ID G3PTS6_GASAC Unreviewed; 1899 AA.
AC G3PTS6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000021013.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000021013.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000021013.1}
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 STRING; 69293.ENSGACP00000021013; -.
DR Ensembl; ENSGACT00000021053.1; ENSGACP00000021013.1; ENSGACG00000015921.1.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000153617; -.
DR InParanoid; G3PTS6; -.
DR OMA; SANIIMM; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000015921; Expressed in camera-type eye and 5 other cell types or tissues.
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; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 11.
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; 7.
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; 8.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
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; 3.
DR PROSITE; PS50853; FN3; 8.
DR PROSITE; PS50835; IG_LIKE; 3.
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:UP000007635};
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 1254..1277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..92
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 104..203
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 216..298
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 305..395
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 400..496
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 498..591
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 596..692
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 697..805
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 806..900
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 904..999
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1003..1087
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1344..1599
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1519..1590
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1631..1890
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1808..1881
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
SQ SEQUENCE 1899 AA; 211547 MW; 3A418724F66F30F6 CRC64;
PPRFTRTPED QTGVQGGVAS FVCQATGDPQ PKIVWNKKGK KVSNQRFEVI EFDDGSGSVL
RIQPLRTPRD EAIYECHASN SAGELTASTR LSVLREDQLP PGFPTIYMGP QLKVVERSRT
ATMLCAASGN PDPEITWFKD FLPISFNNIG RIKQLRSVIA HSGGTPIRGA LQIEMSEESD
QGKYECVATN SDGTRYSTPA NLYVRAELRE VRRVPPRFSI PPADSEIMPG GNVNITCVAV
GSPMPYVKWM LGAEDLTPED DMPIGRNVLE LTDVRQSNNY TCVAMSTLGV IEAVAQIIVK
ALPKAPGNPE VTERTATSIT LTWDSGNPEP VSYYIIQHRA RGSEDPYKEI DGIATTRYSV
GGLSPYSHYD FRVAAVNTIG QGPSSEVVEA RTAEQAPSSP PRQVRGRMLS TTTAIIHWDE
PEEPNGQVVG YRVYYTSDNS LPVNQWEKQM VRSAHFITIQ GLTPNKTYYI RVLAFTSMGD
GPLSQDLQII AKTGVPSQPS EFKGEAKSET SILLSWVAPP QGGPDNLITG YELVYRRADD
TEEKKVSFEP STFHLLKNLK PFSSYTFQLA ARSRHGIGAY TNEVFIDTPQ TLPSAPPQDI
TCASPSSTSI LVSWAPPPVE FQNGVISGYS IQYSTTEGGR VSKSVEGIPP ESSPFLLEGL
EKWTEYGVTV RAQTEAGDGP ESLQLLIRTE EDVPSGPPRG VEAETVNASA VRVKWRAPAP
ERQHGHVRGY QVHYVRTHYG EPQGQPLIKD ILMEDAQREY GDSTEYEVVL GDLRADTAYS
VSVGAYTAKG DGARSKPVTV CSALPLPEKP RLSVSATDSG TALLQWHPQP NPPTPLLGYR
LTFGRLDVLP FTVVEFPTKE SRYTAQDIHK GAKYVFRLSS RNKMGYGEEA LGELTTPEDA
PSGYPENVVL EEASADSLRL AWKSVPLLEQ NGKIRKYSVL YKDVNSRGNA SEAEVAAPGA
AVLLEGLSAD TVYEVRLCAS TAVGAGPLSP AVQFRTRRLD QVFATNFRVK ASMKNSVLLS
WEIRDKNPTQ PFTILYGKGQ SVEVDGKQTQ KLIAGLEPDT LYSFLLTNRA NSAGGLQHRV
TATTAPDILK TKPTVVGKTN ADGMVTVQLP TVQTAAKVRG YYVVVLPLKK QRGGKFLNPW
EEPDQMNLEE LLKEMNRTGV SRALRSRRQA GQSDPRAYVS AHFKTLPLEF TLGDGRDHGD
FRNRPLQNGQ EYVFFVLALL DLSENTMYAT SPYSDPVTSS GVDPQPIVDE EEGLLWVVGP
VLAVIFIVCI VIAILLFKRK RAEAEGRKGS FPCSKAMSSH HPTDPVELRR INFQTPGMAS
HPPVPISELA DHSERLKAND NLKFSQEYES LDPGQQFTWE NSNLEVNKPK NRYANVIAYD
HSRVILSSIE GVPGSDYINS NYIDGYRRQN AYIATQGPLP ETFGEFWRMV WEQHTANIIM
MTKLEEKSRV KCDQYWPTRG TETYGLIQVT LLDTVELATY SVRTFALYKS GSNEKREVRH
FQFTAWPDHG VPEHPTPFLA FLRRVKACNP PDAGPMVVHC SAGVGRTGCF IVIDAMAERI
KQEKTLDVYG HVTLMRSQRN YMVQTEDQYI FIHDALLEAV TCGNTEVPAR NLYSYIQRLT
QMEPGENVTG MEVEFKRLAS AKAHTSRFVS ANLPCNKFKN RLVNIMPYET TRVSLQPIRG
VEGSDYINAS FIDGYRQQKA YIATQGPLAE TTEDYWRMLW EHNSTIVVML TKLREMGREK
CHQYWPAERS ARYQYFVVDP MAEYNMPQYI LREFKVTDAR DGQSRTVRQF QFTDWPEQGV
PKSGEGFIDF IGQVHKTKEQ FGQDGPITVH CSAGVGRTGV FITLSIVLER MRYEGVVDIF
QTVKMLRTQR PATVQTEGQY QFCYRGSLEY SERFDHYAT
//