PTN20_MOUSE
ID PTN20_MOUSE Reviewed; 426 AA.
AC O55082; A4QPF6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 20;
DE EC=3.1.3.48;
DE AltName: Full=Testis-specific tyrosine phosphatase;
GN Name=Ptpn20; Synonyms=Typ;
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] (ISOFORM 1), ENZYME ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Testis;
RX PubMed=9407093; DOI=10.1074/jbc.272.52.33092;
RA Ohsugi M., Kuramochi S., Matsuda S., Yamamoto T.;
RT "Molecular cloning and characterization of a novel cytoplasmic protein-
RT tyrosine phosphatase that is specifically expressed in spermatocytes.";
RL J. Biol. Chem. 272:33092-33099(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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] (ISOFORM 2).
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).
CC -!- FUNCTION: Tyrosine-protein phosphatase targeted to sites of actin
CC polymerization in response of varied extracellular stimuli. Has
CC tyrosine phosphatase activity towards various tyrosyl phosphorylated
CC substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044, ECO:0000269|PubMed:9407093};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250}. Note=Colocalizes with the microtubule-organizing center
CC and intracellular membrane compartments. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O55082-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O55082-2; Sequence=VSP_027074, VSP_027075;
CC -!- TISSUE SPECIFICITY: Testis-specific. Specifically expressed in
CC testicular germ cells that undergo meiosis (at protein level).
CC {ECO:0000269|PubMed:9407093}.
CC -!- DEVELOPMENTAL STAGE: Detected between 2 and 3 weeks after birth, in
CC parallel with the onset of meiosis. {ECO:0000269|PubMed:9407093}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
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DR EMBL; D64141; BAA23761.1; -; mRNA.
DR EMBL; AK029493; BAC26476.1; -; mRNA.
DR EMBL; BC139817; AAI39818.1; -; mRNA.
DR CCDS; CCDS36870.1; -. [O55082-1]
DR RefSeq; NP_033004.1; NM_008978.2. [O55082-1]
DR AlphaFoldDB; O55082; -.
DR SMR; O55082; -.
DR BioGRID; 202485; 2.
DR STRING; 10090.ENSMUSP00000022508; -.
DR iPTMnet; O55082; -.
DR PhosphoSitePlus; O55082; -.
DR PaxDb; O55082; -.
DR PRIDE; O55082; -.
DR ProteomicsDB; 291542; -. [O55082-1]
DR ProteomicsDB; 291543; -. [O55082-2]
DR Antibodypedia; 66300; 90 antibodies from 17 providers.
DR DNASU; 19256; -.
DR Ensembl; ENSMUST00000022508; ENSMUSP00000022508; ENSMUSG00000021940. [O55082-1]
DR Ensembl; ENSMUST00000226512; ENSMUSP00000153829; ENSMUSG00000021940. [O55082-2]
DR GeneID; 19256; -.
DR KEGG; mmu:19256; -.
DR UCSC; uc007szx.1; mouse. [O55082-1]
DR CTD; 26095; -.
DR MGI; MGI:1196295; Ptpn20.
DR VEuPathDB; HostDB:ENSMUSG00000021940; -.
DR eggNOG; KOG0789; Eukaryota.
DR GeneTree; ENSGT00940000160066; -.
DR HOGENOM; CLU_001645_9_5_1; -.
DR InParanoid; O55082; -.
DR OMA; HILYSDW; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; O55082; -.
DR TreeFam; TF315573; -.
DR BioGRID-ORCS; 19256; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ptpn20; mouse.
DR PRO; PR:O55082; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O55082; protein.
DR Bgee; ENSMUSG00000021940; Expressed in spermatocyte and 28 other tissues.
DR ExpressionAtlas; O55082; baseline and differential.
DR Genevisible; O55082; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase; Microtubule;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..426
FT /note="Tyrosine-protein phosphatase non-receptor type 20"
FT /id="PRO_0000295756"
FT DOMAIN 165..418
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 329
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 359..365
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 403
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L1L3"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1L1L3"
FT VAR_SEQ 122..133
FT /note="TETSVSEKELTQ -> DIYKVSDTWNIY (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027074"
FT VAR_SEQ 134..426
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027075"
SQ SEQUENCE 426 AA; 49119 MW; 2B35FB13379502F4 CRC64;
MSSPRKVRGK TGRDNDEEEG NSGNLNLRNS LPSSSQKMTP TKPIFGNKMN SENVKPSHHL
SFSDKYELVY PEPLESDTDE TVWDVSDRSL RNRWNSMDSE TAGPSKTVSP VLSGSSRLSK
DTETSVSEKE LTQLAQIRPL IFNSSARSAM RDCLNTLQKK EELDIIREFL ELEQMTLPDD
FNSGNTLQNR DKNRYRDILP YDSTRVPLGK NKDYINASYI RIVNHEEEYF YIATQGPLPE
TIEDFWQMVL ENNCNVIAMI TREIECGVIK CYSYWPISLK EPLEFEHFSV FLETFHVTQY
FTVRVFQIVK KSTGKSQCVK HLQFTKWPDH GTPASADFFI KYVRYVRKSH ITGPLLVHCS
AGVGRTGVFI CVDVVFSAIE KNYSFDIMNI VTQMRKQRCG MIQTKEQYQF CYEIVLEVLQ
NLLALY
