ID A0A0Q3X8S0_AMAAE Unreviewed; 1377 AA.
AC A0A0Q3X8S0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=AAES_16421 {ECO:0000313|EMBL:KQL60687.1};
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:KQL60687.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQL60687.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQL60687.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000256|ARBA:ARBA00006396}.
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:KQL60687.1}.
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DR EMBL; LMAW01000114; KQL60687.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3X8S0; -.
DR Proteomes; UP000051836; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14632; R-PTPc-U-1; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; IPR003599; Ig_sub.
DR InterPro; IPR000998; MAM_dom.
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; PTHR24051:SF10; PROTEIN-TYROSINE-PHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 3.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
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:KQL60687.1};
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|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 729..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..172
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 174..259
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 272..367
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 370..468
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 469..575
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 881..1117
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1037..1108
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1149..1370
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1286..1361
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 809..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1377 AA; 155388 MW; 362AF2692DE1F845 CRC64;
MDHNLIADAA GCTFEEDGDL NQCEYSHGED DDFEWELIRS YMVPHLMADL PHGSYLMVNS
SQHAPGQKAH LLFQALSEND THCLQFSYFM YSRDGHSPGT LSAYVRVTGG PVGSAVWNAS
GSHGRQWHQA ELAVSLFWPN EYQVLFEAVV SSERRGYLGL DDILLLNYPC SKAPHFSRLG
DVEVNAGQNA TFHCVAAGKA AEAERFLMQR QSGEVVPAAS VKHISHRRFL ATFQLDEVSK
EEQDLYRCVT QSSRGAGVSN FAELIVKEPP TPIAPPQLLR AGSTYLIIQL NTNSIIGDGP
XVRKEIEYRM TSGPWSEVHA VNMQTYKLWH LDPDTEYEIS VLLTRPGEGG TGKPGPPLIS
RTKCAEPMRA PKGLAFSEIQ SRQLTLQWEP LGYNLTRCHT YTVSLCYRYF VGTGHNQTFQ
ECVKMERNAN RYTIKNLLPY KNIHVKLILF NPEGRKEGKE VIFQTDEDVP GGIASESLTF
TPLEDMIFLK WEEPVEPNGL ITQYEISYQS IESSDPAVNV PGPRRTVSKL RNETYHVFSN
LHPGTTYLFS VRARTGKGFG QTALTEITTN ISAPTFDXGD MPSPLSESES TITVLLRPAQ
GRGAPISTYQ VIVEEERPKK LKRELGGQEC FPVPLTFDDA MSRGSVHYFG AELPASSLTE
AKPFTVGDNQ TYSGYWNPPL EPKKAYLIYF QAMSNLKGET RLNCVRIARK AACKESKRPL
EVSQHSEEMG LILGICAGGL IVLIILLGAI IVVIRKGKPV NMTKATINYR HEKTHMMSAI
DRSFTDQSTL QEDERLGLSF MDTHNYSNRG DQRSSVVNES SSLLGGSPRR QCGRKGSPYH
TGQLHPAVRV ADLLQHINQM KTAEGYGFKQ EYESFFEGWD ASKKKDKTKG RQDHVSTYDR
HRVKLHPLLG DPNSDYINAN YIDGYHRSNH FIATQGPKQE MVYDFWRMVW QEHCSSIVMI
TKLVEVGRVK CSKYWPDDSE MYGDIKITLV KSETLAEYAV RTFALERRGY SARHEVKQFH
FTSWPEHGVP YHATGLLAFI RRVKASTPPD AGPVVIHCSA GTGRTGCYIV LDVMLDMAEC
EGVVDIYNCV KTLCSRRINM IQTEEQYIFI HDAILEACLC GETSIPASEF KPTYKEMVRI
EPQSNSSQLR EEFQTLNSVT PHLDVEECSI ALLPRNRERN RSMDVLPPDR CLPFLISVDG
DSNNYINAAL TDSYTKSAAF IVTLHPLQNT TTDFWRLVYD YGCTSIVMLN QLNQSNSAWL
QEGHLMVRHF QYLRWSAYRD TPDSKKSFLH LLAQVERWQK ESGDGRTVVH CLNGGGRSGT
FCASTMILEM LKCHNMADVF YAAKTLRNYK PNMVETLEQY HFCYDIALEY LESLETR
//
