ID A0A0Q3PSP6_AMAAE Unreviewed; 1778 AA.
AC A0A0Q3PSP6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=AAES_32663 {ECO:0000313|EMBL:KQL08873.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQL08873.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL08873.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL08873.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQL08873.1}.
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DR EMBL; LMAW01000570; KQL08873.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3PSP6; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 8.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR CDD; cd14628; R-PTP-D-2; 1.
DR CDD; cd14624; R-PTPc-D-1; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
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; IPR045905; R-PTP-delta_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; 7.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 8.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49265; Fibronectin type III; 5.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
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, ECO:0000256|SAM:Phobius};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Receptor {ECO:0000313|EMBL:KQL08873.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1133..1156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..103
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 111..193
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 200..290
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 295..391
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 393..482
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 487..584
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 589..688
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 689..782
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 787..882
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 886..972
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1223..1478
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1398..1469
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1510..1769
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1687..1760
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 276..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1778 AA; 199751 MW; C3D5F974A7AC320E CRC64;
MGRKTEDQIP RGFPTIDMGP QLKVVERTRT ATMLCAASGN PDPEITWFKD FLPVDTSNNN
GRIKQLRSGA LQIELSEESD QGKYECVATN SAGTRYSAPA NLYVRVRRVP PRFSIPPTNH
EIMPGGSVNI TCVAVGSPMP YVKWMLGAED LTPEDDMPIG RNVLELNDVR QSANYTCVAM
STLGVIEAIA QITVKALPKP PGTPVVTEST ATSITLTWDS GNPEPVSYYI IQHKPRNSEE
PYKEIDGVAT TRYSVAGLSP YSEYEFRVVA VNNIGRGPPS EPVSTRTSEQ APSSAPRNVQ
ARMLSSTTIL VQWEEPEEPN GQIQGYRVYY TMEPTQHVNS WMKHNVADSH ITTIGNLVPQ
KTYSVKVLAF TSVGDGPLSS DIQVITQTGV PGQPLNFKAE PESETSILLS WTPPRSDTIS
SYELVYKDGE HGEEQRVSTE PATSYRLQGL RPNSLYLFRL AARSPQGLGA STAEISARTM
QSKPSAPPQD ISCTSPSSTS ILVSWKPPPA EKQNGIITEY SIKYIGIDGE DIKPHEILGI
SSDSTQYLLE HLEKWTEYRI SVTAHTDVGP GPESLAVLIR TDEDVPSGPP RKVEVEAVNS
TAVKVSWRSP VHNKQHGQIR GYQVHYVRME NGESKGQPML KDIMLADAQE MIISGLQPET
TYSFTVTAYT TKGDGARSKP KLVSTTGAVP GKPRLVISHT QMNTALIQWH PPVDTFGPLQ
GYRLKFGRRD MDTFTTMEFS EKEDHFTATD IHKGASYIFR LSARNKVGFG EEMVKEISVP
EEVPSGFPQN LHSESSTSTS VQLTWQMPLL AERNGIITKY TILYRDINVA YQPVELPVAP
ADTTMTLSGL KPDTTYDVKV RAHTSKGPGP YSPSVQFRTL PVDQVFAKNF HVKAVMKTSV
LLSWEIPENY NSALPFKILY DDGKMVVEVD GRATQKLITN LKPETSYSFV LTNRGNSAGG
LQHRVTAKTA PDVLRTKPVF IGKTNLDGMI TVELPEVPSN ENIKGYYIVI VPLKRSRGKF
IKPWESPDEM ELDELLKEIA RKRRSIRLER EVELKPYIAA HFDVLPTEFT LGDKKHYGGF
ENKQLQSGQE YVFFVLAVME HSESTMYATS PYSDPVVSMD LDPQPITDEE EGLIWVVGPV
LAVVFIICIV IAILLYKRKR AESDSRKSSI PNSKEVPSHH PTDPVELRRL NFQTPGMASH
PPIPILELAD HIERLKANDN LKFSQEYESI DPGQQFTWEH SNLEVNKPKN RYANVIAYDH
SRVLLSAIEG IPGSDYINAN YIDGYRKQNA YIATQGALPE TFGDFWRMMW EQRGATVVMM
TKLEERSRVK CDQYWPSRGT ETYGLIQVTL LDTVELATYC VRTFALYKNG SSEKREVRQF
QFTAWPDHGV PEHPTPFLAF LRRVKTCNPP DAGPMVVHCS AGVGRTGCFI VIDAMLERIK
HEKTVDIYGH VTLMRAQRNY MVQTEDQYIF IHDALLEAVT CGNTEVPARN LYAYIQKLTQ
IETGENVTGM ELEFKRLASS KAHTSRFISA NLPCNKFKNR LVNIMPYEST RVCLQPIRGV
EGSDYINASF IDGYRQQKAY IATQGPLAET TEDFWRMLWE HNSTIVVMLT KLREMGREKC
HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTVRQFQ FTDWPEQGVP
KSGEGFIDFI GQVHKTKEQF GQDGPISVHC SAGVGRTGVF ITLSIVLERM RYEGVVDIFQ
TVKMLRTQRP AMVQTEDQYQ FCYRAALEYL GSFDHYAT
//
