ID H2N2M6_ORYLA Unreviewed; 1397 AA.
AC H2N2M6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 74.
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:ENSORLP00000025715.2};
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:ENSORLP00000025715.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000025715.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000025715.2,
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:ENSORLP00000025715.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000025715.2};
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 STRING; 8090.ENSORLP00000025715; -.
DR Ensembl; ENSORLT00000025716.2; ENSORLP00000025715.2; ENSORLG00000020763.2.
DR GeneTree; ENSGT00940000157151; -.
DR HOGENOM; CLU_001645_0_2_1; -.
DR InParanoid; H2N2M6; -.
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; IBA:GO_Central.
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 735..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..175
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 275..370
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 373..474
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 480..581
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 890..1121
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1041..1112
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1153..1362
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT REGION 811..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1397 AA; 157175 MW; 6B872D299EAA574E CRC64;
MKSNPIFCPL PAAGCTFEED SDPNLCDFTQ GEEDDFDWVL FRTYSSPLSS FDLLKGSYML
VNSSQHAAGH RAQLLLQTLS ENDTHCVQFS YFLYSRDGHS PGALRAYVRV NGGPLGNPVW
NISGSHGKQW HQVELAVSTF WPNEYQVLIE ATVSRERQGY IAVDDIMVLN YPCYKAPHFS
RLGEEEINAG QNATFQCVAA GKASEADKFL LERHNGDILT MASVKHLSHR RFVVSFQLDS
VQRSHQDLYR CVTQSLRGSG VSNFAELVVK VPPSPIAPPQ LLRAGSTYLI IQLNTNSILG
DGPIIRKEIE YRASQSPWSE VHGVNMAAYK LWHLDPDTEY HISVLLTRPG EGGTGPPGPP
LVSRTKCAEP MRPLRGLTAT EIQSRQLTLQ WENLAFNLTR CHTYSVSLCY RYTMAGGGGD
HNTTVRECLA VEHNASRFTL RDLPPYHSIH VRLSLANQEG KKEGREVIFQ TEEDIPGGIA
PESLTFTPLD DMIFLKWEEP VEPNGLITQY EISYQSIASS DPGINVPGPR RAVSKLKNET
YHMFSNLHPG TTYLISVRAR TAKGFGQTAL KEITTNISAP SFDYRDMPGP LNETESTITV
LLRPAQGRGA PVSTYQVVVE EEMVKKVKRE LGPQDCFPLP MPHSVAQAQG LPHYYAAEMP
PSTLPEASPF TVGDNHTYNG YWNSPLDPRK SYLVYFQAMS NFKGESRINC IRIARKASCK
DHRSVLERTQ HSEDMGLILA VCAGGLVVLV LLLGAVIIII KKGKPVNMNK 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 GRTVVHCLSL SGSVASQSEG RLLTQQIFFH
KESKPQNVVK QERLHFC
//
