ID MIG23_CAEEL Reviewed; 552 AA. AC Q21815; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2002, sequence version 2. DT 16-JUN-2009, entry version 62. DE RecName: Full=Nucleoside-diphosphatase mig-23; DE Short=NDPase; DE EC=3.6.1.6; DE AltName: Full=Abnormal cell migration protein 23; GN Name=mig-23; ORFNames=R07E4.4; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND MUTAGENESIS OF GLY-268 AND ASP-290. RX PubMed=14688791; DOI=10.1038/ncb1079; RA Nishiwaki K., Kubota Y., Chigira Y., Roy S.K., Suzuki M., RA Schvarzstein M., Jigami Y., Hisamoto N., Matsumoto K.; RT "An NDPase links ADAM protease glycosylation with organ morphogenesis RT in C. elegans."; RL Nat. Cell Biol. 6:31-37(2004). RN [2] 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 [3] RP LACK OF INDUCTION BY STRESS. 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). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=16354716; DOI=10.1242/dev.02195; RA Kubota Y., Sano M., Goda S., Suzuki N., Nishiwaki K.; RT "The conserved oligomeric Golgi complex acts in organ morphogenesis RT via glycosylation of an ADAM protease in C. elegans."; RL Development 133:263-273(2006). CC -!- FUNCTION: Seems to be able to hydrolyze ADP, UDP and GDP. Supports CC mig-17 glycosylation and surface expression, which is required for CC proper migration of distal tip cells during gonad morphogenesis. CC -!- CATALYTIC ACTIVITY: A nucleoside diphosphate + H(2)O = a CC nucleotide + phosphate. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass CC membrane protein. CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles. CC -!- INDUCTION: 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; AB126261; BAD02168.1; -; mRNA. DR EMBL; U39652; AAA80403.2; -; Genomic_DNA. DR PIR; T16696; T16696. DR RefSeq; NP_508994.1; -. DR UniGene; Cel.6413; -. DR Ensembl; R07E4.4; Caenorhabditis elegans. DR GeneID; 180860; -. DR KEGG; cel:R07E4.4; -. DR WormBase; WBGene00003254; mig-23. DR WormPep; R07E4.4; CE28748. DR OMA; Q21815; SAWITSV. DR BRENDA; 3.6.1.6; 672. DR NextBio; 911292; -. DR ArrayExpress; Q21815; -. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IEA:EC. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW. 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; Developmental protein; Differentiation; KW Glycoprotein; Golgi apparatus; Gonadal differentiation; Hydrolase; KW Membrane; Transmembrane. FT CHAIN 1 552 Nucleoside-diphosphatase mig-23. FT /FTId=PRO_0000209923. FT TOPO_DOM 1 6 Cytoplasmic (Potential). FT TRANSMEM 7 27 Potential. FT TOPO_DOM 28 489 Lumenal (Potential). FT TRANSMEM 490 510 Potential. FT TOPO_DOM 511 552 Cytoplasmic (Potential). FT CARBOHYD 190 190 N-linked (GlcNAc...) (Potential). FT CARBOHYD 284 284 N-linked (GlcNAc...) (Potential). FT MUTAGEN 268 268 G->E: In k166; reduced migration of the FT gonad arms in both the anterior and FT posterior direction. FT MUTAGEN 290 290 D->N: In k146; reduced migration of the FT gonad arms in both the anterior and FT posterior direction. SQ SEQUENCE 552 AA; 62511 MW; E5DC32C858AE4D94 CRC64; MRVSLRFTIL AVSAMIFFPV IVFIYVVEAH TSPKVIADDQ ERSYGVICDA GSTGTRLFVY NWISTSDSEL IQIEPVIYDN KPVMKKISPG LSTFGTKPAQ AAEYLRPLME LAERHIPEEK RPYTPVFIFA TAGMRLIPDE QKEAVLKNLR NKLPKITSMQ VLKEHIRIIE GKWEGIYSWI AVNYALGKFN KTATLDFPGT SPAHARQKTV GMIDMGGASA QIAFELPDTD SFSSINVENI NLGCREDDSL FKYKLFVTTF LGYGVNEGIR KYEHMLLSKL KDQNGTVIQD DCMPLNLHKT VTLENGENFV RRGTGNWNTC SNEVKKLLNP ESSSEVCKAE AAKCYFGAVP APSIPLSNIE MYGFSEYWYS THDVLGLGGQ YDAENIAKKT QQYCSKRWST IQAESKKQLY PRADEERLRT QCFKSAWITS VLHDGFSVDK THNKFQSVST IAGQEVQWAL GAMIYHMRFF PLRDSSRNLI VKETHSSSES LWAPLFFLSA VFCLFVLVCA KEQSVLCFDD KRRSSFGMSR SQYSYKMLKE NRTSSSFLEN FA //