MIG23_CAEBR
ID MIG23_CAEBR Reviewed; 553 AA.
AC Q617Y0; A8XKN6;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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 {ECO:0000250|UniProtKB:Q21815}; ORFNames=CBG14784;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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 (By
CC similarity). {ECO:0000250|UniProtKB:Q21815}.
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:0000250|UniProtKB:Q21815}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q21815}.
CC -!- SIMILARITY: Belongs to the GDA1/CD39 NTPase family. {ECO:0000255}.
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DR EMBL; HE600983; CAP33210.3; -; Genomic_DNA.
DR RefSeq; XP_002644771.1; XM_002644725.1.
DR AlphaFoldDB; Q617Y0; -.
DR SMR; Q617Y0; -.
DR STRING; 6238.CBG14784; -.
DR EnsemblMetazoa; CBG14784.1; CBG14784.1; WBGene00035179.
DR GeneID; 8586767; -.
DR KEGG; cbr:CBG_14784; -.
DR CTD; 8586767; -.
DR WormBase; CBG14784; CBP03461; WBGene00035179; Cbr-mig-23.
DR eggNOG; KOG1386; Eukaryota.
DR HOGENOM; CLU_010246_6_1_1; -.
DR InParanoid; Q617Y0; -.
DR OMA; QDEIGPP; -.
DR OrthoDB; 1337265at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043262; F:adenosine-diphosphatase activity; IEA:EnsemblMetazoa.
DR GO; GO:0004382; F:guanosine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0017110; F:nucleoside-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0045134; F:uridine-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046032; P:ADP catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0046712; P:GDP catabolic process; IEA:EnsemblMetazoa.
DR GO; GO:0035262; P:gonad morphogenesis; IEA:EnsemblMetazoa.
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; IEA:EnsemblMetazoa.
DR GO; GO:0030334; P:regulation of cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0006256; P:UDP catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Developmental protein; Differentiation; Glycoprotein; Golgi apparatus;
KW Gonadal differentiation; Hydrolase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..553
FT /note="Nucleoside-diphosphatase mig-23"
FT /id="PRO_0000298775"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..489
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 490..510
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..553
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"
SQ SEQUENCE 553 AA; 62594 MW; C1953A7F183DF876 CRC64;
MRVSRRFTIL AITAMIFLSL IICIYAVAAH TTVNVILQKQ ERSYGVICDA GSTGTRLFVY
NWVSTSDSEL IQIEPVIYDN KPVMKKISPG LSTFGTKPDE AAEYLRPLME LAELHIPEEK
RPYTPVFIFA TAGMRLIPDE QKEAVLTNLR TELPKITSMQ VLKEHIRIIE GKWEGIYSWI
AVNYALGKFN RTFTPDFPGT SPGQQRSKTV GMIDMGGASA QIAFELPDND DFNSINVENI
NLGCREDDSL FRYKLFVTTF LGYGVNEGIR KYEKTLMAKL KDQNGTVIQD DCMPLNLHKT
VTMENGDNFV RRGTGNWDTC AAEVKKLLNP ETSSEVCKAE VAKCYFGAVP APNIPLSNVE
MYGFSEYWYS THDVLGLGGQ YNAENIAKKS EQYCGQRWST IQAASKKNLY PRADEERLKT
QCFKSAWITS VLHDGFSVDK THNKFQSVST IAGQEVQWAL GAMIYHMRFF PLRDSTRNLI
VKETHSASES LWAPLFFLSA VFCLFVLVCA KEHSLLCFDD KRRASFGLTR RQYSYKMLKE
DRTSSSAFLE NFA
