PPIP2_MOUSE
ID PPIP2_MOUSE Reviewed; 334 AA.
AC Q99M15; Q6GTF6; Q9Z189;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Proline-serine-threonine phosphatase-interacting protein 2;
DE Short=PEST phosphatase-interacting protein 2;
DE AltName: Full=Macrophage actin-associated tyrosine-phosphorylated protein;
DE AltName: Full=pp37;
GN Name=Pstpip2; Synonyms=Mayp;
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], AND PROTEIN SEQUENCE OF 2-10; 52-61; 76-81;
RP 104-111; 117-128; 173-176; 182-196; 201-210; 224-228; 264-271 AND 273-287.
RX PubMed=9804836; DOI=10.1074/jbc.273.46.30638;
RA Yeung Y.-G., Soldera S., Stanley E.R.;
RT "A novel macrophage actin-associated protein (MAYP) is tyrosine
RT phosphorylated following colony stimulating factor-1 stimulation.";
RL J. Biol. Chem. 273:30638-30642(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Skin;
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 STRAIN=FVB/N; TISSUE=Mammary gland;
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 TYR-323 AND TYR-329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [5]
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).
CC -!- FUNCTION: Binds to F-actin. May be involved in regulation of the actin
CC cytoskeleton.
CC -!- INTERACTION:
CC Q99M15; Q61152: Ptpn18; NbExp=7; IntAct=EBI-8653964, EBI-7074223;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in macrophage-containing tissues,
CC including bone marrow, spleen, liver, kidney, intestine and brain.
CC -!- PTM: Phosphorylated on tyrosine.
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DR EMBL; Y18101; CAA77027.1; -; mRNA.
DR EMBL; AK132418; BAE21158.1; -; mRNA.
DR EMBL; AK154724; BAE32788.1; -; mRNA.
DR EMBL; AK157994; BAE34306.1; -; mRNA.
DR EMBL; BC002123; AAH02123.1; -; mRNA.
DR EMBL; BC057654; AAH57654.1; -; mRNA.
DR CCDS; CCDS37868.1; -.
DR RefSeq; NP_038859.3; NM_013831.4.
DR AlphaFoldDB; Q99M15; -.
DR SMR; Q99M15; -.
DR IntAct; Q99M15; 3.
DR MINT; Q99M15; -.
DR STRING; 10090.ENSMUSP00000110389; -.
DR iPTMnet; Q99M15; -.
DR PhosphoSitePlus; Q99M15; -.
DR MaxQB; Q99M15; -.
DR PaxDb; Q99M15; -.
DR PRIDE; Q99M15; -.
DR ProteomicsDB; 291834; -.
DR Antibodypedia; 22437; 94 antibodies from 20 providers.
DR DNASU; 19201; -.
DR Ensembl; ENSMUST00000114741; ENSMUSP00000110389; ENSMUSG00000025429.
DR GeneID; 19201; -.
DR KEGG; mmu:19201; -.
DR UCSC; uc008fry.1; mouse.
DR CTD; 9050; -.
DR MGI; MGI:1335088; Pstpip2.
DR VEuPathDB; HostDB:ENSMUSG00000025429; -.
DR eggNOG; KOG2398; Eukaryota.
DR GeneTree; ENSGT00940000158788; -.
DR HOGENOM; CLU_038196_1_0_1; -.
DR InParanoid; Q99M15; -.
DR OMA; EEADQNM; -.
DR OrthoDB; 727724at2759; -.
DR PhylomeDB; Q99M15; -.
DR TreeFam; TF313677; -.
DR BioGRID-ORCS; 19201; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Pstpip2; mouse.
DR PRO; PR:Q99M15; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q99M15; protein.
DR Bgee; ENSMUSG00000025429; Expressed in granulocyte and 58 other tissues.
DR ExpressionAtlas; Q99M15; baseline and differential.
DR Genevisible; Q99M15; MM.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IEA:InterPro.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR CDD; cd07672; F-BAR_PSTPIP2; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR030106; PSTPIP2.
DR InterPro; IPR042694; PSTPIP2_F-BAR.
DR PANTHER; PTHR23065:SF9; PTHR23065:SF9; 1.
DR Pfam; PF00611; FCH; 1.
DR SMART; SM00055; FCH; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51741; F_BAR; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Membrane;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9804836"
FT CHAIN 2..334
FT /note="Proline-serine-threonine phosphatase-interacting
FT protein 2"
FT /id="PRO_0000058542"
FT DOMAIN 4..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT REGION 288..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..163
FT /evidence="ECO:0000255"
FT MOD_RES 323
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 329
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CONFLICT 298
FT /note="G -> E (in Ref. 3; AAH02123)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 38948 MW; 77B4B0F7BB06095B CRC64;
MTGSLFKGNF WSTDILSTIG YDSIIQHLNN GRKNCKEFED FLKERASIEE KYGKDLLNLS
RKKPCGQSEI NTLKRALEVF KQQVDNVAQC HIQLAQTLRE EARKMEEFRE KQKLQRKKTE
TIMDAAHKQR NAQFKKAMDA KKNYEQKCRD KDEAEQAVHR SANVANQRQQ EKLFVKLATS
KTAVEDSDKA YMLHINMLEK VREDWQSEHI KACEVFEAQE CERINFFRNA LWLHLNQLSQ
QCVANDEMYE QVRKSLETCS IEKDIQYFVN QRKTGQTPPA PIMYENFYSP QRNAAPPGKT
TGPNPARRGP LPVPKRIPDD PDYSVVEDYS LLYQ
