ID G1L3T2_AILME Unreviewed; 1114 AA.
AC G1L3T2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000934};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000934};
GN Name=PTPN21 {ECO:0000313|Ensembl:ENSAMEP00000001542.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000001542.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000001542.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000001542.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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;
CC Evidence={ECO:0000256|PIRNR:PIRNR000934};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000934}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC ECO:0000256|PIRNR:PIRNR000934}.
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DR STRING; 9646.ENSAMEP00000001542; -.
DR Ensembl; ENSAMET00000001601.2; ENSAMEP00000001542.2; ENSAMEG00000001393.2.
DR Ensembl; ENSAMET00000026841.1; ENSAMEP00000030677.1; ENSAMEG00000030096.1.
DR eggNOG; KOG0792; Eukaryota.
DR GeneTree; ENSGT00940000155613; -.
DR HOGENOM; CLU_006456_1_0_1; -.
DR TreeFam; TF315900; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
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; 3.
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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR000934};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR000934}; Hydrolase {ECO:0000256|PIRNR:PIRNR000934};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000934};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912}.
FT DOMAIN 23..308
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 836..1107
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1018..1098
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 364..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1048
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000934-1"
SQ SEQUENCE 1114 AA; 125999 MW; 0A8E33EDFFB224E4 CRC64;
MPLPFGLKLK RTRRYTVSSK SCLVARIQLL NNEFVEFTLS VESTGQESLE AVAQRLELRE
ITYFSLWYHN KQNQRRWVDL EKPLKKQLDK YASEPTVYFG VVFYVPSVSQ LQQEITRYQY
YLQLKKDILE GNIPCTLEQA IQLAGLAVQA DFGDFDQYES QDFLQKFALF PVGWLQDEKV
LEEATQKVAV LHQKYRRLTA PDAEMLYMQE VERMDGYGEE SYPAKDSQGS DISIGACLEG
IFVKHKNGRP PVIFRWHDIA NMSHNKSFFA LELANKEETI QFQTEDMETA KYVWRLCVPK
PQPYVMPPPP QLHYNGHYTE PYTSSQDNLF ATNQNGYYCH SLTSLDRAQI DLNGRIRNGS
VYSAHSTNSL NNPQPYLQPS PMSSNPSITG SDVMRPDYVP SHRHSALIPP SYRPTPDYET
VMKQLNRGMV HAERQSHSLR NLNIGNSYAY SRPDALVYSQ PEIREHAHFA SPQSAHYPFS
LNYSFHSPSP YPHPAERRLV VGAVSVPELT NVQLQAQDYP APNIMRTQVY RPPPPYPPPR
PANSTPDLSR HLYISSSNPD LITRRVHHSV QTFQEASLPV AHSLQEVSEP LTAARRAHLH
KRNSIEVAGL AHSLEGLRLK ERTLSASAAD TLPRPVSAGS QPGGFPERAE RDPVDERGGL
GYGHKKSLSD ATMLIHSSED EEDLEEEIAS RCRNPPAGPA APPAAPGPGL LHGREPAPPL
GEALRPRREG LLTPSMSESD LTTSGRYRAR RDSVKQRPVS DLLSGKKNVV EGLPPLGGMK
KSRVDAKKIG PLKLAALNGL SLSRLPLPDE GKEVPARATN DERCRILEQR LEQGMVFTEY
EKILKKRLVD GECSTARLPE NAERNRFQDV LPYDDARVEL VPTKENNTGY INASHIKVSV
SGIEWDYIAT QGPLQNTCQD FWQMVWEQGI AIIAMVTVEE EGGREKSFRY WPRLGSRHNT
VTYGRFKITT RFRTDSGCYA TTGLKMKHLL TGQERTVWHL QYTDWPEHGC PEDLKGFLSY
LEEIQSVRRH TNSTSEPKSP NPPLLVHCSA GVGRTGVVIL SEIMIACLEH NEVLDVPRVL
GMLRQQRMAM VQTLCQYTFV YRVLVQFLKS SRLI
//
