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Database: UniProt
Entry: A0A2R8QCZ8_DANRE
LinkDB: A0A2R8QCZ8_DANRE
Original site: A0A2R8QCZ8_DANRE 
ID   A0A2R8QCZ8_DANRE        Unreviewed;      1478 AA.
AC   A0A2R8QCZ8; A0A8M2B6M2;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=ptprua {ECO:0000313|Ensembl:ENSDARP00000150888,
GN   ECO:0000313|RefSeq:XP_005159609.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-060503-232};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000150888};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000150888, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000150888};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000150888}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000150888};
RG   Ensembl;
RL   Submitted (APR-2018) to UniProtKB.
RN   [3] {ECO:0000313|RefSeq:XP_005159609.1}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_005159609.1};
RG   RefSeq;
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   EMBL; AL929594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX000467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR848723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU633478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU856379; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005159609.1; XM_005159552.4.
DR   STRING; 7955.ENSDARP00000150888; -.
DR   Ensembl; ENSDART00000189521; ENSDARP00000150888; ENSDARG00000092638.
DR   Ensembl; ENSDART00000189521.1; ENSDARP00000150888.1; ENSDARG00000092638.6.
DR   GeneID; 563584; -.
DR   AGR; ZFIN:ZDB-GENE-060503-232; -.
DR   CTD; 563584; -.
DR   ZFIN; ZDB-GENE-060503-232; ptprua.
DR   OrthoDB; 2875525at2759; -.
DR   ChiTaRS; ptprua; zebrafish.
DR   Proteomes; UP000000437; Chromosome 19.
DR   Bgee; ENSDARG00000092638; Expressed in brain 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   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; 1.
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; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
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; 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};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Receptor {ECO:0000313|RefSeq:XP_005159609.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..1478
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041163689"
FT   DOMAIN          24..186
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..488
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          494..595
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          921..1158
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1078..1149
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1190..1471
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1387..1462
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          654..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..875
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..860
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1478 AA;  166509 MW;  AC8004D205094C68 CRC64;
     MNLCAVLLFL IARVCAESLE GPTAGCTFEE DSDPTLCEYR QAQEDDFDWQ LVRTYSWPHM
     TSDLIRGSYM LVNASQYGAG QRAQLMLRPL SENDTHCVQF SYFLYSRDGH SPGGLNVYVR
     VNGGSRGNAV WNVSGSQGRQ WHQVEMAVST FWPSEYQIVF EATISSEQKG YIGLDDIVLL
     NYPCYKVPHF SRLGDVEVNA GQNATFQCVA TGRSVKTDPF LMERRNGVLM APYSVTSSIG
     ERRLVAWFQV GGAQRGEQDL YRCITQSTFG AAVSNFAELI VRVPPTPIAP PQLLRSGPTY
     LIIQLNTNSI VGDGPVIRRE IVYRASHSPW SETHGVNSLT YKVWHLEPDT EYRISVLLTR
     PGEGGTGPPG PPLVSRTKCA EPMRPLRGLT ATEIQSRQLL LQWEPVGYNL TRCHTYSLSL
     CYRYSTATGG GAGGNNATVR ECLSVERNTS RFTLRDLPPF HTVHVRLALA NPEGKKESRE
     VTFQTEEDIP GGIAPESLTF TPLDDMIFLK WEEPLEPNGL ITQYEISYQS IESSDPSINV
     PGPRRTVSKL KNETYHMFSG LHPGTTYLVS VRARTAKGFG QTALTEITTN ISAPAFDYED
     VPSPLSESES TITVLLRPAL GRGAPVSTYH VVVVEEDGSR QVRRRELGHM ECFPAPSSHG
     ETSGGAGGTP PHYYTAELSP SSLPEATPFT VGDNHTYSGY WNTPLDPSKN YLIYFQASSN
     FRGETRINCI RIARKVACKD HKRALEVSQH AEDMGLILGA CAGGLVVLIL LLGAIVVIVK
     KGRDIYSYPY YPRKKVNINK AVMTYRQEKT CKLGSLDCST TEHSTLQQDD RTAHTFLDSH
     NCTARNEQRS TVNESSSLLG GSPRRHCRRK SSPYHTGQLH PAVRVADLLQ HINQMKTGEG
     YGFKQEYESF FDGWDINDKK DKTKGRHDTL LGQDRHRVKM HSLLADPNSD YVNANYIDIR
     INREGYQRSN HFIATQGPKQ DMIYDFWRMV WQENCYSIVM ITKLVEVGRM KCCKYWPDDS
     ELYGDIKITL LKTETLAEYT VRTFAMERRG YPAKHEVCQF HFTSWPEHGV PYHATGLLAF
     LRRVKASTPP DAGPVVVHCS MGAGRTGCYI VLDVMLDMAE CEGVVDIYNC VKTLCSRRIN
     MIQTEEQYIF IHDAILEACL CGETAIPITE FGLSYKDMLS VDSQTNTSQL REEFQTLNSV
     TPHLDVEECS VSLLPRNREK NRSMDVLPPD RALAFLVSNE GDGNNYINAA LMDSFLQPAA
     FVVTPHPLPT TTTDFWRLVF DYGCTSIVML NQLNQSNSAW PCLQYWPETG MQQYGPMTVE
     LLSRSTDENV VTRLFRVNNI TRDPRENLPC WNADSRIPKK LQEGHLVVRH FQFLRWSAYR
     EIPDSKKAFL NLLAQVQKWQ RECGDGRTIV HCLNGGGRSG TFCACTMIME MVHHHNMVDV
     FYAVKTLRNS KPNMVESMEQ YRFCYELALE YLDCLEVR
//
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