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   27-MAR-2024, entry version 158.
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; 10090-ENSMUSP00000092268; -.
DR   PeptideAtlas; Q8K1I7; -.
DR   ProteomicsDB; 299786; -.
DR   Pumba; Q8K1I7; -.
DR   Antibodypedia; 4053; 180 antibodies from 34 providers.
DR   DNASU; 215280; -.
DR   Ensembl; ENSMUST00000094681.11; ENSMUSP00000092268.5; ENSMUSG00000075284.11.
DR   Ensembl; ENSMUST00000102679.8; ENSMUSP00000099740.2; ENSMUSG00000075284.11.
DR   Ensembl; ENSMUST00000102680.8; ENSMUSP00000099741.2; ENSMUSG00000075284.11.
DR   GeneID; 215280; -.
DR   KEGG; mmu:215280; -.
DR   UCSC; uc008kcu.2; mouse.
DR   AGR; MGI:2178801; -.
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; EPQRSRM; -.
DR   OrthoDB; 5324507at2759; -.
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   BioGRID-ORCS; 215280; 2 hits in 77 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 250 other cell types or tissues.
DR   ExpressionAtlas; Q8K1I7; baseline and differential.
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:0044183; F:protein folding chaperone; ISO:MGI.
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:0046827; P:positive regulation of protein export from nucleus; ISO:MGI.
DR   GO; GO:0051707; P:response to other organism; IMP:MGI.
DR   CDD; cd22076; WH2_WAS_WASL-1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR48226; OS06G0326200 PROTEIN; 1.
DR   PANTHER; PTHR48226:SF1; WAS_WASL-INTERACTING PROTEIN FAMILY MEMBER 1; 1.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
DR   Genevisible; Q8K1I7; MM.
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
//