WIPF3_MOUSE
ID WIPF3_MOUSE Reviewed; 485 AA.
AC P0C7L0;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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 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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17573773; DOI=10.1111/j.1365-2443.2007.01088.x;
RA Suetsugu S., Banzai Y., Kato M., Fukami K., Kataoka Y., Takai Y.,
RA Yoshida N., Takenawa T.;
RT "Male-specific sterility caused by the loss of CR16.";
RL Genes Cells 12:721-733(2007).
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] OF 1-68 AND 203-485.
RC TISSUE=Brain, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Testis;
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 [5]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-57, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and 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: May be a regulator of cytoskeletal organization (Potential).
CC May have a role in spermatogenesis. {ECO:0000269|PubMed:17573773,
CC ECO:0000305}.
CC -!- SUBUNIT: Interacts with WASL, and monomeric and filamentous actin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17573773}. Note=In
CC hippocampal neurons colocalizes with WASL in the cell body, axons and
CC the growth cone (By similarity). Localizes to the actin filaments at
CC the Sertoli cell-spermatid junctions. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0C7L0-1; Sequence=Displayed;
CC Name=2; Synonyms=deltains;
CC IsoId=P0C7L0-2; Sequence=VSP_034030;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain and testis and
CC isoform 2 is expressed only in brain (at protein level).
CC {ECO:0000269|PubMed:17573773}.
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 -!- DISRUPTION PHENOTYPE: Mice are normal but males are sterile due to
CC defects in spermatogenesis. {ECO:0000269|PubMed:17573773}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CB723002; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC087841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BQ952480; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CB723002; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; P0C7L0; -.
DR STRING; 10090.ENSMUSP00000120240; -.
DR iPTMnet; P0C7L0; -.
DR PhosphoSitePlus; P0C7L0; -.
DR MaxQB; P0C7L0; -.
DR PaxDb; P0C7L0; -.
DR PRIDE; P0C7L0; -.
DR ProteomicsDB; 297847; -. [P0C7L0-1]
DR ProteomicsDB; 297848; -. [P0C7L0-2]
DR MGI; MGI:3044681; Wipf3.
DR eggNOG; KOG4462; Eukaryota.
DR InParanoid; P0C7L0; -.
DR PhylomeDB; P0C7L0; -.
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 ChiTaRS; Wipf3; mouse.
DR PRO; PR:P0C7L0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P0C7L0; protein.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
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; Alternative splicing; Cytoplasm; Developmental protein;
KW Differentiation; Methylation; Phosphoprotein; Reference proteome;
KW Spermatogenesis.
FT CHAIN 1..485
FT /note="WAS/WASL-interacting protein family member 3"
FT /id="PRO_0000337998"
FT DOMAIN 56..73
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 1..485
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 31..36
FT /note="Profilin-binding motif"
FT MOTIF 69..72
FT /note="RLRK"
FT MOTIF 424..448
FT /note="WASP-binding motif"
FT COMPBIAS 1..45
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..248
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NGB9"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NGB9"
FT VAR_SEQ 417..451
FT /note="DDFESKFTFHSMEDFPPPDEYKPCQKIYPSKVPRS -> G (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17573773"
FT /id="VSP_034030"
FT CONFLICT 482
FT /note="L -> LPV (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 49453 MW; 1ACA37E855D40447 CRC64;
MPVPPPPPPP PPPPPPPPPP LGAPPPPPLG APPPPPPPGP PVSTDTPSLR KPDLKGRSAL
LADIQQGTRL RKVTQINDRS APQIEGSKGT SKEGGAAGSN ARGGNTPPAL GDLFAGGFPV
LRPAGQRDVS GGKSGQGPGS RAPSPRLPIK AISGPLPAPA SPRLGNASET HSSARPVPPR
PSVPAPPPPT PPPPPPPPLP PASPIKAQLV SPPAPPTKVN PSVVPPPLPC APPLPPPPPT
PPPLPPASAL SDKAVRPQLA PLHLPPIPPP LPLLPPCGYP GLHSEPNSPA QEVREPPAPP
PPPPPPPPPP LPTYASCSSR TAVAPPPLPG ANNSGSETPP PLPPKSPSFQ TQKALPTPPG
APGPQAILQK KRRGPGTSGG KLNPPPAPPA RSPTTELSSK SQQPGGQLRN GGQHAIDDFE
SKFTFHSMED FPPPDEYKPC QKIYPSKVPR SRTPGSWLQA EAAGQSSDDI KSRNSQLSLK
ALPVR
