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   27-MAR-2024, entry version 152.
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; 10090-ENSMUSP00000022508; -.
DR   ProteomicsDB; 291542; -. [O55082-1]
DR   ProteomicsDB; 291543; -. [O55082-2]
DR   Antibodypedia; 66300; 109 antibodies from 17 providers.
DR   DNASU; 19256; -.
DR   Ensembl; ENSMUST00000022508.8; ENSMUSP00000022508.7; ENSMUSG00000021940.11. [O55082-1]
DR   Ensembl; ENSMUST00000226512.2; ENSMUSP00000153829.2; ENSMUSG00000021940.11. [O55082-2]
DR   GeneID; 19256; -.
DR   KEGG; mmu:19256; -.
DR   UCSC; uc007szx.1; mouse. [O55082-1]
DR   AGR; MGI:1196295; -.
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; TQMRKQR; -.
DR   OrthoDB; 1342035at2759; -.
DR   PhylomeDB; O55082; -.
DR   TreeFam; TF315573; -.
DR   BioGRID-ORCS; 19256; 0 hits in 78 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 30 other cell types or tissues.
DR   ExpressionAtlas; O55082; baseline and differential.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR46900:SF3; FERM AND PDZ DOMAIN-CONTAINING 2; 1.
DR   PANTHER; PTHR46900; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 13; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
DR   Genevisible; O55082; MM.
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
//