WIPF2_MOUSE
ID WIPF2_MOUSE Reviewed; 440 AA.
AC Q6PEV3;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=WAS/WASL-interacting protein family member 2;
DE AltName: Full=WASP-interacting protein-related protein;
DE AltName: Full=WIP-related protein;
GN Name=Wipf2; Synonyms=Wire;
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 [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [3]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-37, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Plays an active role in the formation of cell surface
CC protrusions downstream of activated PDGFB receptors. Plays an important
CC role in actin-microspike formation through cooperation with WASL. May
CC cooperate with WASP and WASL to induce mobilization and reorganization
CC of the actin filament system (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with WASL and WASP, and this interaction results in
CC cytoplasmic relocation of these two proteins along actin filaments.
CC Interacts with NCK2 resulting in the localization to sites of focal
CC adhesions (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Localized to stress fibers and bundles of actin filaments.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC057854; AAH57854.1; -; mRNA.
DR CCDS; CCDS25366.1; -.
DR RefSeq; NP_922922.1; NM_197940.2.
DR RefSeq; XP_006534119.1; XM_006534056.3.
DR RefSeq; XP_006534120.1; XM_006534057.3.
DR RefSeq; XP_006534121.1; XM_006534058.2.
DR RefSeq; XP_006534122.1; XM_006534059.3.
DR AlphaFoldDB; Q6PEV3; -.
DR SMR; Q6PEV3; -.
DR BioGRID; 212907; 7.
DR STRING; 10090.ENSMUSP00000046991; -.
DR iPTMnet; Q6PEV3; -.
DR PhosphoSitePlus; Q6PEV3; -.
DR EPD; Q6PEV3; -.
DR jPOST; Q6PEV3; -.
DR MaxQB; Q6PEV3; -.
DR PaxDb; Q6PEV3; -.
DR PeptideAtlas; Q6PEV3; -.
DR PRIDE; Q6PEV3; -.
DR ProteomicsDB; 299980; -.
DR Antibodypedia; 16452; 164 antibodies from 26 providers.
DR DNASU; 68524; -.
DR Ensembl; ENSMUST00000037480; ENSMUSP00000046991; ENSMUSG00000038013.
DR GeneID; 68524; -.
DR KEGG; mmu:68524; -.
DR UCSC; uc007lht.2; mouse.
DR CTD; 147179; -.
DR MGI; MGI:1924462; Wipf2.
DR VEuPathDB; HostDB:ENSMUSG00000038013; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00940000155557; -.
DR HOGENOM; CLU_039513_0_0_1; -.
DR InParanoid; Q6PEV3; -.
DR OMA; SGPGMKH; -.
DR OrthoDB; 1265175at2759; -.
DR PhylomeDB; Q6PEV3; -.
DR TreeFam; TF332135; -.
DR Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-MMU-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR BioGRID-ORCS; 68524; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Wipf2; mouse.
DR PRO; PR:Q6PEV3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PEV3; protein.
DR Bgee; ENSMUSG00000038013; Expressed in urinary bladder urothelium and 207 other tissues.
DR ExpressionAtlas; Q6PEV3; baseline and differential.
DR Genevisible; Q6PEV3; MM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030048; P:actin filament-based movement; IBA:GO_Central.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR028294; WIPF2.
DR PANTHER; PTHR23202:SF3; PTHR23202:SF3; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Methylation; Reference proteome.
FT CHAIN 1..440
FT /note="WAS/WASL-interacting protein family member 2"
FT /id="PRO_0000065976"
FT DOMAIN 36..53
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..52
FT /note="Binds actin"
FT /evidence="ECO:0000255"
FT REGION 56..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..265
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 440 AA; 46297 MW; 8DBE6864CABD52B4 CRC64;
MPIPPPPPPP PGPPPPPTFN QANTEQPKLS RDEQRNRGAL LQDICKGTKL KKVTNVNDRS
APVIEKPRGS SGGYGPGAAA LQPKGGLFQG GVPKLRPVGA KDASEAPAGK PALQVPSSRA
AAPRPPGSAA SGRPHDDTDS NRASLPELPR MQRPSLPDLS RPNTASGTGM KHSSSAPPPP
PPGRRANAPP TPLPLHSNKA QAYNREKPLP PTPGQRLHPG REGHPAPPPV KPPPSPVNIR
TGPSGQSLAP PPPPYRQPPG VPNGPSSPTN ESAPELPQRH NSLHRKTPGP VRGLAPPPPT
SATPSLLSNR PPPPAREPPS RGAAPPPPPP MIRNGARDAP PPPPPYRMHG SEPPSRGKPP
PPPSRTPAGP PPPPPPPLRN GHRDSITTVR SFLDDFESKY SFHPVEDFPA PEEYKHLQRV
YPSKTNRAAR GAPPLPPILR
