WIPF2_HUMAN
ID WIPF2_HUMAN Reviewed; 440 AA.
AC Q8TF74; A8K0L3; Q658J8; Q71RE1; Q8TE44;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=WAS/WASL-interacting protein family member 2;
DE AltName: Full=WASP-interacting protein-related protein;
DE AltName: Full=WIP- and CR16-homologous protein;
DE AltName: Full=WIP-related protein;
GN Name=WIPF2; Synonyms=WICH, WIRE; ORFNames=PP10631;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH WASL.
RX PubMed=11829459; DOI=10.1006/bbrc.2002.6406;
RA Kato M., Miki H., Kurita S., Endo T., Nakagawa H., Miyamoto S.,
RA Takenawa T.;
RT "WICH, a novel verprolin homology domain-containing protein that functions
RT cooperatively with N-WASP in actin-microspike formation.";
RL Biochem. Biophys. Res. Commun. 291:41-47(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH WASP; WASL; NCK2 AND PFN1.
RX PubMed=12213210; DOI=10.1006/excr.2002.5576;
RA Aspenstroem P.;
RT "The WASP-binding protein WIRE has a role in the regulation of the actin
RT filament system downstream of the platelet-derived growth factor
RT receptor.";
RL Exp. Cell Res. 279:21-33(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Cerebellum, Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
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. {ECO:0000269|PubMed:11829459,
CC ECO:0000269|PubMed:12213210}.
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. No interaction was seen with WASF2 and WASF3.
CC {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}.
CC -!- INTERACTION:
CC Q8TF74; P62993: GRB2; NbExp=6; IntAct=EBI-2850112, EBI-401755;
CC Q8TF74; O60504: SORBS3; NbExp=3; IntAct=EBI-2850112, EBI-741237;
CC Q8TF74; A6NH52: TVP23A; NbExp=3; IntAct=EBI-2850112, EBI-13296313;
CC Q8TF74; O00401: WASL; NbExp=5; IntAct=EBI-2850112, EBI-957615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11829459, ECO:0000269|PubMed:12213210}.
CC Note=Localized to stress fibers and bundles of actin filaments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TF74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TF74-2; Sequence=VSP_012967;
CC -!- TISSUE SPECIFICITY: Expressed mainly in brain, colon, lung and stomach
CC (at protein level). Ubiquitously expressed, with high expression in
CC brain, kidney, lung, and placenta. {ECO:0000269|PubMed:11829459,
CC ECO:0000269|PubMed:12213210}.
CC -!- MISCELLANEOUS: Access to the profilin-binding site is masked in the
CC full-length protein.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ15232.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB043786; BAB85113.1; -; mRNA.
DR EMBL; AJ431177; CAD24007.1; -; mRNA.
DR EMBL; AF370396; AAQ15232.1; ALT_FRAME; mRNA.
DR EMBL; AK289578; BAF82267.1; -; mRNA.
DR EMBL; AK289779; BAF82468.1; -; mRNA.
DR EMBL; AK290301; BAF82990.1; -; mRNA.
DR EMBL; AK315836; BAF98727.1; -; mRNA.
DR EMBL; AL834239; CAH56360.1; -; mRNA.
DR EMBL; BC065551; AAH65551.1; -; mRNA.
DR CCDS; CCDS11364.1; -. [Q8TF74-1]
DR PIR; JC7807; JC7807.
DR RefSeq; NP_573571.1; NM_133264.4. [Q8TF74-1]
DR RefSeq; XP_005257140.1; XM_005257083.2. [Q8TF74-1]
DR RefSeq; XP_005257141.1; XM_005257084.2. [Q8TF74-1]
DR RefSeq; XP_011522715.1; XM_011524413.1. [Q8TF74-2]
DR AlphaFoldDB; Q8TF74; -.
DR SMR; Q8TF74; -.
DR BioGRID; 127043; 30.
DR ELM; Q8TF74; -.
DR IntAct; Q8TF74; 16.
DR MINT; Q8TF74; -.
DR STRING; 9606.ENSP00000320924; -.
DR GlyGen; Q8TF74; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8TF74; -.
DR PhosphoSitePlus; Q8TF74; -.
DR BioMuta; WIPF2; -.
DR DMDM; 60390855; -.
