WIPF3_RAT
ID WIPF3_RAT Reviewed; 485 AA.
AC Q9Z0G8; Q62775;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=WAS/WASL-interacting protein family member 3;
DE AltName: Full=Corticosteroids and regional expression protein 16;
GN Name=Wipf3; Synonyms=Cr16;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Fischer 344; TISSUE=Brain;
RX PubMed=8839352; DOI=10.1159/000126932;
RA Masters J.N., Cotman S.L., Osterburg H.H., Nichols N.R., Finch C.E.;
RT "Modulation of a novel RNA in brain neurons by glucocorticoid and
RT mineralocorticoid receptors.";
RL Neuroendocrinology 63:28-38(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=Fischer 344; TISSUE=Liver;
RX PubMed=8906616; DOI=10.1007/bf02736841;
RA Weiler M.C., Smith J.L., Masters J.N.;
RT "CR16, a novel proline-rich protein expressed in rat brain neurons, binds
RT to SH3 domains and is a MAP kinase substrate.";
RL J. Mol. Neurosci. 7:203-215(1996).
RN [3]
RP INDUCTION.
RX PubMed=2357595; DOI=10.1016/0361-9230(90)90004-j;
RA Nichols N.R., Masters J.N., Finch C.E.;
RT "Changes in gene expression in hippocampus in response to glucocorticoids
RT and stress.";
RL Brain Res. Bull. 24:659-662(1990).
RN [4]
RP INTERACTION WITH WASL AND ACTIN, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11553796; DOI=10.1073/pnas.211420498;
RA Ho H.-Y.H., Rohatgi R., Ma L., Kirschner M.W.;
RT "CR16 forms a complex with N-WASP in brain and is a novel member of a
RT conserved proline-rich actin-binding protein family.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11306-11311(2001).
RN [5]
RP DOMAIN WH2, KLKR MOTIF, AND PROFILIN-BINDING MOTIF.
RX PubMed=16182290; DOI=10.1016/j.febslet.2005.08.053;
RA Aspenstroem P.;
RT "The verprolin family of proteins: regulators of cell morphogenesis and
RT endocytosis.";
RL FEBS Lett. 579:5253-5259(2005).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF 58-ARG--LYS-61.
RX PubMed=17418095; DOI=10.1016/j.bbrc.2007.03.144;
RA Meng L., Rajmohan R., Yu S., Thanabalu T.;
RT "Actin binding and proline rich motifs of CR16 play redundant role in
RT growth of vrp1Delta cells.";
RL Biochem. Biophys. Res. Commun. 357:289-294(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May have a role in spermatogenesis (By similarity). May be a
CC regulator of cytoskeletal organization. {ECO:0000250,
CC ECO:0000269|PubMed:17418095}.
CC -!- SUBUNIT: Isoform 1 interacts with WASL (via WH1 domain), and monomeric
CC and filamentous actin. {ECO:0000269|PubMed:11553796}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11553796}. Note=In
CC hippocampal neurons colocalizes with WASL in the cell body, axons and
CC the growth cone.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z0G8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0G8-2; Sequence=VSP_034031;
CC -!- TISSUE SPECIFICITY: Detected mainly in brain and at lower levels in
CC heart and lung (at protein level). Also detected in testis but not in
CC kidney, liver or spleen. {ECO:0000269|PubMed:11553796,
CC ECO:0000269|PubMed:8839352}.
CC -!- INDUCTION: By aldosterone, corticosterone and RU28362 in hippocampus.
CC By corticosterone and RU28362 in cortex. The response to corticosterone
CC is slow. Does not respond to vibratory stress. May be regulated by both
CC the mineralocorticoid receptor and glucocorticoid receptor.
CC {ECO:0000269|PubMed:2357595, ECO:0000269|PubMed:8839352}.
CC -!- DOMAIN: The WH2 domain is found in a number of putative actin-binding
CC proteins. {ECO:0000269|PubMed:16182290}.
CC -!- DOMAIN: The profilin-binding motif has been implicated in the
CC interaction with profilin and SH3 domains.
CC {ECO:0000269|PubMed:16182290}.
CC -!- DOMAIN: The KLKR motif is essential for G-actin binding and for actin
CC polymerization. {ECO:0000269|PubMed:16182290}.
