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Database: UniProt
Entry: W5K060_ASTMX
LinkDB: W5K060_ASTMX
Original site: W5K060_ASTMX 
ID   W5K060_ASTMX            Unreviewed;      1368 AA.
AC   W5K060;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPRZ1 {ECO:0000313|Ensembl:ENSAMXP00000000970.2};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000000970.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000000970.2}
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   -!- 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 5 subfamily. {ECO:0000256|ARBA:ARBA00006246}.
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DR   STRING; 7994.ENSAMXP00000000970; -.
DR   Ensembl; ENSAMXT00000000970.2; ENSAMXP00000000970.2; ENSAMXG00000000934.2.
DR   eggNOG; KOG0789; Eukaryota.
DR   GeneTree; ENSGT00940000155529; -.
DR   HOGENOM; CLU_001120_2_0_1; -.
DR   InParanoid; W5K060; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000000934; Expressed in zone of skin and 12 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd03122; alpha_CARP_receptor_like; 1.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR041887; Alpha_CARP_receptor-type.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
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; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR19134:SF461; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ZETA; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
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   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1368
FT                   /note="protein-tyrosine-phosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017279057"
FT   DOMAIN          39..302
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          316..413
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          766..1042
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          959..1033
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1073..1334
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1251..1325
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          438..472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1343..1368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1368 AA;  152683 MW;  BC0BCCF41114BC69 CRC64;
     MESLDSKCAL SLALLLICQI VEVSQAYGFR SQKKLAENID WSYAGTLNQN NWAKKYPSCN
     NAKQSPINIE ESLSQVKVQY QKLRLEHWDQ DTSDFTTVKN DGKTVAIDVG GEFFISGGGL
     RSRFKVGRLT FHWGRCNASS DGSEHSLNGV KFPLEMQIYC HEDNHSSVDA AIRDGGRITA
     LSVFIETSVE DNENYAAIID AVNSVSRHGK TGSVSPFTLQ GLLPNSTEKY FIYNGSLTSP
     PCSETVEWIV FKNTAAISEA QLEMFCEVMT MQQAGYVMLM DYLQNNYREQ QSQFMGQVFS
     SYTGTEELLT PVCSTEPENV QAYPHNYTSL LVIWERPRAV YDASIEKYSV TYRQIQGEDP
     PTLEYLTDGD QDVGAIIQDL AANTSYMVQV VAVCTNGLNG RTSEQLIVDM PVNDPETDPD
     PDPFELDEEE SYQPNPFLVR HDLNQPPYPV RTTTPRPRFT TTDPPVPPIF GVTSRATTTT
     IATTTTIATT TATTTAISTT TSTEIQVQYT PQTAQTTTIT TLMTDLLAPE SDYSGSSEPT
     DLLTSESHYS SSTTLIMATE GDSSSHTFVE PTVETVTPDA ESSSTSAVAG GEEVIDSIDN
     SGDSTVSVTT VTTVSPLSEN FATSTSSLPP PEVPLQPTTP SVPFPTTTAF SAVLLQTTQP
     VFKDASNSSH ESRVSLVGSV ERQRKAVVPL AVVSTLTFLC LVILIGILIY WRKCFQTAHF
     YIEDSTSPRV ISTSPAHLLL RTDEHEPLSV KQFVKHVAEL HNNNSFSREF QILKECFEEV
     QACTVDLGTT TDSSNHPENK TKNRYVNILA YDHSRVRLSA QSDKDGKNEG DYINANFVDG
     FNQQRAYIAA QGPLKSSTVD FWRMVWEQNV GVIVMITNLV ENGRRKCDQY WPLETQEEYG
     CFLVTVKSTE VMAYYTQRTF TIRNTHVKKG SQKGRANERT VTHYHYTQWP DMGVPEYVLP
     VISFIRRSSR ARTQDMGPVV VHCSAGVGRT GTYIVLDSMM KQISEQGLVN ILGFLKHIRT
     QRNYLVQTEE QYVFIHDALV EAILSKETEV PTSRVHNYVN ELLTTGPSCR TRLEKQFKLV
     NQSSAKQCDY SSALKDCNRE KNRSSSLIPV ERSRICLSTS ADETTDYINA SYILGYRKSS
     EYIITQNPLP ATVKDFWRMI WDHNAQVIVS LPDTSSLTEE PEPMIFWPKR DQPISCSMFT
     VSLGREERVC MSNEEMLIVQ DYILEATKDD YVLEVRHYRA PRWPNPDAPI SNTFELINII
     QRERSLKEGP IVVHDDYGGV TAGTFCALHT LLQQLETDSS VDVYLVAKMI NLMRPGVFTD
     IEQYQFLYKA ILSLVGTQED EKALQSSDNN GAVPGGPASA TESLESLV
//
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