PTN21_RAT
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 03-AUG-2022, entry version 147.
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. [Q62728-1]
DR AlphaFoldDB; Q62728; -.
DR SMR; Q62728; -.
DR BioGRID; 251084; 1.
DR STRING; 10116.ENSRNOP00000059572; -.
DR iPTMnet; Q62728; -.
DR PhosphoSitePlus; Q62728; -.
DR PaxDb; Q62728; -.
DR PRIDE; Q62728; -.
DR GeneID; 171070; -.
DR KEGG; rno:171070; -.
DR UCSC; RGD:620216; rat. [Q62728-1]
DR CTD; 11099; -.
DR RGD; 620216; Ptpn21.
DR eggNOG; KOG0792; Eukaryota.
DR InParanoid; Q62728; -.
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:0006470; P:protein 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; -; 1.
DR Gene3D; 3.90.190.10; -; 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 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; SSF47031; SSF47031; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF54236; SSF54236; 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
