ID G5E7I1_MELGA Unreviewed; 1575 AA.
AC G5E7I1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=PTPRD {ECO:0000313|Ensembl:ENSMGAP00000017817.2};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000017817.2, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000017817.2, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000017817.2}
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|ARBA:ARBA00001490};
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000256|ARBA:ARBA00010504}.
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DR Ensembl; ENSMGAT00000018298.2; ENSMGAP00000017817.2; ENSMGAG00000016387.2.
DR GeneTree; ENSGT00940000153617; -.
DR HOGENOM; CLU_390081_0_0_1; -.
DR Proteomes; UP000001645; Chromosome Z.
DR Bgee; ENSMGAG00000016387; Expressed in brain and 3 other cell types or tissues.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 6.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR CDD; cd14553; R-PTPc-LAR-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 9.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
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 PANTHER; PTHR46957; CYTOKINE RECEPTOR; 1.
DR PANTHER; PTHR46957:SF8; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE S; 1.
DR Pfam; PF00041; fn3; 5.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 4.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000001645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 8..94
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 105..194
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 202..284
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 291..381
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 386..480
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 509..608
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 609..702
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 707..802
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 806..892
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1151..1359
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1279..1350
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1391..1575
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT REGION 367..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1575 AA; 176570 MW; 3C4396D9A58F0FAD CRC64;
LLLFSSPPKF TRTPVDQTGV SGGVASFICQ ATGDPRPKIV WNKKGKKVSN QRFEVLESSL
LLHPICIQDR LSVLYTCEST EGFSDVKSFK LYITFSEDQI PRGFPTIDMG PQLKVVERTR
TATMLCAASG NPDPEITWFK DFLPVDTSNN NGRIKQLRSG ALQIELSEES DQGKYECVAT
NSAGTRYSAP ANLYVRVRRV PPRFSIPPTN HEIMPGGSVN ITCVAVGSPM PYVKWMLGAE
DLTPEDDMPI GRNVLELNDV RQSANYTCVA MSTLGVIEAI AQITVKALPK PPGTPVVTES
TATSITLTWD SGNPEPVSYY IIQHKPKNSE EPYKEIDGVA TTRYSVAGLS PYSEYEFRVV
AVNNIGRGPP SEPVSTRTSE QAPSSAPRNV QARMLSSTTI LVQWEEPEEP NGQIQGYRVY
YTMDPTQHVN SWLKHNVADS HITTIGNLVP QKTYSVKVLA FTSVGDGPLS SDIQVITQTG
GKAVAKVIGG TGACNFVLSN DVVPVPSGPP RKVEVEAVNS TAVKVSWRSP VPNKQHGQIR
GYQVHYVRME NGEPRGQPML KDIMLADAQE MIISGLQPDT TYSFTVTAYT TKGDGARSKP
KLVSTTGAVP GKPRLVISHT QMNTALIQWH PPVDTFGPLQ GYRLKFGRKD VDTFTTMEFS
EKEDHFTATD IHKGASYVFR LSARNKVGFG EEMVKEISVP EEVPSGFPQN LHSESSTSTS
VQLTWQMPLL AERNGIITKY TILYRDINVA YQPIELPVVP ADTTMTLSGL KPDTTYDVKV
RAHTSKGPGP YSPSVQFRTL PVDQVFAKNF HVKAVMKTSV LLSWEIPENY NSALPFKILY
DDGKMVMEVD GRATQKLITN LKPETSYSFV LTNRGNSAGG LQHRVTAKTA PDVLRTKPVF
IGKTNLDGMI TVELPEVPSN ENIKGYYIVI VPLKRSRGKF IKPWESPDEM ELDELLKEIA
RKRRSIRFGR EAELKPYIAA HFEVLPTEFT LGDKKHYGGF ENKQLQTGQE YVFFVLAVME
HSESTMYATS PYSDPVVSMD LDPQPITDEE EGLIWVVGPV LAVVFIICIV IVSLFCTISF
AGSGVCGYLG NLHPSSMASH PPIPILELAD HIERLKANDN LKFSQEYEVI YFHASQIIKN
IMYVHSSFFA GIPGSDYINA NYIDGYRKQN AYIATQGALP ETFGDFWRMM WEQRGATVVM
MTKLEERSRV KCDQYWPSRG TETYGLIQVT LLDTVELATY CVRTFALYKN GSSEKREVRQ
FQFTAWPDHG VPEHPTPFLA FLRRVKTCNP PDAGPMVVHC SAGVGRTGCF IVIDAMLERI
KHEKTVDIYG HVTLMRAQRN YMVQTEDQYI FIHDALLEAV TCGNTEVPAR NLYAYIQKLT
QIETGENVTG MELEFKRLAS SKAHTSRFIS ANLPCNKFKN RLVNIMPYES TRVCLQPIRG
VEGSDYINAS FVDGYRQQKA YIATQGPLAE TTEDFWRMLW EHNSTIVVML TKLREMGREK
CHQYWPAERS ARYQYFVVDP MAEYNMPQYI LREFKVTDAR VSCSIYLLFK YTLYLSLFTH
YTRIISLWKT DFIQI
//
