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Database: UniProt
Entry: Q62728
LinkDB: Q62728
Original site: Q62728 
ID   PTN21_RAT               Reviewed;        1175 AA.
AC   Q62728; Q62732;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 21;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 2E;
GN   Name=Ptpn21; Synonyms=Ptp2e;
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 [MRNA] (ISOFORMS 1 AND 2E).
RC   STRAIN=Sprague-Dawley;
RX   PubMed=7805871; DOI=10.1016/0014-5793(94)01305-5;
RA   L'Abbe D., Banville D., Tong Y., Stocco R., Masson S., Ma S., Fantus G.,
RA   Shen S.H.;
RT   "Identification of a novel protein tyrosine phosphatase with sequence
RT   homology to the cytoskeletal proteins of the band 4.1 family.";
RL   FEBS Lett. 356:351-356(1994).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637; SER-710 AND SER-711, AND
RP   IDENTIFICATION BY 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   -!- 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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62728-1; Sequence=Displayed;
CC       Name=2E;
CC         IsoId=Q62728-2; Sequence=VSP_000498;
CC   -!- TISSUE SPECIFICITY: Particularly abundantly in adrenal glands.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000305}.
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DR   EMBL; U17971; AAA62153.1; -; mRNA.
DR   EMBL; U18293; AAA62154.1; -; mRNA.
DR   PIR; S51005; S51005.
DR   RefSeq; NP_598229.1; NM_133545.1.
DR   AlphaFoldDB; Q62728; -.
DR   SMR; Q62728; -.
DR   BioGRID; 251084; 1.
DR   STRING; 10116.ENSRNOP00000068645; -.
DR   iPTMnet; Q62728; -.
DR   PhosphoSitePlus; Q62728; -.
DR   PaxDb; 10116-ENSRNOP00000059572; -.
DR   GeneID; 171070; -.
DR   KEGG; rno:171070; -.
DR   UCSC; RGD:620216; rat. [Q62728-1]
DR   AGR; RGD:620216; -.
DR   CTD; 11099; -.
DR   RGD; 620216; Ptpn21.
DR   eggNOG; KOG0792; Eukaryota.
DR   InParanoid; Q62728; -.
DR   OrthoDB; 3108587at2759; -.
DR   PhylomeDB; Q62728; -.
DR   PRO; PR:Q62728; -.
DR   Proteomes; UP000002494; Unplaced.
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; IDA:RGD.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:RGD.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR   CDD; cd17192; FERM_F1_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   Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase; Phosphoprotein;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..1175
FT                   /note="Tyrosine-protein phosphatase non-receptor type 21"
FT                   /id="PRO_0000219441"
FT   DOMAIN          23..308
FT                   /note="FERM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT   DOMAIN          897..1168
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   REGION          395..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          663..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        395..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1109
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT                   ECO:0000255|PROSITE-ProRule:PRU10044"
FT   BINDING         1068
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         1109..1115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   MOD_RES         589
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   MOD_RES         590
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   MOD_RES         637
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         711
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         798
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   MOD_RES         800
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   MOD_RES         805
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62136"
FT   VAR_SEQ         1..839
FT                   /note="Missing (in isoform 2E)"
FT                   /evidence="ECO:0000303|PubMed:7805871"
FT                   /id="VSP_000498"
SQ   SEQUENCE   1175 AA;  133412 MW;  82A684F1C0F5ECF7 CRC64;
     MPLPFGLKLK RTRRYTVSSK SCLVARIQLL NNEFVEFTLS VESTGQESLE AVAQRLELRE
     ITYFSLWYYN KQNQRRWVDL EKPLKKQLDK HALEPTVYFG VVFYVPSVSQ LQQEITRYQY
     YLQLKKDVLE GNLPCTLEQA IQLAGLAVQA DFGDFDQYES QDFLQKFALL PVGWLQDEKL
     LEEAAQKVAL LHQKYRGLTA PEAEMLYMQE VERMDGYGEE SYPAKDSQGS DISIGACLDG
     IFVKHKNGRP PVVFRWHDIA NMSHNKSFFA LELANKEETI QFQTEDMETA KYVWRLCVAR
     HKFYRLNQCN LQTQAATLNS VRRGSSSRMS LPKPQPYAMP PPPQLHYNGH YTEPFASSQD
     NVFVPNKNGF YCHSQTSLDR TQIDLSGRIR NGSVYSAHST NSLNTPQPYL QPSPMSSNPS
     IPGSDVMRPD YIPSHRHSAL IPPSYRPTPD YESVMKRLNR GMVHADRHSH SLRNLNIGSS
     YAYSRPDALV YSQPEIREHP HLASPQSAHY PFNLNYSFHS QAPYPYPVER RPVVGAVSVP
     ELTNVQLQAQ DYPAPNIMRT QVYRPPPPYP YPRPANSTPD LSRHLYISSS NPDLITRRVH
     HSVQTFQEDS LPVAHSLQEV SEPLTAARHA HLQKRNSIEI AGLTHGFEGL RLKEETMSAS
     AADVAPRTFS AGSQSSVFSD KVKQEGTEEQ GSGGYSHKKS LSDATMLIHS SEEDEDLEDD
     SSREHAVSEP RLTAAFSQEQ QLNYPCASVT PVTGPLHIFE PKSHVTEPEK RAKDISPVHL
     VMETHQPRRH GLLTPSMSES DLTTSGRYRA RRDSLKKRPV SDLLSGKKNT VEGLPPLGGM
     KKTRADAKKI GPLKLAALNG LSLSRLPLPD EGKEVSTRAT NDERCKVLEQ RLEQGTVFTE
     YERILKKRLV DGECSTARLP ENAERNRFQD VLPYDDARVE LVPTKENNTG YINASHIKVS
     VSGIEWDYIA TQGPLQNTCQ DFWQMVWEQG VAIIAMVTAE EEGGREKSFR YWPRLGSRHN
     TVTYGRFKIT TRFRTDSGCY ATTGLKMKHL LTGQERTVWH LQYTDWPEHG CPEDLKGFLS
     YLEEIQSVRR HTNSTSEPRS PNPPLLVHCS AGVGRTGVVI LSEIMVACLE HNEVLDIPRV
     LELLRQQRMM LVQTLSQYTF VYRVLIQFLK SSRLI
//
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