WIPF1_MOUSE
ID WIPF1_MOUSE Reviewed; 493 AA.
AC Q8K1I7; Q3U0U8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH WASL.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12147689; DOI=10.1074/jbc.m204145200;
RA Benesch S., Lommel S., Steffen A., Stradal T.E.B., Scaplehorn N., Way M.,
RA Wehland J., Rottner K.;
RT "Phosphatidylinositol 4,5-biphosphate (PIP2)-induced vesicle movement
RT depends on N-WASP and involves Nck, WIP, and Grb2.";
RL J. Biol. Chem. 277:37771-37776(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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-143 AND SER-330, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, and Spleen;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DBNL.
RX PubMed=19910490; DOI=10.1091/mbc.e09-02-0106;
RA Cortesio C.L., Perrin B.J., Bennin D.A., Huttenlocher A.;
RT "Actin-binding protein-1 interacts with WASp-interacting protein to
RT regulate growth factor-induced dorsal ruffle formation.";
RL Mol. Biol. Cell 21:186-197(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-33; ARG-126 AND ARG-135, AND
RP IDENTIFICATION BY MASS 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: Plays a role in the reorganization of the actin cytoskeleton.
CC Contributes with NCK1 and GRB2 in the recruitment and activation of
CC WASL. May participate in regulating the subcellular localization of
CC WASL, resulting in the disassembly of stress fibers in favor of
CC filopodia formation (By similarity). Plays a role in the formation of
CC cell ruffles. {ECO:0000250, ECO:0000269|PubMed:12147689,
CC ECO:0000269|PubMed:19910490}.
CC -!- SUBUNIT: Binds to WAS within the N-terminal region, at a site distinct
CC from the CDC42-binding site. Binds profilin and actin (By similarity).
CC Binds to WASL. Interacts with DBNL. Interacts with DBNL. Interacts with
CC FNBP1L (via the SH3 domain) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O43516, ECO:0000269|PubMed:12147689,
CC ECO:0000269|PubMed:19910490}.
CC -!- INTERACTION:
CC Q8K1I7; P70315: Was; NbExp=3; IntAct=EBI-644216, EBI-644195;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell projection, ruffle
CC {ECO:0000269|PubMed:12147689, ECO:0000269|PubMed:19910490}.
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 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Recruited to PIP5K-induced vesicle surfaces in the
CC absence of functional WASL.
CC -!- SIMILARITY: Belongs to the verprolin family. {ECO:0000305}.
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DR EMBL; AJ437262; CAD24773.1; -; mRNA.
DR EMBL; AK031046; BAC27228.1; -; mRNA.
DR EMBL; AK156547; BAE33753.1; -; mRNA.
DR EMBL; BC049788; AAH49788.1; -; mRNA.
DR CCDS; CCDS16131.1; -.
DR RefSeq; NP_001276651.1; NM_001289722.1.
DR RefSeq; NP_001276652.1; NM_001289723.1.
DR RefSeq; NP_694778.1; NM_153138.4.
DR RefSeq; XP_006499187.1; XM_006499124.3.
DR RefSeq; XP_006499190.1; XM_006499127.2.
DR RefSeq; XP_011237735.1; XM_011239433.2.
DR AlphaFoldDB; Q8K1I7; -.
DR SMR; Q8K1I7; -.
DR BioGRID; 229611; 2.
DR CORUM; Q8K1I7; -.
DR DIP; DIP-37798N; -.
DR IntAct; Q8K1I7; 8.
DR STRING; 10090.ENSMUSP00000092268; -.
DR iPTMnet; Q8K1I7; -.
DR PhosphoSitePlus; Q8K1I7; -.
DR EPD; Q8K1I7; -.
DR jPOST; Q8K1I7; -.
DR MaxQB; Q8K1I7; -.
DR PaxDb; Q8K1I7; -.
DR PeptideAtlas; Q8K1I7; -.
DR PRIDE; Q8K1I7; -.
DR ProteomicsDB; 299786; -.
DR Antibodypedia; 4053; 157 antibodies from 34 providers.
DR DNASU; 215280; -.
DR Ensembl; ENSMUST00000094681; ENSMUSP00000092268; ENSMUSG00000075284.
DR Ensembl; ENSMUST00000102679; ENSMUSP00000099740; ENSMUSG00000075284.
DR Ensembl; ENSMUST00000102680; ENSMUSP00000099741; ENSMUSG00000075284.
DR GeneID; 215280; -.
DR KEGG; mmu:215280; -.
DR UCSC; uc008kcu.2; mouse.
DR CTD; 7456; -.
DR MGI; MGI:2178801; Wipf1.
DR VEuPathDB; HostDB:ENSMUSG00000075284; -.
DR eggNOG; KOG4462; Eukaryota.
DR GeneTree; ENSGT00910000144296; -.
DR HOGENOM; CLU_041032_0_0_1; -.
DR InParanoid; Q8K1I7; -.
DR OMA; NTPRPVQ; -.
DR OrthoDB; 1265175at2759; -.
DR PhylomeDB; Q8K1I7; -.
DR TreeFam; TF332135; -.
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 BioGRID-ORCS; 215280; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Wipf1; mouse.
DR PRO; PR:Q8K1I7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8K1I7; protein.
DR Bgee; ENSMUSG00000075284; Expressed in granulocyte and 248 other tissues.
DR ExpressionAtlas; Q8K1I7; baseline and differential.
DR Genevisible; Q8K1I7; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005884; C:actin filament; IDA:MGI.
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:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0030048; P:actin filament-based movement; IDA:MGI.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
DR GO; GO:0051707; P:response to other organism; IMP:MGI.
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; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Methylation; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..493
FT /note="WAS/WASL-interacting protein family member 1"
FT /id="PRO_0000065942"
FT DOMAIN 32..49
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REPEAT 342..351
FT /note="XRSGPXPPXP motif 1"
FT REPEAT 364..373
FT /note="XRSGPXPPXP motif 2"
FT REPEAT 400..409
FT /note="XRSGPXPPXP motif 3"
FT REGION 1..493
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 145..194
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 126
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 135
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43516"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43516"
SQ SEQUENCE 493 AA; 50080 MW; 0BADBE69463B5960 CRC64;
MPVPPPPAPP PPPTFALANT EKPTLNKTEQ AGRNALLSDI SKGKKLKKTV TNDRSAPILD
KPKGAGASAG GYGGGGGGGG GGGGGGGGSG GNFGGGGPPG LGGLFQAGMP KLRSTANRDN
DSGGSRPPIL PPGGRATSAK PFSPPSGPGR FPAPSPGHRS GPPEPPRNRM PPPRPDVGSK
PDSLPPPVPN TPRPVPSSLH NRGSPAGLGA PRPPFPGNRG AAFGAGSARQ NPSGSSSPFP
RPPLPPTPSR ALDDKPPPPP PPVGNRPSMH REAVPPPPSQ TSKPPVPSTP RPGLGSQAPP
PPPPPSRPGP PPLPPASNDE IPRLPQRNLS LTSSAPPLPS PGRSGPLPPP PSERPPPPVR
DPPGRSGPLP PPPPINRNGS TARALPATPQ LPSRSGMDSP RSGPRPPLPP DRPGAGAPPP
PPPSTSVRNG FQDSSCEDEW ESRFYFHPIS DLPPPEPYVP TTKTYPSKLA RNESRSGSNR
RERGAPPLPP IPR