DR EPD; Q8TF74; -.
DR jPOST; Q8TF74; -.
DR MassIVE; Q8TF74; -.
DR MaxQB; Q8TF74; -.
DR PaxDb; Q8TF74; -.
DR PeptideAtlas; Q8TF74; -.
DR PRIDE; Q8TF74; -.
DR ProteomicsDB; 74574; -. [Q8TF74-1]
DR ProteomicsDB; 74575; -. [Q8TF74-2]
DR Antibodypedia; 16452; 164 antibodies from 26 providers.
DR DNASU; 147179; -.
DR Ensembl; ENST00000323571.9; ENSP00000320924.4; ENSG00000171475.14. [Q8TF74-1]
DR Ensembl; ENST00000583130.5; ENSP00000462350.1; ENSG00000171475.14. [Q8TF74-1]
DR Ensembl; ENST00000585043.5; ENSP00000462826.1; ENSG00000171475.14. [Q8TF74-1]
DR GeneID; 147179; -.
DR KEGG; hsa:147179; -.
DR MANE-Select; ENST00000323571.9; ENSP00000320924.4; NM_133264.5; NP_573571.1.
DR UCSC; uc002hug.2; human. [Q8TF74-1]
DR CTD; 147179; -.
DR DisGeNET; 147179; -.
DR GeneCards; WIPF2; -.
DR HGNC; HGNC:30923; WIPF2.
DR HPA; ENSG00000171475; Low tissue specificity.
DR MIM; 609692; gene.
DR neXtProt; NX_Q8TF74; -.
DR OpenTargets; ENSG00000171475; -.
DR PharmGKB; PA162409210; -.
DR VEuPathDB; HostDB:ENSG00000171475; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00940000155557; -.
DR HOGENOM; CLU_039513_0_0_1; -.
DR InParanoid; Q8TF74; -.
DR OMA; SGPGMKH; -.
DR OrthoDB; 1265175at2759; -.
DR PhylomeDB; Q8TF74; -.
DR TreeFam; TF332135; -.
DR PathwayCommons; Q8TF74; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q8TF74; -.
DR BioGRID-ORCS; 147179; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; WIPF2; human.
DR GeneWiki; WIPF2; -.
DR GenomeRNAi; 147179; -.
DR Pharos; Q8TF74; Tbio.
DR PRO; PR:Q8TF74; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8TF74; protein.
DR Bgee; ENSG00000171475; Expressed in secondary oocyte and 211 other tissues.
DR ExpressionAtlas; Q8TF74; baseline and differential.
DR Genevisible; Q8TF74; HS.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; Alternative splicing; Cytoplasm; Cytoskeleton; Methylation;
KW Reference proteome.
FT CHAIN 1..440
FT /note="WAS/WASL-interacting protein family member 2"
FT /id="PRO_0000065975"
FT DOMAIN 36..53
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..36
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..387
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 206..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:0000250|UniProtKB:Q6PEV3"
FT VAR_SEQ 1..150
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_012967"
FT CONFLICT 82
FT /note="Q -> H (in Ref. 2; CAD24007)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 46289 MW; 7386B44F995AD798 CRC64;
MPIPPPPPPP PGPPPPPTFH QANTEQPKLS RDEQRGRGAL LQDICKGTKL KKVTNINDRS
APILEKPKGS SGGYGSGGAA LQPKGGLFQG GVLKLRPVGA KDGSENLAGK PALQIPSSRA
AAPRPPVSAA SGRPQDDTDS SRASLPELPR MQRPSLPDLS RPNTTSSTGM KHSSSAPPPP
PPGRRANAPP TPLPMHSSKA PAYNREKPLP PTPGQRLHPG REGPPAPPPV KPPPSPVNIR
TGPSGQSLAP PPPPYRQPPG VPNGPSSPTN ESAPELPQRH NSLHRKTPGP VRGLAPPPPT
SASPSLLSNR PPPPARDPPS RGAAPPPPPP VIRNGARDAP PPPPPYRMHG SEPPSRGKPP
PPPSRTPAGP PPPPPPPLRN GHRDSITTVR SFLDDFESKY SFHPVEDFPA PEEYKHFQRI
YPSKTNRAAR GAPPLPPILR
