ID W5L9P2_ASTMX Unreviewed; 504 AA.
AC W5L9P2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Ectonucleoside triphosphate diphosphohydrolase 2 {ECO:0000313|Ensembl:ENSAMXP00000016554.2};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000016554.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000016554.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family.
CC {ECO:0000256|ARBA:ARBA00009283, ECO:0000256|RuleBase:RU003833}.
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DR AlphaFoldDB; W5L9P2; -.
DR STRING; 7994.ENSAMXP00000016554; -.
DR Ensembl; ENSAMXT00000016554.2; ENSAMXP00000016554.2; ENSAMXG00000016068.2.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01100000263542; -.
DR HOGENOM; CLU_010246_2_3_1; -.
DR InParanoid; W5L9P2; -.
DR OrthoDB; 180318at2759; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000016068; Expressed in pharyngeal gill and 14 other cell types or tissues.
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:SF33; ECTONUCLEOSIDE TRIPHOSPHATE DIPHOSPHOHYDROLASE 2; 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:UP000018467};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 469..494
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-1"
FT BINDING 206..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR600407-2"
SQ SEQUENCE 504 AA; 55558 MW; A03756309337ED32 CRC64;
MANQQQQCRL LVPLAVLLLG VVGILLLAIN SEDIEEPPQY MYGIVLDAGS SHTAMFIYKW
PANKQNGTGI VSQHSECDVD GGGISSYAGQ KGGAARSLEK CMDHAIQKIP KVRHHQTPIY
LGATAGMRLL NISQPKVSDE ILKEVGEKLK TYPFSVKGAT ILTGQEEGAY GWVTVNYLLE
NFIKYGFVGH WLSPGKKTVG ALDFGGASTQ ITFETKEKVE NVENLMKLRL YGRDYHIYTQ
SFLCYGRDQM LRKLLAHLVE TQGSNDAIIH PCYPADYNVS ITLDNVFDTP CTADSKPSPY
NAGKKLQIQG SGNYQHCLGN MSHIFSFQTC TYSKCSFNGV FQPNVSGNFM AFAAFFYIHS
FLKSTTGITV TSPSLLEEAA ITVCNMSFHE MLQKVPEQQS RLQDYCAATV FMKVLLLKGY
GFDRLSFPQI SFQKKAGETS VGWALGYMLS LSSLLPAESV SLRKALSPGA WNTLIFLFSV
ALFIALVSVC LIMFRKKKGS DGVL
//
