ID A0A3Q2GI96_CYPVA Unreviewed; 1910 AA.
AC A0A3Q2GI96;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000026560.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000026560.1}
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; ENSCVAT00000016770.1; ENSCVAP00000026560.1; ENSCVAG00000012259.1.
DR GeneTree; ENSGT00940000155060; -.
DR Proteomes; UP000265020; Unplaced.
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; 8.
DR CDD; cd05738; IgI_2_RPTP_IIa_LAR_like; 1.
DR CDD; cd05739; IgI_3_RPTP_IIa_LAR_like; 1.
DR CDD; cd14629; R-PTP-F-2; 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:SF1; PHOSPHATIDYLINOSITOL PHOSPHATASE PTPRQ; 1.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF07679; I-set; 2.
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; 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 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:UP000265020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1910
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018685191"
FT TRANSMEM 1254..1277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..126
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 138..233
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 241..323
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 330..420
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 425..519
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 523..612
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 617..714
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 719..818
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 819..913
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 917..1009
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1012..1096
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1355..1610
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1530..1601
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1642..1901
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1819..1892
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 406..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1910 AA; 213347 MW; 218C872B0C75CDE9 CRC64;
MVPNIHLAGP LLHRGALLLL FLLGSKVISS LADNRPQFIK TPEDQTGVSG GVASFVCQAS
GEPRPRITWM KKGKKVSSQR FEVIEFDDGS GSVLRIQPLR THRDEAIYEC TATNSVDEIH
ASAKLTVLDE DQIPHGFPVI DMGPQLKVVE RTRTATMLCA ASGNPDPEIS WYKDMLPVDI
NSSNGRIKQL RSGGTPIRGA LQIENSEMSD QGKYECVAMN SAGTRYSAPA NLYVRVRRVP
PRFSIPPTNQ EVMPGGSVNL TCVAVGSPMP FVKWTMGQLE LTKEEELPLG RNVLEVTNIR
ESANYTCVAM SSLGVIDATA QVIVKALPKP PTSLTVTETT ATSVTLTWDS GNPEPVSYYM
IQYRAKSSDN GFQEVEGVAT TRYSIGGLSP YSEYEFRVMA VNNIGRGPPS DPVETRTGEQ
APSSPPLHVQ ARMLSASTML VQWEPPEEPN GQIRGYRVYY SSDMTAPLSA WQKHNTDDSS
LTTISGLTPE ITYSLRVLGF TSVGDGPPSD ILQVKTQQGV PAQPSSFEAE AELDSRISLS
WLWPVQDQIT KYELQYWEAG SDSKKHVTFN PAGSYAVDGL KPDTLYYFSL AARSETGLGV
YTQPIQARTA QSTPSAPPQE VHVVSLTSTS LKVSWVAPPA DSRHGAIVRY TISYQAPAGE
DTERHDVSDI GADATSYVLE GLEKWTEYDV WVRAHTDVGP GPESVPVKIR TKEDVPGAPP
RKLEVDAINS TAIRVTWKPP VQVKQHGQIR GYQVIFSRLE NGEPRGQPNI MDVALPEAQE
AIIGGLHAET TYSVTVAAYT TKGDGARSKA KVVTTTGAVP GKPTMMISTT MGNTALIQWQ
PPKEMVGELI GYQLQYKRTD EEAFTSLELS KTKDHHTVTE LHKGATYIFR LSARNRAGAG
EAYVKEISTT EDKPTGFPLN LKVTGLTQSS TQLTWEPPNL KERNGKITHY LVVYRDINNQ
QDNTSSTEDT HLTIEGLNPD TTYDIRVQAF TSKGGGPLSP SIQSRTMSND FPTLNFGVKA
VTKTSVLLTW DLPENHKSQA PFKILYNQQS VEVEGNQKRK LITQLQPDTD YSFVLTSRGI
IAGGLQQQVS IRTAPDLIKT KPITETPQGG KSTINLPKVQ TTSRVRWYYI VVVPQTESMQ
RWKNPDEMDL EELLRSREGP VLRRRRHVDS PRAYVAAKLA HLPETFTLGD DKEYMGFRNK
PLTNQQQYLC FVVAVLRNEG TDGAANYMTF SASPYSDPIH IEPDKAPMTD PPEMLWVMGP
VLAVVVIIII VIAILLFKKK RASPLPKDEH SGGVKDSLLA NSSDPVEMRR LNYQTPGPSS
HRCPNTPRMR EHPPIPVIDL ADHIERLKAN DGLRFSQEYE SIDPGQQFTW ENSNMEVNKP
KNRYANVIAY DHSRVVLTSV DAVPGSDYIN ANYIDGYRKQ NAYIATQGPL PETLSDFWRM
VWEQRANTIV MMTRLEEKSR VKCDQYWPSR GTETYGMIQV TMLDTVELAT YSVRTFLLYK
SGSTEKREVR QFQFMAWPDH GVPEYPTPIL AFLRRVKACN PPDAGPMVVH CSAGVGRTGC
FIVIDAMLER MKHEKTVDIY GHVTCMRSQR NYMVQTEDQY IFIHEALLEA ATCGNTEVPA
RNLYAHIQKL TQPPSGETVT AMELEFKRLA NSKAHTSRFI SANLPCNKFK NRLVNIMPFE
STRVCLQPIR GVEGSDYINA SFIDGYRQQK AYIATQGPLA ETTEDFWRML WEHNSTIVVM
LTKLREMGRE KCHQYWPAER SARYQYFVVD PMAEYNMPQY ILREFKVTDA RDGQSRTIRQ
FQFTDWPEQG VPKTGEGFID FIGQVHKTKE QFGQDGPITV HCSAGVGRTG VFITLSIVLE
RMRYEGVVDL FQTVKTLRTQ RPAMVQTEDQ YQLCYRAALE YLGSFDHYAT
//