ID H3CAQ7_TETNG Unreviewed; 831 AA.
AC H3CAQ7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase alpha {ECO:0000256|PIRNR:PIRNR002006};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR002006};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000005329.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000005329.1}
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|PIRNR:PIRNR002006};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 4 subfamily. {ECO:0000256|ARBA:ARBA00007765,
CC ECO:0000256|PIRNR:PIRNR002006}.
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DR AlphaFoldDB; H3CAQ7; -.
DR STRING; 99883.ENSTNIP00000005329; -.
DR Ensembl; ENSTNIT00000005475.1; ENSTNIP00000005329.1; ENSTNIG00000002768.1.
DR GeneTree; ENSGT00940000159585; -.
DR HOGENOM; CLU_001645_8_2_1; -.
DR InParanoid; H3CAQ7; -.
DR OMA; TESWEGN; -.
DR TreeFam; TF351829; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IEA:Ensembl.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR CDD; cd14621; R-PTPc-A-1; 1.
DR CDD; cd14623; R-PTPc-A-2; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
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 InterPro; IPR016336; Tyr_Pase_rcpt_a/e-type.
DR InterPro; IPR027262; Tyr_Pase_rcpt_alpha.
DR PANTHER; PTHR19134; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR19134:SF433; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE ALPHA; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PIRSF; PIRSF500808; PTPR_alpha; 1.
DR PIRSF; PIRSF002006; PTPR_alpha_epsilon; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR002006};
KW Membrane {ECO:0000256|PIRNR:PIRNR002006};
KW Phosphoprotein {ECO:0000256|PIRSR:PIRSR002006-3};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR002006};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Signal {ECO:0000256|PIRNR:PIRNR002006};
KW Transmembrane {ECO:0000256|PIRNR:PIRNR002006};
KW Transmembrane helix {ECO:0000256|PIRNR:PIRNR002006}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|PIRNR:PIRNR002006"
FT CHAIN 19..831
FT /note="Receptor-type tyrosine-protein phosphatase alpha"
FT /evidence="ECO:0000256|PIRNR:PIRNR002006"
FT /id="PRO_5016196887"
FT TRANSMEM 182..205
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR002006"
FT DOMAIN 271..531
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 451..522
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 563..820
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 736..811
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 472
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR002006-1"
FT ACT_SITE 761
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR002006-1"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR002006-2"
FT BINDING 472..478
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR002006-2"
FT BINDING 516
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR002006-2"
FT MOD_RES 827
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000256|PIRSR:PIRSR002006-3"
SQ SEQUENCE 831 AA; 92886 MW; 41DE598C354DE0A0 CRC64;
MGVCPLLLLL ALALGASAQD YVPITKVPQI SLPSYGPPAT PPFRIPVAST QTPTGPPTTV
APTTAEAKTT TTTAAAAIPN PAGDDNLPQA GPNATGRVLP IPPAPTDAPQ RPPAVETPLP
PFTEGQDNAT AAAPSTPTPE TYIDEDTDVV DRESTSGLGV SFPTEPNPHD PEDNNQSVDV
PIIAVMVALS SLLVIIFIII ILYMLRFKKY KQAGSHSNSF RLTNGRSDDT ELQSVPLLAR
SPSTNRKYPP LPVDKLEEEM NRRMADDNKL FREEFNALPV CPIQASCDAA SKEENKEKNR
YVNILPYDHS RVHLSSLEGV PDSDFINASF INGYQEKNKF IAAQGPKEET VNDFWRMIWE
QNTATIVMVT NLKERKECKC AQYWPDQGCW TYGNIRVSVE DTMVLVDYTI RKFCIQQVGD
VSGKKPQRLV TQFHFTSWPD FGVPFTPIGM LKFLKKVKNC NPQYAGAIVV HCSAGVGRTG
TFIVIDAMLD MMIAERKVDV FGFVTRIRAQ RCQMVQTDMQ YVFIFQALLE HYLYGDTELE
VTSLESHLAK LYAPAPGAGC SGLEAEFKKL TSIKIQNDKM RTGNLPANMK KNRVLQIIPY
EFNRVIIPVK RGEENTDYVN ASFIDGYRQK DSYMASQGPL QHTMEDFWRM IWEWRSCSIV
MLTELEERGQ EKCAQYWPSD GTVYGDISIE IKKEEENESY TVRDLLVTNT RENKARAVRQ
FHFHGWPEVG IPTDGKGMIN LIAAVQKQQQ QSGNHPITVH CSAGAGRTGT FCALSTVLER
VKAEGILDVF QTVKSLRLQR PHMVQTLEQY EFCYKVVQEY IDAFSDYANF K
//
