ID NTP1_CAEEL Reviewed; 485 AA. AC Q18411; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 05-MAY-2009, entry version 48. DE RecName: Full=Nucleoside-triphosphatase ntp-1; DE EC=3.6.1.15; GN Name=ntp-1; ORFNames=C33H5.14; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for RT investigating biology."; RL Science 282:2012-2018(1998). RN [2] RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=15102851; DOI=10.1074/jbc.M402624200; RA Uccelletti D., O'Callaghan C., Berninsone P., Zemtseva I., Abeijon C., RA Hirschberg C.B.; RT "ire-1-dependent transcriptional up-regulation of a lumenal uridine RT diphosphatase from Caenorhabditis elegans."; RL J. Biol. Chem. 279:27390-27398(2004). CC -!- FUNCTION: Seems to be able to hydrolyze CTP, ATP and UTP. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass CC membrane protein (Potential). CC -!- MISCELLANEOUS: In contrast to uda-1, expression is not induced by CC stress. CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U41007; AAA82272.1; -; Genomic_DNA. DR PIR; T34147; T34147. DR RefSeq; NP_501289.1; -. DR UniGene; Cel.17788; -. DR Ensembl; C33H5.14; Caenorhabditis elegans. DR GeneID; 177567; -. DR KEGG; cel:C33H5.14; -. DR WormBase; WBGene00016380; ntp-1. DR WormPep; C33H5.14; CE04157. DR OMA; Q18411; ICDAGSS. DR BRENDA; 3.6.1.15; 672. DR NextBio; 897400; -. DR ArrayExpress; Q18411; -. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:EC. DR InterPro; IPR000407; GDA1_CD39_NTPase. DR PANTHER; PTHR11782; GDA1_CD39_NTPase; 1. DR Pfam; PF01150; GDA1_CD39; 1. DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Golgi apparatus; Hydrolase; Membrane; KW Transmembrane. FT CHAIN 1 485 Nucleoside-triphosphatase ntp-1. FT /FTId=PRO_0000209924. FT TRANSMEM 439 459 Potential. SQ SEQUENCE 485 AA; 54309 MW; DE64D1ADC20F581E CRC64; MSGGSSERVQ RSVRSVVETK NNIKYGVICD AGSSGTRLFV YTLKPLSGGL TNIDTLIHES EPVVKKVTPG LSSFGDKPEQ VVEYLTPLLR FAEEHIPYEQ LGETDLLIFA TAGMRLLPEA QKDAIIKNLQ NGLKSVTALR VSDSNIRIID GAWEGIYSWI AVNYILGRFD KENDSKVGMI DMGGASVQIA FEIANEKESY NGGNVYEINL GSIETNEDYK YKIYSTTFLG YGANEGLKKY ENSLVKSGNS NDSCSPRGLN RLIGEFTVNG TGEWDVCLAQ VSSLIGDKAQ PSCPNPTCFL RNVIAPSVNL STVQLYGFSE YWYTTSNFGS GGEYHYQKFT DEVRKYCQKD WNDIQDGFKR NEFPNADIER LGTNCFKAAW VTSVLHDGFN VDKTKHLFQS VLKIAGEEMQ WALGAMLYHS KDLKFNLLEQ LEVAQSTQQI SNFFSFFVIL IIVLAVALYR QLQSESTYKK YNFLRTDSKP DFLNV //