WIPF1_RAT
ID WIPF1_RAT Reviewed; 487 AA.
AC Q6IN36; Q8VDA4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=WAS/WASL-interacting protein family member 1;
DE AltName: Full=Wiskott-Aldrich syndrome protein-interacting protein;
DE Short=WASP-interacting protein;
GN Name=Wipf1; Synonyms=Waspip, Wip;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH WASL.
RC STRAIN=Fischer 344; TISSUE=Brain;
RX PubMed=11687573; DOI=10.1074/jbc.m104555200;
RA Vetterkind S., Miki H., Takenawa T., Klawitz I., Scheidtmann K.-H.,
RA Preuss U.;
RT "The rat homologue of Wiskott-Aldrich syndrome protein (WASP)-interacting
RT protein (WIP) associates with actin filaments, recruits N-WASP from the
RT nucleus, and mediates mobilization of actin from stress fibers in favor of
RT filopodia formation.";
RL J. Biol. Chem. 277:87-95(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, 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: Plays a role in the reorganization of the actin cytoskeleton.
CC Contributes with NCK1 and GRB2 in the recruitment and activation of
CC WASL. Plays a role in the formation of cell ruffles (By similarity).
CC May participate in regulating the subcellular localization of WASL,
CC resulting in the disassembly of stress fibers in favor of filopodia
CC formation. {ECO:0000250, ECO:0000269|PubMed:11687573}.
CC -!- SUBUNIT: Binds to WAS within the N-terminal region, at a site distinct
CC from the CDC42-binding site. Binds profilin and actin. Interacts with
CC DBNL (By similarity). Binds to WASL. Interacts with DBNL. Interacts
CC with FNBP1L (via the SH3 domain) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O43516, ECO:0000269|PubMed:11687573}.
CC -!- INTERACTION:
CC Q6IN36; P31016: Dlg4; NbExp=5; IntAct=EBI-6986245, EBI-375655;
CC Q6IN36; P21575: Dnm1; NbExp=2; IntAct=EBI-6986245, EBI-80070;
CC Q6IN36; O08816: Wasl; NbExp=2; IntAct=EBI-6986245, EBI-6142604;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:11687573}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:11687573}. Cell projection, ruffle {ECO:0000250}.
CC Note=Vesicle surfaces and along actin tails. Colocalizes with actin
CC stress fibers. When coexpressed with WASL, no longer associated with
CC actin filaments but accumulated in perinuclear and cortical areas like
CC WASL.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q6IN36-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Isoforms were differentially expressed. One isoform
CC was ubiquitously expressed, another was muscle-specific and another was
CC expressed in the liver, heart and testis.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
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DR EMBL; AJ303456; CAC22282.1; -; mRNA.
DR EMBL; BC072475; AAH72475.1; -; mRNA.
DR RefSeq; NP_476540.2; NM_057192.2.
DR AlphaFoldDB; Q6IN36; -.
DR SMR; Q6IN36; -.
DR DIP; DIP-42685N; -.
DR IntAct; Q6IN36; 11.
DR MINT; Q6IN36; -.
DR STRING; 10116.ENSRNOP00000024922; -.
DR iPTMnet; Q6IN36; -.
DR PhosphoSitePlus; Q6IN36; -.
DR PaxDb; Q6IN36; -.
DR GeneID; 117538; -.
DR KEGG; rno:117538; -.
DR UCSC; RGD:620887; rat. [Q6IN36-1]
DR CTD; 7456; -.
DR RGD; 620887; Wipf1.
DR eggNOG; KOG4462; Eukaryota.
DR InParanoid; Q6IN36; -.
DR OrthoDB; 1265175at2759; -.
DR PhylomeDB; Q6IN36; -.
DR TreeFam; TF332135; -.
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:Q6IN36; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005884; C:actin filament; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:RGD.
DR GO; GO:0030048; P:actin filament-based movement; ISO:RGD.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IDA:RGD.
DR GO; GO:0051707; P:response to other organism; ISO:RGD.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR003124; WH2_dom.
DR InterPro; IPR028295; WIP.
DR PANTHER; PTHR23202:SF32; PTHR23202:SF32; 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; Cell projection; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Methylation; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..487
FT /note="WAS/WASL-interacting protein family member 1"
FT /id="PRO_0000065943"
FT DOMAIN 32..49
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REPEAT 336..345
FT /note="XRSGPXPPXP motif 1"
FT REPEAT 358..367
FT /note="XRSGPXPPXP motif 2"
FT REPEAT 394..403
FT /note="XRSGPXPPXP motif 3"
FT REGION 1..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..48
FT /note="Binds actin"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..189
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..420
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 121
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 130
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1I7"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43516"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 329
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43516"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43516"
FT CONFLICT 139
FT /note="S -> P (in Ref. 2; AAH72475)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 49751 MW; BF505071BB7012FE CRC64;
MPVPPPPAPP PPPTFALANT EKPSLNKTEQ AGRNALLSDI SKGKKLKKTV TNDRSAPILD
KPKGAGGGYG GGSGGGGGGG SSGGGGNFGG GGPPGLGGLF QAGMPKLRST ANRDNDSGGS
RPPILPPGGR ATSAKPFSSP SGPGRFPAPS PGHRSGPPEP PRNRMPPPRP DVGSKPDSLP
PPVPNTPRPI PSSLHNRGSP AGLGAPRPPF PGNRGAAFGA GSVRQNLSSS SSPFPRPPLP
PTPSRALDDK PPPPPPPVGN RPSMHREAVP PPPSQNSKPP VPSTPRPGAG SQAPPPPPPS
RPGPPPLPPT SSDEIPRLPQ RNLSLTSPTP PLPSPGRSGP LPPPPTERPP PPVRDPPGRS
GPLPPPPPIN RNGSTARALP ATPQLPSRSG MDSPRSGPRP PLPPDRPGAG APPPPPPSTS
VRNGFQDSSC EDEWESRFYF HPISDLPPPE PYVPTTKTYP SKVARSESRS GSNRRERGAP
PLPPIPR
