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Database: UniProt
Entry: A0A3Q3G2S7_9LABR
LinkDB: A0A3Q3G2S7_9LABR
Original site: A0A3Q3G2S7_9LABR 
ID   A0A3Q3G2S7_9LABR        Unreviewed;      1375 AA.
AC   A0A3Q3G2S7;
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};
GN   Name=PTPRG {ECO:0000313|Ensembl:ENSLBEP00000025979.1};
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:ENSLBEP00000025979.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000025979.1}
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.ENSLBEP00000025979; -.
DR   Ensembl; ENSLBET00000027271.1; ENSLBEP00000025979.1; ENSLBEG00000019629.1.
DR   GeneTree; ENSGT00940000155048; -.
DR   InParanoid; A0A3Q3G2S7; -.
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   CDD; cd17670; R-PTP-G-2; 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, ECO:0000256|SAM:Phobius};
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, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        696..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..286
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          314..413
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          778..1049
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          969..1040
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1080..1340
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1257..1331
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          497..664
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        533..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        563..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..592
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..664
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1375 AA;  155037 MW;  FB4001114C59178A CRC64;
     MLKWLSCHFL PTNVYVFHKL LFFSISAGSH GPRGWDASYP ECGAKNQSPV NIADEQTLVS
     EEYQELVLEK FTAESSNQTT MKNTGKTVAV LLKDDYFVRG AGLPGRFKAE KMEFHWGQSN
     GSAGSEHSIN GRRFPVEMQI YLYNSDDFDS LSAAIKERRI IAAMAVFFEV KYNQDNPAVE
     PIIQGLKGVV HHEKETHLRS FILRDLLPSS VDSYYRYTGS LTTPPCSKVV EWIIFSRPVY
     LSHSQLEFFY HIFTTEQQDH VKSVDYLRNN FRHLQNLDNR KVYKSAVKDA WQRDLTEIME
     SPHGTESSRV CSSAPVSMKI KPLNQTALMV SWERPLTDYH PPITSYMVSY SWVKRDVADE
     KTFTKTGDQS MKAVITNVSP DVLYLFRVQA VCQHDLRSDF SQTLLFRANT TRIFEGSRIV
     KTGMPTISPA SSADMAPISS GSSTWTSSGI HFSIVSMATG MGPSSSGSQA TVASVVTSTL
     LAGLGVSGGV LSSLPSSAWP TQAPKATQNP TRPSAPPEKS STEQAPPRAS ETDAPSEESK
     AKREGEGSEK EEEEEGEGEQ EEGEDEKKTK SKTGAHNEEK QANSTVANEP FIPTPASTAK
     EKGEGNSTVR GSTAPESTAD DQLVNVENNH TDINAVSTQE PRNDSAEMQI PQSSTLSPKI
     NRDDKSNWPF SVHTGELTSH SFTDIHPQQG MGRMVWIVPL VVVSALTLLC LIMLLIVMVY
     WRRFFQTAHF YVEESSSPRV VANENIPVIP IPDDMEAIPV KHFVKHIMEL YKNNLQGFSE
     EFEEVQRSTA DLKITAEHSN HPDNKHKNRY INIVAYDHSR VKLRALAGKD AKHSDYMNAN
     YVDGYNRPRA YIAAQGPLKS TFEDFWRMVW EQNTGIIIMI TNLVEKGRRK CDQYWPMENS
     EQYGNIVVTL KSTKVHACYT HRRFHIRNTK VKKGQKGNPK WKLNERIVVQ YHYTQWPDMG
     VPEYTLPVLT FINRSSAART ADMGPVLVHC SAGVGRTGTY IVIDSMLQQI KDKSTVSVLD
     FLKHIRTQRN YLVQTEEQYV FIHDALMEDI LSRETEVPAW QLHSYVNSIL TPNSAGRTQL
     EKQFRLLTQC NTRFVECFSA HKDSNKEKNR NSSVVPSERA RVGLTTLPGM KGTDYINASY
     IMGYFRSNEF IITQHPLPHT TTDFWRMIWD HNAQIIVMLP DNLGLAEDEF VYWPSREEAM
     NCIAFTVTLI SKDRLCLSNE EQIIIHDFIL EATQDDYVLE VRHFQCPKWP NPDAPLSSAF
     ELISVIKEEA MTRDGPTIVH DEYGAVSAGM LCALTTLSQQ LENEGVVDIY QVAKMINLMR
     PGVFTDIEQY QYLYKAMLSL VGNRECSLSP MHMDTNGVVV IADESDPAES MESLV
//
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