ID A0A452H892_9SAUR Unreviewed; 1786 AA.
AC A0A452H892;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000010939.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000010939.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; ENSGAGT00000012533.1; ENSGAGP00000010939.1; ENSGAGG00000008474.1.
DR Proteomes; UP000291020; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000291020};
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 1138..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..95
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 107..189
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 196..286
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 291..387
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 389..478
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 483..580
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 585..693
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 694..791
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 792..887
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 891..977
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1232..1487
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1407..1478
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1519..1765
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1696..1769
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 472..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1786 AA; 200378 MW; 87228749693BB532 CRC64;
MGPQLKVVER TRTATMLCAA SGNPDPEITW FKDFLPVDTS NNNGRIKQLR SESIGGTPIR
GALQIELSEE SDQGKYECVA TNSAGTRYSA PANLYVRELR EVRRVPPRFS IPPTNHEIMP
GGSVNITCVA VGSPMPYVKW MLGAEDLTPE DDMPIGRNVL ELNDVRQSAN YTCVAMSTLG
VIEAIAQITV KALPKPPGTP VVTESTATSI TLTWDSGNPE PVSYYIIQHK PKNSEELYKE
IDGVATTRYS VAGLSPYSEY EFRVVAVNNI GRGPPSAPVS TRTSEQAPSS APRSVQARML
SSTTILVQWE EPEEPNGQIQ GYRVYYTMDP TQHVNSWMKH NVADSHITTI GNLVPQKTYS
VKVLAFTSVG DGPLSTDIQV ITQTGVPGQP LNFKAEPESE TSILLSWTPP RSDTISSYEL
VYKDGDQGEE QRVSIEPTTS YRLQSLKPNS LYYFRLAARS PQGLGASTAE ISARTMQSKP
SAPPQDISCT SPSSTSILVS WQPPPVEKQN GIITEYSIKY IGIDGEDDKP HEILGISSDT
TQYLLEQLEK WTEYRISVTA HTDVGPGPES LAVLIRTDED VPSGPPRKVE VEAVNSTSVK
VSWRSPVPNK QHGQIRGYQV HYVRMENGEP KGQPMLKDVM LADAQWEYDD TAEHEMIISG
LQPETTYSLT VTAYTTKGDG ARSKPKLVST TGAVPGKPRL VISHTQMNTA LIQWHPPVDT
FGLLQGYRLK FGRKDLDMFT TLEFSEKEDH FTATDIHKGA SYLFRLSARN KVGYGEEMVK
EISIPEEVPN GFPQNLHSES STSTSVQLTW QPPVLAERNG IITKYTLLYR DINVAHHPVE
LPIVPADTAM TLSGLKPDTT YDVKVRAHTS KGPGPYSPSV QFRTLPVDQV FAKNFHVKAV
MKTSVLLSWE IPENYNSAMP FKILYDDGKM VVEVDGRATQ KLITNLKPET SYSFVLTNRG
NSAGGLQHRV TAKTAPDVLR TKPVFIGKTN LDGMITVELP EVPANENIKG YYIVIVPLKK
SHGKFIKPWE SPDEMELDEL LKEIVRKRRS IRFGREVELK PYIAAHFEVL PTEFTLGDKK
QYGGFENKQL QSGQEYVFFV LAVMEHSEST MYATSPYSDP VVSMDLDPQP ITDEEEGLIW
VVGPVLAVVF IICIVIAILL YKSKPDRKRA ESDSRKSSIP NSKEIPSHHP TDPVELRRLN
FQTPGMASHP PIPILELADH IERLKANDNL KFSQEYESID PGQQFTWEHS NLEVNKPKNR
YANVIAYDHS RVLLSAIEGI PGSDYVNANY IDGYRKQNAY IATQGALPET FGDFWRMMWE
QRGATVVMMT KLEERSRVKC DQYWPSRGTE TYGLIQVTLL DTVELATYCV RTFALYKNGS
SEKREVRQFQ FTAWPDHGVP EHPTPFLAFL RRVKTCNPPD AGPMVVHCSA GVGRTGCFIV
IDAMLERIKH EKTVDIYGHV TLMRAQRNYM VQTEDQYIFI HDALLEAVTC GNTEVPARNL
YAYIQKLTQI ETGENVTGME LEFKRLASSK AHTSRFISAN LPCNKFKNRL VNIMPYESTR
VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRMLWEH NSTIVVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
TDWPEQGVPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDIFQT VKMLRTQRPA MVQTEVRRIT YICIVGGWVD ARLGMG
//
