ID   PTN20_RAT               Reviewed;         421 AA.
AC   A1L1L3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 20;
DE            EC=3.1.3.48;
GN   Name=Ptpn20;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
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};
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   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; BC129117; AAI29118.1; -; mRNA.
DR   RefSeq; NP_001073618.1; NM_001080149.1.
DR   RefSeq; XP_006252827.1; XM_006252765.3.
DR   RefSeq; XP_006252829.1; XM_006252767.3.
DR   RefSeq; XP_008769321.1; XM_008771099.1.
DR   RefSeq; XP_017455576.1; XM_017600087.1.
DR   AlphaFoldDB; A1L1L3; -.
DR   SMR; A1L1L3; -.
DR   STRING; 10116.ENSRNOP00000027352; -.
DR   iPTMnet; A1L1L3; -.
DR   PhosphoSitePlus; A1L1L3; -.
DR   PaxDb; A1L1L3; -.
DR   PeptideAtlas; A1L1L3; -.
DR   PRIDE; A1L1L3; -.
DR   Ensembl; ENSRNOT00000027352; ENSRNOP00000027352; ENSRNOG00000020203.
DR   GeneID; 306281; -.
DR   KEGG; rno:306281; -.
DR   UCSC; RGD:1309812; rat.
DR   CTD; 26095; -.
DR   RGD; 1309812; Ptpn20.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000160066; -.
DR   HOGENOM; CLU_001645_9_5_1; -.
DR   InParanoid; A1L1L3; -.
DR   OMA; HILYSDW; -.
DR   OrthoDB; 411281at2759; -.
DR   PhylomeDB; A1L1L3; -.
DR   TreeFam; TF315573; -.
DR   PRO; PR:A1L1L3; -.
DR   Proteomes; UP000002494; Chromosome 16.
DR   Bgee; ENSRNOG00000020203; Expressed in testis.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
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   Cytoplasm; Cytoskeleton; Hydrolase; Microtubule; Nucleus; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..421
FT                   /note="Tyrosine-protein phosphatase non-receptor type 20"
FT                   /id="PRO_0000295757"
FT   DOMAIN          160..413
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          93..116
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        354
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         354..360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100"
SQ   SEQUENCE   421 AA;  48580 MW;  E908283346F8C0B6 CRC64;
     MSSPGNVRQK HGRDNDEHEG DSDDLNLQKS LPSSSQQKTP TKPVFGNKVN SESVKTSHHM
     SFSNKYDLVF PEPVESDNDE TLWDVRDLSH RNRWSSVDPE SAGPSKTVST VLSESSTDTA
     VSERELTQLA QIRPLIFNSS SRAALRDCLK ALQKKEELDI IREFLELEEM IPPDDFKSGY
     ELQNRDKNRY RDILPYDSTR VPLGKNKDYI NASYIRIVNH EEEYFYIATQ GPLPDTIEDF
     WQMVLENNCN VIAMITREIE GGVIKCCSYW PVSLKEPLEF KHFHVLLENF QITQYFVIRI
     FQIVKKSTGK SHSVKHLQFI KWPDHGTPAS ADFFIKYVRY VRKSHITGPL LVHCSAGVGR
     TGVFICVDVV FCTIEKNYSF NIMNIVTQMR KQRFGMIQTK EQYQFCYEIV LEVLQNLLAL
     N