ID   PTN21_MOUSE             Reviewed;        1176 AA.
AC   Q62136;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 149.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 21;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase PTP-RL10;
GN   Name=Ptpn21;
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].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=7838537;
RA   Higashitsuji H., Arii S., Furutani M., Imamura M., Kaneko Y., Takenawa J.,
RA   Nakayama H., Fujita J.;
RT   "Enhanced expression of multiple protein tyrosine phosphatases in the
RT   regenerating mouse liver: isolation of PTP-RL10, a novel cytoplasmic-type
RT   phosphatase with sequence homology to cytoskeletal protein 4.1.";
RL   Oncogene 10:407-414(1995).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577; SER-637 AND SER-806, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-590; SER-637;
RP   SER-673; SER-799; SER-801 AND SER-806, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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).
CC   -!- FUNCTION: May be involved in the regulation of growth and
CC       differentiation of liver cells.
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: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Liver.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; D37801; BAA07053.1; -; mRNA.
DR   CCDS; CCDS26098.1; -.
DR   PIR; I58345; I58345.
DR   AlphaFoldDB; Q62136; -.
DR   SMR; Q62136; -.
DR   STRING; 10090.ENSMUSP00000082197; -.
DR   iPTMnet; Q62136; -.
DR   PhosphoSitePlus; Q62136; -.
DR   jPOST; Q62136; -.
DR   MaxQB; Q62136; -.
DR   PaxDb; 10090-ENSMUSP00000082197; -.
DR   ProteomicsDB; 301938; -.
DR   Pumba; Q62136; -.
DR   AGR; MGI:1344406; -.
DR   MGI; MGI:1344406; Ptpn21.
DR   eggNOG; KOG0792; Eukaryota.
DR   InParanoid; Q62136; -.
DR   PhylomeDB; Q62136; -.
DR   ChiTaRS; Ptpn21; mouse.
DR   PRO; PR:Q62136; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q62136; Protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR014392; PTP_non-rcpt_14/21.
DR   InterPro; IPR041782; PTPN14/21_FERM_C.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF3; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 21; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 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; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..1176
FT                   /note="Tyrosine-protein phosphatase non-receptor type 21"
FT                   /id="PRO_0000219440"
FT   DOMAIN          23..308
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          898..1169
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          668..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          789..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..824
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1110
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1069
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         1110..1116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         637
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62728"
FT   MOD_RES         711
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62728"
FT   MOD_RES         799
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         801
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1176 AA;  133491 MW;  529FBE22F1335B75 CRC64;
     MPLPFGLKLK RTRRYTVSSK SCLVARIQLL NNEFVEFTLS VESTGQESLE AVAQRLELRE
     VTYFSLWYYN KQNQRRWVDL EKPLKKQLDK HALEPTVYFG VLFYVPSVSQ LQQEITRYQY
     YLQLKKDILE GNLPCTLEHA IQLAGLAVQA DFGDFDQYES QDFLQKFALL PVAWLQDEKV
     LEEAAQKVAL LHQKYRGLTA PEAELLYMQE VERMDGYGEE SYPAKDSQGS DISIGACLDG
     IFVKHKNGRP PVVFRWHDIA NMSHNKSFFA LELANKEETI QFQTEDMETA KYVWRLCVAR
     HKFYRLNQCS LQTQAATLNS VRRDSSSRMS LPKPQPYAMP PPPQLHYNGH YTEPFASSQD
     NIFVPNKNGF YCHSQTSLDR TQIDLSGRIR NGSVYSAHST NSLNTLQPYL QPSPMSSNPS
     ITGSDVMRPD SLPSHRHSAL IPPSYRPTPD YETVMKQLNR GMVHADRHSH SLRNLNIGSS
     YAYSRPDALV YSQPEIREHP HLTSPQSAHY PFNLNYSFHS QSPYPYPAER RPVVGAVSVP
     ELTNVQLQAQ DYPAPNIMRT QVYRPPPPYP YPRPANSTPD LSRHLYISSS NPDLITRRVH
     HSVQTFQEDS LPVAHSLQEV SEPLTAARHA HLQKRNSIEI AGLTHGFEGL RLKERTVSAS
     AADVAPRTFS AGSQSSVFSD KMKQEGTEEQ EGGRYSHKKS LSDATMLIDS SEEDEDLEED
     SSREQAISAV SEPRLTAAFS QELNYPCASA TPITGPLHIF EPKPHVTEPE KRAKDISPVH
     LVVETHRPRR DGLLTPSMSE SDLTTSGRYR ARRDSVKKRP VSDLLSGKKS AVEGLPPLGG
     MKKTRADAKK IGPLKLAALN GLSLSRLPLP DEGKEVSTRA TNDERCKVLE QRLEQGMVFT
     EYERILKKRL VDGECSTARL PENAERNRFQ DVLPYDDARV ELVPTKENNT GYINASHIKV
     SVSGIEWDYI ATQGPLQNTC QDFWQMVWEQ GVAIIAMVTA EEEGGREKSF RYWPRLGSRH
     NTVTYGRFKI TTRFRTDSGC YATTGLKMKH LLTGQERTVW HLQYTDWPEH GCPEDLKGFL
     SYLEEIQSVR RHTNSTSEPK SHNPPLLVHC SAGVGRTGVV ILSEIMVACL EHNEVLDIPR
     VLDMLRQQRM MLVQTLGQYT FVYRVLIQFL KSSRLI
//