ID G1T1R8_RABIT Unreviewed; 604 AA.
AC G1T1R8;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 7 {ECO:0000313|Ensembl:ENSOCUP00000010043.3};
GN Name=ENTPD7 {ECO:0000313|Ensembl:ENSOCUP00000010043.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000010043.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000010043.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000010043.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000010043.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000010043.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AAGW02060763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_008268546.1; XM_008270324.2.
DR AlphaFoldDB; G1T1R8; -.
DR SMR; G1T1R8; -.
DR STRING; 9986.ENSOCUP00000010043; -.
DR PaxDb; 9986-ENSOCUP00000010043; -.
DR Ensembl; ENSOCUT00000011680.4; ENSOCUP00000010043.3; ENSOCUG00000011679.4.
DR GeneID; 100355397; -.
DR KEGG; ocu:100355397; -.
DR CTD; 57089; -.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01100000263540; -.
DR HOGENOM; CLU_010246_6_0_1; -.
DR InParanoid; G1T1R8; -.
DR OMA; LNCATKQ; -.
DR OrthoDB; 180318at2759; -.
DR TreeFam; TF354343; -.
DR Proteomes; UP000001811; Chromosome 18.
DR Bgee; ENSOCUG00000011679; Expressed in uterus and 15 other cell types or tissues.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043273; F:CTPase activity; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0006254; P:CTP catabolic process; IEA:Ensembl.
DR GO; GO:0046039; P:GTP metabolic process; IEA:Ensembl.
DR GO; GO:0034656; P:nucleobase-containing small molecule catabolic process; IEA:Ensembl.
DR GO; GO:0050776; P:regulation of immune response; IEA:Ensembl.
DR GO; GO:0072539; P:T-helper 17 cell differentiation; IEA:Ensembl.
DR GO; GO:0046052; P:UTP catabolic process; IEA:Ensembl.
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:SF37; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 7; 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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR600407-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 261..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 604 AA; 68756 MW; C27682282247C3E0 CRC64;
MARISFSFLC PASWYFTVPT VSPFLRQRVA LLGLFCISCL LLLMFIMDFR HWGASLPRDR
QYERYLARVG ELEATDTEDP NLSYGLVVDC GSSGSRIFVY FWPRHNGNPH DLLDIKQMRD
RNSQPVVKKI KPGISAVADT PEHASDYLRP LLSFAAAHVP VKKHKETPLY ILCTAGMRLL
PERKQLAILG DLVKDLPLEF DFLFSQSQAE VISGKQEGVY AWIGINFVLG RFDHEDESEA
ETSQELAGGR RRTVGILDMG GASLQIAYEV PTSTSVLPPK QEEAAKILLA EFNLGCDVQH
TEHVYRVYVT TFLGFGGNFA RQRYEELVLN ETLNKNRLLG QKTGLSPDNP FLDPCLPVGL
TDVLERNGHI LHIRGKGDWA TCGALLRPLL ARSNTSHASL NGIYQSPIDF NNSEFYGFSE
FFYCTEDVLR IGGHYHGPTF AKAAQDYCGM AWSVLTQRFK DGLFSSHADE HRLKYQCFKS
AWMYQVLHEG FHFPYDYSNL RTAQLVYDRE VQWTLGAILY KTRFLPLRDL RQEGVRQAHG
SWFRLSFVYN HYLFFACILV VLLAIILYLL RLRRIHHRQT RASAPLDLLW IEEVVPVIGG
QVGP
//
