ID A0A3Q3MWP4_9LABR Unreviewed; 1367 AA.
AC A0A3Q3MWP4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000025580.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000025580.1}
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|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; 56723.ENSLBEP00000025580; -.
DR Ensembl; ENSLBET00000026868.1; ENSLBEP00000025580.1; ENSLBEG00000019448.1.
DR GeneTree; ENSGT00940000155048; -.
DR InParanoid; A0A3Q3MWP4; -.
DR Proteomes; UP000261660; Unplaced.
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:SF449; RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE GAMMA; 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:UP000261660};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692}.
FT DOMAIN 1..265
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT DOMAIN 293..392
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 768..1040
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 957..1031
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1071..1331
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 1248..1322
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 478..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1367 AA; 152784 MW; 0B3DBE7AED20D162 CRC64;
MSCFPSGIYG PDEGWLTAYP QCRERNQSPI NIGEQDAKIS TEFQEMTLEG FDTESSNKTT
MKNTGKTVAI MLKDDYFVRG AGLPGRFKAE KVEFHWGPSN GSDGSEHSIN GRRYPVEMQI
YMYNSDDFDS LGAALREKRI IAAMAVFFQV GGKDNPAVDP IIHGLKGVVH HEKETVLEPF
VLKDLLPSSL GSYYRYTGSL TTPPCSKVVE WIIFSRPIYV SYKQLEAFYS IFTTEQQDHV
KSVEYLRSNF RPIQSLDNRH VFKSAVKDAW MPDLTDGSSG PYGTETSKVC SSAPINMKVQ
HVNSSALVVR WDRPEVTYHP PILFFLVSYS WTAHDDSYEE TYLTPATHRL EAIISPVSPD
VLYLFRVQAA CMNDMRSDFS QSMLFRANTT RVFEGTRIVK TGMPTVSPAS SADMAPISSG
SSTWTSSGIP FSFVSMATGI GPSSSGSQAT VASVVTSTLL AGLGFSGGVI SSFPSSVWPS
RAPTRNPAST HQTAEPTEPA KDAAASPSAA ATTSANDNGE VAGEERENSK GQGEDGEREG
EEKEEEEEED EKDEKKGRKR SRSEGKERRK NNSAEVNEPT SQTPDATAKE KKQTEPDPSN
MLPVVEDQMD VYTHSPLDSN STITTEADDD MEAYPALKGP AATLRSSTGR KKQWPFSIQT
DRPSAVTNLT HQVRTGSGAG LGRVEWLVPL GVVSALTFLC LVLLLVVLVY WRRCFQTAHF
YVEDSNSPRV VPNETLPVIP IPDDMEAVSV KQFIKRVYEL HSNNHHGYSE DFEEVQRCTA
DMKITSEHSN HPDNKHKNRY INIVAYDHSR VKLRPLAGKD SKHTDYINAN YVDGYNKPQA
YIAAQGPLKS TFEDFWRMVW EQNTGVIVMI TNLVEKGRRK CDQYWPTENS EEYGNMLVTL
KSTKVHACYT VRCFTLRNTK VKKSVKGNPK ARAQSERTVH QFHYTQWPDM GVPEYTLPVL
TFVRRSSAAQ TPDMGPMLVH CSAGVGRTGT YIVIDSMLRQ IKDKNTVNVL GFLKHIRTQR
NYLVQTEEQY IFIHNALMEA ILGKETEVSA RQLHSYFSNI STPGHSGGTR LEKQFKLVTQ
CNARFTDCFN AQKECNKEKN RNSSVVPSER ARVGLAPLPG VKGTDYINAS YIMGYYRSNE
FIITQHPLPH TTKDFWRMIW DHNAQIIVML PANHGLAEDE FVYWPSREEA MNCEAFTVTL
ISKDRLCLSN EEQISIHDFI LEATQDDYVL EVRHFQCPKW PNPDAPISST FELINVIKEE
AASRDGPTIV HDELGAVSAG TLCALTTLSQ QLESEGAVDV YEVAKMINLM RPGVFAYIDQ
YEYLYKALLS LVSTKDSGSA LLSRDINVTM GSISDHSDQA ESMESLV
//
