MIG23_CAEEL
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 03-AUG-2022, entry version 139.
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; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC 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., Schvarzstein M.,
RA Jigami Y., Hisamoto N., Matsumoto K.;
RT "An NDPase links ADAM protease glycosylation with organ morphogenesis in C.
RT elegans.";
RL Nat. Cell Biol. 6:31-37(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX 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 investigating
RT 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 via
RT 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 mig-
CC 17 glycosylation and surface expression, which is required for proper
CC migration of distal tip cells during gonad morphogenesis.
CC {ECO:0000269|PubMed:14688791}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-
CC phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; EC=3.6.1.6;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:14688791, ECO:0000269|PubMed:16354716}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:14688791,
CC ECO:0000269|PubMed:16354716}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles.
CC {ECO:0000269|PubMed:14688791}.
CC -!- INDUCTION: In contrast to uda-1, expression is not induced by stress.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000305}.
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DR EMBL; AB126261; BAD02168.1; -; mRNA.
DR EMBL; FO080885; CCD67510.1; -; Genomic_DNA.
DR PIR; T16696; T16696.
DR RefSeq; NP_508994.1; NM_076593.5.
DR AlphaFoldDB; Q21815; -.
DR SMR; Q21815; -.
DR STRING; 6239.R07E4.4; -.
DR iPTMnet; Q21815; -.
DR EPD; Q21815; -.
DR PaxDb; Q21815; -.
DR PeptideAtlas; Q21815; -.
DR EnsemblMetazoa; R07E4.4.1; R07E4.4.1; WBGene00003254.
DR GeneID; 180860; -.
DR KEGG; cel:CELE_R07E4.4; -.
DR UCSC; R07E4.4; c. elegans.
DR CTD; 180860; -.
DR WormBase; R07E4.4; CE28748; WBGene00003254; mig-23.
DR eggNOG; KOG1386; Eukaryota.
DR GeneTree; ENSGT01050000244974; -.
DR HOGENOM; CLU_010246_6_1_1; -.
DR InParanoid; Q21815; -.
DR OMA; QDEIGPP; -.
DR OrthoDB; 1337265at2759; -.
DR PhylomeDB; Q21815; -.
DR Reactome; R-CEL-8850843; Phosphate bond hydrolysis by NTPDase proteins.
DR PRO; PR:Q21815; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003254; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; ISS:WormBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IMP:WormBase.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IMP:WormBase.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IMP:WormBase.
DR GO; GO:0046032; P:ADP catabolic process; IMP:WormBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0046712; P:GDP catabolic process; IMP:WormBase.
DR GO; GO:0035262; P:gonad morphogenesis; IMP:WormBase.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:UniProtKB-KW.
DR GO; GO:0009134; P:nucleoside diphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0060050; P:positive regulation of protein glycosylation; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0006256; P:UDP catabolic process; IMP:WormBase.
DR InterPro; IPR000407; GDA1_CD39_NTPase.
DR PANTHER; PTHR11782; PTHR11782; 1.
DR Pfam; PF01150; GDA1_CD39; 1.
DR PROSITE; PS01238; GDA1_CD39_NTPASE; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Glycoprotein; Golgi apparatus;
KW Gonadal differentiation; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..552
FT /note="Nucleoside-diphosphatase mig-23"
FT /id="PRO_0000209923"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 268
FT /note="G->E: In k166; reduced migration of the gonad arms
FT in both the anterior and posterior direction."
FT /evidence="ECO:0000269|PubMed:14688791"
FT MUTAGEN 290
FT /note="D->N: In k146; reduced migration of the gonad arms
FT in both the anterior and posterior direction."
FT /evidence="ECO:0000269|PubMed:14688791"
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
