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Database: UniProt
Entry: A0A2Y9NGH9_DELLE
LinkDB: A0A2Y9NGH9_DELLE
Original site: A0A2Y9NGH9_DELLE 
ID   A0A2Y9NGH9_DELLE        Unreviewed;      1439 AA.
AC   A0A2Y9NGH9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
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|RefSeq:XP_022428388.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022428388.1};
RN   [1] {ECO:0000313|RefSeq:XP_022428388.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022428388.1};
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 5 subfamily. {ECO:0000256|ARBA:ARBA00006246}.
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DR   RefSeq; XP_022428388.1; XM_022572680.1.
DR   Proteomes; UP000248483; 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   CDD; cd17667; R-PTPc-G-1; 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   Receptor {ECO:0000313|RefSeq:XP_022428388.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
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        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        731..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..321
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000259|PROSITE:PS51144"
FT   DOMAIN          349..448
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          842..1113
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1030..1104
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          1144..1404
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1321..1395
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          461..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..589
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..701
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1439 AA;  161081 MW;  C89F5C4F7058C50C CRC64;
     MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYMGALHE NRQGSSVQIR RRKASGDPYW
     AYSGAYGPEH WVTSSVSCGG HHQSPIDISD QDARVGEEYQ DLQLDGFDNE SSNKTWMKNT
     GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSINGRRF PVEMQIFFYN
     PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFVLRD
     LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RTPVPISYHQ LEAFYSIFTT EQQDHVKSVE
     YLRNNFRPQQ DLNDRVVSKS AVRDAWNHDM TDFLENPLGT EASKVCSSPP IHMKVQPLNQ
     TALQVSWNQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SPVSPDSLYL
     FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
     TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FSGGGISSFP STVWPTRLPT
     AAAASKQAGR PVPATPEALA SPGPDGDSAP TKDGEGAEEG EKDEKSENED GEREHEEEGE
     KGSEKKERNG VTHAPQARSG TEPSPAPSAP GRADQDGGRQ TIAGRERDRA AVPTAQPEDA
     LDPRPVTLTQ VPPTVTEEHY RENDPKRPET PSKKPMSPGD RFSEDSKFIT VNPEKNTSGM
     ISRPSPGRME WIVPLIVVSA LTFVCLILLI AVLVYWRGCN KIKSKGFPRR FHEVPSSGER
     GEKGSRKCFQ TAHFYVEDSS SPRVVPNESI PIIPIPDDME AIPVKQFVKH IGELYSNNQH
     GFSEDFEEVQ RCTADMNITA EHSNHPDNKH KNRYINILAY DHSRVKLRPL PGKDSKHSDY
     INANYVDGYN KAKAYIATQG PLKSTFEDFW RMIWEQNTGI IVMITNLVEK GRRKCDQYWP
     TENSEEYGNI IVTLKSTKVH ACYTVRRFSV RNTKVKKGQK GNPKGRQNER VVIQYHYTQW
     PDMGVPEYAL PVLTFVRRSS AARTPEMGPV LVHCSAGVGR TGTYIVIDSM LQQIKDKSTV
     NVLGFLKHIR TQRNYLVQTE EQYIFIHDAL LEAILGKETE VSSSQLHSYV NSILIPGAGG
     KTRLEKQFKL VTQCNAKYVE CFSAQKECNK EKNRNSSVVP SERARVGLAP LPGMKGTDYI
     NASYIMGYYR SNEFIITQHP LPHTTKDFWR MIWDHNAQII VMLPDNQSLA EDEFVYWPSR
     EESMNCEAFT VTLISKDRLC LSNEEQIIIH DFILEATQDD YVLEVRHFQC PKWPNPDAPI
     SSTFELINVI KEEALTRDGP TIVHDEYGAV SAGMLCALTT LSQQLENENA VDVFQVAKMI
     NLMRPGVFTD IEQYQFVYKA MLSLVSTKEN GNGPMTVDKN GAVLMADESD PAESMESLV
//
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