CC -!- MISCELLANEOUS: Suppress the growth and endocytosis defect of yeast
CC lacking VRP1 without correcting the actin patch polarization defect.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
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DR EMBL; U25281; AAA87791.1; -; mRNA.
DR EMBL; U31159; AAC99858.1; -; mRNA.
DR EMBL; U31168; AAC99859.1; -; Genomic_DNA.
DR EMBL; U31161; AAC99859.1; JOINED; Genomic_DNA.
DR EMBL; U31162; AAC99859.1; JOINED; Genomic_DNA.
DR EMBL; U31163; AAC99859.1; JOINED; Genomic_DNA.
DR EMBL; U31164; AAC99859.1; JOINED; Genomic_DNA.
DR EMBL; U31165; AAC99859.1; JOINED; Genomic_DNA.
DR EMBL; U31166; AAC99859.1; JOINED; Genomic_DNA.
DR EMBL; U31167; AAC99859.1; JOINED; Genomic_DNA.
DR RefSeq; NP_671744.1; NM_147211.1. [Q9Z0G8-2]
DR RefSeq; XP_008761099.1; XM_008762877.2. [Q9Z0G8-1]
DR AlphaFoldDB; Q9Z0G8; -.
DR CORUM; Q9Z0G8; -.
DR ELM; Q9Z0G8; -.
DR STRING; 10116.ENSRNOP00000012747; -.
DR iPTMnet; Q9Z0G8; -.
DR PhosphoSitePlus; Q9Z0G8; -.
DR PaxDb; Q9Z0G8; -.
DR PRIDE; Q9Z0G8; -.
DR Ensembl; ENSRNOT00000012755; ENSRNOP00000012755; ENSRNOG00000009571. [Q9Z0G8-2]
DR GeneID; 259242; -.
DR KEGG; rno:259242; -.
DR UCSC; RGD:708559; rat. [Q9Z0G8-1]
DR CTD; 644150; -.
DR RGD; 708559; Wipf3.
DR VEuPathDB; HostDB:ENSRNOG00000009571; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00940000160267; -.
DR HOGENOM; CLU_039513_1_0_1; -.
DR InParanoid; Q9Z0G8; -.
DR OMA; QVTAWTP; -.
DR OrthoDB; 1265175at2759; -.
DR PhylomeDB; Q9Z0G8; -.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q9Z0G8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009571; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; Q9Z0G8; RN.
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; IMP:RGD.
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_0000337999"
FT DOMAIN 45..62
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 20..25
FT /note="Profilin-binding motif"
FT MOTIF 58..61
FT /note="RLRK"
FT MOTIF 426..450
FT /note="WASP-binding motif"
FT COMPBIAS 1..33
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:A6NGB9"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NGB9"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NGB9"
FT VAR_SEQ 419..453
FT /note="DDFESKFTFHSMEDFPPPDEYKPGQKIYPSKVPRS -> G (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8839352"
FT /id="VSP_034031"
FT MUTAGEN 58..61
FT /note="RLRK->AAAA: Does not abolish the ability to suppress
FT the growth defect of yeast lacking VRP1."
FT /evidence="ECO:0000269|PubMed:17418095"
SQ SEQUENCE 485 AA; 49381 MW; 195673E854CB37D9 CRC64;
MPVPPPPPPP LPPPPPPLGA PPPPPPPGPP ISTDAPSLRK SDLKGRSALL ADIQQGTRLR
KVTQINDRSA PQIESSKGTS KEGGAAGSNA RGGSTPPALG DLFAGGFPVL RPAGQRDVAG
GKTGQGPGSR APSPRLPTKA ISGPLPAPAS PRLGNASDTH SSARPVPPRP SVPAPPPPTT
PPPPPPPPPP PPPPPLPPAS PIKAPSVSPP VPPTKGNPSA VPAPIPCVPP LPPPPPTPPP
LPPASALSEK AVRPQLAPLH LPPIPPPLPL LPPYGYPALH SEPSSPAQDV REPPAPPPPP
PPPPPPPPPP LPTYASCSPR AAVAPPPPPL PGSSNSGSET PPPLPPKSPS FQTQKALPTP
PGAPGPQIIL QKKRRGPGAG GGKLNPPPAP PARSPTTELS SKTQQPGGQL RNGGQHVIDD
FESKFTFHSM EDFPPPDEYK PGQKIYPSKV PRSRTPGSWL QAEAAGQSSD DIKTRNSQLS
LKALR
