ID G5B9R9_HETGA Unreviewed; 667 AA.
AC G5B9R9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 4 {ECO:0000313|EMBL:EHB06030.1};
GN ORFNames=GW7_20745 {ECO:0000313|EMBL:EHB06030.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB06030.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB06030.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR EMBL; JH169129; EHB06030.1; -; Genomic_DNA.
DR AlphaFoldDB; G5B9R9; -.
DR STRING; 10181.G5B9R9; -.
DR eggNOG; KOG1386; Eukaryota.
DR InParanoid; G5B9R9; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.30.420.150; Exopolyphosphatase. Domain 2; 1.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; ADENOSINE/GUANOSINE DIPHOSPHATASE; 1.
DR PANTHER; PTHR11782:SF29; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 4; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Hydrolase {ECO:0000256|RuleBase:RU003833, ECO:0000313|EMBL:EHB06030.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 48..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 333..337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 667 AA; 74964 MW; 3DE3EFE98588A441 CRC64;
MPPTCGPALP GAPACRSGEA AFPRWRTEGG RAARAAGVSG AGGPAGALYP PEPSGCADPA
AQPRAHIRAP RDPGASISPV SCPRILSTNL RQIVVISVLA AAVSLLYFSV VIIRNKYGRL
SKDRKFQRYL ARVTDVEATD TNNPSVNYGI VVDCGSSGSR IFVYCWPRHN GNPRDLLDIR
QMRDKNRKPV VMKIKPGISE FATSPEKVSD YISPLLNFAA EHVPRAKHKE TPLYILCTAG
MRVLPESQQK AILEDLLTDI PVHFDFLFSD SHAEVISGKQ EGVYAWIGIN FVLGRFEHIE
EDDEAIVEVS LPGSENSEAI IRKRTAGILD MGGVSTQIAY EVPETEEVAK NLLAEFNLGC
DVHQTEHVYR VYVATFLGFG GNAARQRYED RLFASVFQKN RLLGKQPGLT REAPYLDPCL
PLDIKDEIQQ NGQTMYLRGT GDFDLCRETL QPFMNKTNET QTSLNGVYQP PIHFRNSEFY
GFSEFYYCTE DVLRMGGDYN AAKFTKAAKD YCATKWSILR DRFDRGLYAS HADLHRLKYQ
CFKSAWMFEV FHRGFSFPNN YRNLKTALQV YDKEVQWTLG AILYRTRFLP LRDIQQEAFR
ASHSHWRGVS FVYNHYLFSG CFLVVLLSIL LYLLRLRRIH RRPLRAGSAA ALWMEEGLPS
QKGAGTL
//
