ID H2N2M5_ORYLA Unreviewed; 1378 AA.
AC H2N2M5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
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};
GN Name=ptprub {ECO:0000313|Ensembl:ENSORLP00000025714.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000025714.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000025714.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000025714.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000025714.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000025714.2};
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 -!- 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}.
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DR Ensembl; ENSORLT00000025715.2; ENSORLP00000025714.2; ENSORLG00000020763.2.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000157151; -.
DR TreeFam; TF312900; -.
DR Proteomes; UP000001038; Chromosome 16.
DR Bgee; ENSORLG00000020763; Expressed in sexually immature organism and 12 other cell types or tissues.
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; 2.
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; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; 2.
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; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
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:UP000001038};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1378
FT /note="protein-tyrosine-phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017321755"
FT TRANSMEM 747..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 25..187
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 287..382
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 385..486
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 492..593
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 910..1141
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1061..1132
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1173..1378
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT REGION 831..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1378 AA; 155124 MW; 718CBA7D9C5AAEFA CRC64;
MNTCTFLLIL TVQIYADGIE GPTAAGCTFE EDSDPNLCDF TQGEEDDFDW VLFRTYSSPL
SSFDLLKGSY MLVNSSQHAA GHRAQLLLQT LSENDTHCVQ FSYFLYSRDG HSPGALRAYV
RVNGGPLGNP VWNISGSHGK QWHQVELAVS TFWPNEYQVL IEATVSRERQ GYIAVDDIMV
LNYPCYKAPH FSRLGEEEIN AGQNATFQCV AAGKASEADK FLLERHNGDI LTMASVKHLS
HRRFVVSFQL DSVQRSHQDL YRCVTQSLRG SGVSNFAELV VKVPPSPIAP PQLLRAGSTY
LIIQLNTNSI LGDGPIIRKE IEYRASQSPW SEVHGVNMAA YKLWHLDPDT EYHISVLLTR
PGEGGTGPPG PPLVSRTKCA EPMRPLRGLT ATEIQSRQLT LQWENLAFNL TRCHTYSVSL
CYRYTMAGGG GDHNTTVREC LAVEHNASRF TLRDLPPYHS IHVRLSLANQ EGKKEGREVI
FQTEEDIPGG IAPESLTFTP LDDMIFLKWE EPVEPNGLIT QYEISYQSIA SSDPGINVPG
PRRAVSKLKN ETYHMFSNLH PGTTYLISVR ARTAKGFGQT ALKEITTNIS APSFDYRDMP
GPLNETESTI TVLLRPAQGR GAPVSTYQVV VEEEMVKKVK RELGPQDCFP LPMPHSVAQA
QGLPHYYAAE MPPSTLPEAS PFTVGDNHTY NGYWNSPLDP RKSYLVYFQA MSNFKGESRI
NCIRIARKAS CKDHRSVLER TQHSEDMGLI LAVCAGGLVV LVLLLGAVII IIKKGRDYYS
YYPKPVNMNK TPITYRQEKS HMGSMERSFT DQSTLQEDER MALSFMDTHT CGTRSDARSS
VNEASSLLGG SPRHQCGRKG SPYHTGQLHP AVRVADLLQH INQMKTGEGY GFKQEYESFF
DGWDCTKKKD KIKGRQDTLL GYDRHRVKLH PLLGDPNSDY INANYIDGYH RSNHFIATQG
PKQETLYDFW RMVWQENCFS IVMITKLVEV GRVKCCKYWP DDSEMYGDIK ITLLKTETLA
EYTVRTFALE RRGYSTKHEV RQFHFTSWPE HGVPYHATGL LAFIRRVKAS TPPDAGPVVV
HCSAGAGRTG CYIVLDVMLD MAECEGVVDI YNCVKTLCSR RINMIQTEEQ YIFIHDAILE
ACLCGDTSIL MSEFAVTYKD MLRVDSQSNS SPLREEFQTL NSVTPHLDVE ECSIALLPRN
REKNRSMDVL PPDRALAFLV TTEGESNNYI NAALADSFHR QAAFIVTPHP LPGTTADFWR
LVFDYGCTAV VMLNQLNQSN SAWPCVQYWP EPGLQQYGPM EVEFLSMSAD EDVITRLFRV
KNVTRLQEGQ LVVCQFQFLR WSAYRDVPDS KKAFLNLLAQ VHKWQRECGE GRTVVHCL
//
