WIPF3_HUMAN
ID WIPF3_HUMAN Reviewed; 483 AA.
AC A6NGB9; B8ZZV2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 4.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=WAS/WASL-interacting protein family member 3;
DE AltName: Full=Corticosteroids and regional expression protein 16 homolog;
GN Name=WIPF3; Synonyms=CR16;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-483.
RA Ebert L., Heil O., Hennig S., Neubert P., Partsch E., Peters M.,
RA Radelof U., Schneider D., Korn B.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SYNTHESIS OF 420-430.
RX PubMed=12372256; DOI=10.1016/s0960-9822(02)01112-0;
RA Zettl M., Way M.;
RT "The WH1 and EVH1 domains of WASP and Ena/VASP family members bind distinct
RT sequence motifs.";
RL Curr. Biol. 12:1617-1622(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-202 AND SER-383, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-46, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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: May be a regulator of cytoskeletal organization. May have a
CC role in spermatogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with WASL, and monomeric and filamentous actin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In hippocampal neurons
CC colocalizes with WASL in the cell body, axons and the growth cone.
CC {ECO:0000250}.
CC -!- DOMAIN: The WH2 domain is found in a number of putative actin-binding
CC proteins. {ECO:0000250}.
CC -!- DOMAIN: The profilin-binding motif has been implicated in the
CC interaction with profilin and SH3 domains. {ECO:0000250}.
CC -!- DOMAIN: The KLKR motif is essential for G-actin binding and for actin
CC polymerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
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DR EMBL; AC004912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471073; EAW93924.1; -; Genomic_DNA.
DR EMBL; BX107905; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS56472.1; -.
DR RefSeq; NP_001073998.2; NM_001080529.2.
DR AlphaFoldDB; A6NGB9; -.
DR BioGRID; 569353; 12.
DR ELM; A6NGB9; -.
DR IntAct; A6NGB9; 4.
DR STRING; 9606.ENSP00000242140; -.
DR GlyGen; A6NGB9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NGB9; -.
DR PhosphoSitePlus; A6NGB9; -.
DR BioMuta; WIPF3; -.
DR EPD; A6NGB9; -.
DR jPOST; A6NGB9; -.
DR MassIVE; A6NGB9; -.
DR PaxDb; A6NGB9; -.
DR PeptideAtlas; A6NGB9; -.
DR PRIDE; A6NGB9; -.
DR ProteomicsDB; 1115; -.
DR ProteomicsDB; 7445; -.
DR Antibodypedia; 48600; 25 antibodies from 11 providers.
DR DNASU; 644150; -.
DR Ensembl; ENST00000242140.10; ENSP00000242140.6; ENSG00000122574.12.
DR GeneID; 644150; -.
DR KEGG; hsa:644150; -.
DR MANE-Select; ENST00000242140.10; ENSP00000242140.6; NM_001080529.3; NP_001073998.2.
DR UCSC; uc022aaz.1; human.
DR CTD; 644150; -.
DR DisGeNET; 644150; -.
DR GeneCards; WIPF3; -.
DR HGNC; HGNC:22004; WIPF3.
DR HPA; ENSG00000122574; Tissue enhanced (brain, ovary).
DR MIM; 612432; gene.
DR neXtProt; NX_A6NGB9; -.
DR OpenTargets; ENSG00000122574; -.
DR PharmGKB; PA162409231; -.
DR VEuPathDB; HostDB:ENSG00000122574; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00940000160267; -.
DR InParanoid; A6NGB9; -.
DR OMA; QVTAWTP; -.
DR OrthoDB; 1265175at2759; -.
DR PhylomeDB; A6NGB9; -.
DR PathwayCommons; A6NGB9; -.
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-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; A6NGB9; -.
DR BioGRID-ORCS; 644150; 14 hits in 1078 CRISPR screens.
DR GenomeRNAi; 644150; -.
DR Pharos; A6NGB9; Tdark.
DR PRO; PR:A6NGB9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A6NGB9; protein.
DR Bgee; ENSG00000122574; Expressed in tibialis anterior and 160 other tissues.
DR ExpressionAtlas; A6NGB9; baseline and differential.
DR Genevisible; A6NGB9; 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:0017124; F:SH3 domain binding; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR003124; WH2_dom.
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; Developmental protein; Differentiation;
KW Methylation; Phosphoprotein; Reference proteome; Spermatogenesis.
FT CHAIN 1..483
FT /note="WAS/WASL-interacting protein family member 3"
FT /id="PRO_0000337997"
FT DOMAIN 45..62
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 3..8
FT /note="Profilin-binding motif"
FT MOTIF 11..16
FT /note="Profilin-binding motif"
FT MOTIF 20..25
FT /note="Profilin-binding motif"
FT MOTIF 58..61
FT /note="RLRK"
FT MOTIF 424..448
FT /note="WASP-binding motif"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..202
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..241
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..334
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 321
FT /note="E -> G (in dbSNP:rs3750092)"
FT /id="VAR_043729"
SQ SEQUENCE 483 AA; 49458 MW; 78A600C2FE4F9CCE CRC64;
MPVPPPPPPP LPPPPPPLGA PPPPPPSAPP VSTDTSSLRR ADPKGRSALL ADIQQGTRLR
KVTQINDRSA PQIESSKGTN KEGGGSANTR GASTPPTLGD LFAGGFPVLR PAGQRDVAGG
KTGQGPGSRA PSPRLPNKTI SGPLIPPASP RLGNTSEAHG AARTAPPRPN VPAPPPPTPP
PPPPPLPPPL PSSSPIKTPL VSPPGPLTKG NLPVVAPPVP CAPPPPPPPP PPTPPPLPPA
SVLSDKAVKP QLAPLHLPPI PPPLPLLPPC GYPGLKAEPA SPAQDAQEPP APPPPLPPYA
SCSPRASLPA PPLPGVNSSS ETPPPLPPKS PSFQAPPQKA GAQALPAPPA PPGSQPFLQK
KRHGRPGAGG GKLNPPPAPP ARSPTTELSS KSQQATAWTP TQQPGGQLRN GSLHIIDDFE
SKFTFHSVED FPPPDEYKPC QKIYPSKIPR SRTPGPWLQA EAVGQSSDDI KGRNSQLSLK
TLR
