL1/SHIP2 and SRCIN1 (By similarity).
CC Interacts with DLG5 through its third SH3 domain. Interacts with SOCS7
CC and MAPK1/ERK2. Interacts with FASLG (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell junction.
CC Cytoplasm, cytoskeleton. Note=Localized at focal adhesion sites, cell-
CC cell junctions and cell-extracellular matrix junctions.
CC -!- PTM: Phosphorylated at Ser-594 by MAPK1/ERK2 during cell spreading.
CC {ECO:0000269|PubMed:15184391}.
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DR EMBL; AF064806; AAD32303.1; -; mRNA.
DR EMBL; U58889; AAC52642.1; -; mRNA.
DR CCDS; CCDS27249.1; -.
DR RefSeq; NP_035496.1; NM_011366.3.
DR AlphaFoldDB; Q9R1Z8; -.
DR SMR; Q9R1Z8; -.
DR BioGRID; 203212; 18.
DR ELM; Q9R1Z8; -.
DR IntAct; Q9R1Z8; 4.
DR MINT; Q9R1Z8; -.
DR STRING; 10090.ENSMUSP00000022682; -.
DR iPTMnet; Q9R1Z8; -.
DR PhosphoSitePlus; Q9R1Z8; -.
DR jPOST; Q9R1Z8; -.
DR MaxQB; Q9R1Z8; -.
DR PaxDb; Q9R1Z8; -.
DR PRIDE; Q9R1Z8; -.
DR ProteomicsDB; 299952; -.
DR Antibodypedia; 2849; 87 antibodies from 18 providers.
DR DNASU; 20410; -.
DR Ensembl; ENSMUST00000022682; ENSMUSP00000022682; ENSMUSG00000022091.
DR GeneID; 20410; -.
DR KEGG; mmu:20410; -.
DR UCSC; uc007unk.1; mouse.
DR CTD; 10174; -.
DR MGI; MGI:700013; Sorbs3.
DR VEuPathDB; HostDB:ENSMUSG00000022091; -.
DR eggNOG; KOG4225; Eukaryota.
DR GeneTree; ENSGT00940000160558; -.
DR HOGENOM; CLU_026296_0_0_1; -.
DR InParanoid; Q9R1Z8; -.
DR OMA; QVHREPR; -.
DR OrthoDB; 228183at2759; -.
DR PhylomeDB; Q9R1Z8; -.
DR TreeFam; TF320680; -.
DR Reactome; R-MMU-445355; Smooth Muscle Contraction.
DR BioGRID-ORCS; 20410; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sorbs3; mouse.
DR PRO; PR:Q9R1Z8; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9R1Z8; protein.
DR Bgee; ENSMUSG00000022091; Expressed in external carotid artery and 157 other tissues.
DR ExpressionAtlas; Q9R1Z8; baseline and differential.
DR Genevisible; Q9R1Z8; MM.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0017166; F:vinculin binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IEA:InterPro.
DR GO; GO:0031589; P:cell-substrate adhesion; IDA:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR CDD; cd11921; SH3_Vinexin_1; 1.
DR CDD; cd11924; SH3_Vinexin_2; 1.
DR CDD; cd11918; SH3_Vinexin_3; 1.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR003127; SoHo_dom.
DR InterPro; IPR028510; Vinexin.
DR InterPro; IPR035609; Vinexin_SH3_1.
DR InterPro; IPR035608; Vinexin_SH3_2.
DR InterPro; IPR035607; Vinexin_SH3_3.
DR PANTHER; PTHR14167:SF54; PTHR14167:SF54; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF14604; SH3_9; 2.
DR Pfam; PF02208; Sorb; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 3.
DR SMART; SM00459; Sorb; 1.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
DR PROSITE; PS50831; SOHO; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..733
FT /note="Vinexin"
FT /id="PRO_0000065831"
FT DOMAIN 164..232
FT /note="SoHo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00195"
FT DOMAIN 444..503
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 518..579
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 674..733
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..579
FT /note="Binds to vinculin"
FT REGION 584..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..733
FT /note="Binds to SOS"
FT /evidence="ECO:0000250"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 594
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:15184391"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60504"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60504"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60504"
SQ SEQUENCE 733 AA; 82349 MW; D7716FA1D4F0E3CE CRC64;
MARILGVGRS SASSLNNKED NESDVALLSP KDPNRVHTKE QLAHPASSNL DPSMQGLPAG
LSLDDFIPGH LRTHIGSSSR GTRVPVIRNG GSNTLNFQFH DPAPRTVCNG CPPPRRDGSL
NPDPAWYQTW PGPGSRPSMS PKPPASQHAQ NWSATWTKDS KRQDKRWVKY EGIGPVDESG
MPIAPRSSVD SPRDWYRRMF QQIHRKMPDL QLDWTLEDPP KVVSARASSA EPRHLGTLQR
PASRPGTTET SSGRNWNHSE ETSRNTFNYN FRPSSSGLHP PNQVPRHREK VENVWTEDSW
NQFLHELETG HKPKKPLVDD PVEKPAQPIE VLLERELAKL SAELDKDLRA IETRLPSPKN
SQAPRRPLEQ PGLEQQPSAR LSSAWRPNSP HAPYFSSSRP LSPHRMADGG GSPFLGRRDF
VYPSSAREPS ASERGSSPSR KEEKKRKAAR LKFDFQAQSP KELSLQKGDI VYIHKEVDKN
WLEGEHHGRL GIFPANYVEV LPADEIPKPI KPPTYQVLEY GDAVAQYTFK GDLEVELSFR
KGERICLIRK VNEHWYEGRI TGTGRQGIFP ASYVQINREP RLRLCDDGPQ LPASPNPTTT
AHLSSHSHPS SIPVDPTDWG GRTSPRRSAF PFPITLQEPR SQTQSLNTPG PTLSHPRATS
RPINLGPSSP NTEIHWTPYR AMYQYRPQNE DELELREGDR VDVMQQCDDG WFVGVSRRTQ
KFGTFPGNYV APV
