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Reviewed, UniProtKB/Swiss-Prot Q21815 (MIG23_CAEEL)

Last modified June 16, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nucleoside-diphosphatase mig-23
      Short name=NDPase
    EC=3.6.1.6
Alternative name(s):
    Abnormal cell migration protein 23
Gene names
Name: mig-23
ORF Names: R07E4.4
OrganismCaenorhabditis elegans [Complete proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Seems to be able to hydrolyze ADP, UDP and GDP. Supports mig-17 glycosylation and surface expression, which is required for proper migration of distal tip cells during gonad morphogenesis. Ref.1

Catalytic activity

A nucleoside diphosphate + H2O = a nucleotide + phosphate.

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein. Ref.1 Ref.4

Tissue specificity

Expressed in body wall muscles. Ref.1

Induction

In contrast to uda-1, expression is not induced by stress. Ref.3

Sequence similarities

Belongs to the GDA1/CD39 NTPase family.

Ontologies

Keywords
   Biological processDifferentiation
Gonadal differentiation
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
   Molecular functionDevelopmental protein
Hydrolase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

gonadal mesoderm development

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionnucleoside-diphosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Nucleoside-diphosphatase mig-23
PRO_0000209923

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721 Potential
Topological domain28 – 489462Lumenal Potential
Transmembrane490 – 51021 Potential
Topological domain511 – 55242Cytoplasmic Potential

Amino acid modifications

Glycosylation1901N-linked (GlcNAc...) Potential
Glycosylation2841N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis2681G → E in k166; reduced migration of the gonad arms in both the anterior and posterior direction. Ref.1
Mutagenesis2901D → N in k146; reduced migration of the gonad arms in both the anterior and posterior direction. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q21815-1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: E5DC32C858AE4D94

FASTA55262,511
        10         20         30         40         50         60 
MRVSLRFTIL AVSAMIFFPV IVFIYVVEAH TSPKVIADDQ ERSYGVICDA GSTGTRLFVY 

        70         80         90        100        110        120 
NWISTSDSEL IQIEPVIYDN KPVMKKISPG LSTFGTKPAQ AAEYLRPLME LAERHIPEEK 

       130        140        150        160        170        180 
RPYTPVFIFA TAGMRLIPDE QKEAVLKNLR NKLPKITSMQ VLKEHIRIIE GKWEGIYSWI 

       190        200        210        220        230        240 
AVNYALGKFN KTATLDFPGT SPAHARQKTV GMIDMGGASA QIAFELPDTD SFSSINVENI 

       250        260        270        280        290        300 
NLGCREDDSL FKYKLFVTTF LGYGVNEGIR KYEHMLLSKL KDQNGTVIQD DCMPLNLHKT 

       310        320        330        340        350        360 
VTLENGENFV RRGTGNWNTC SNEVKKLLNP ESSSEVCKAE AAKCYFGAVP APSIPLSNIE 

       370        380        390        400        410        420 
MYGFSEYWYS THDVLGLGGQ YDAENIAKKT QQYCSKRWST IQAESKKQLY PRADEERLRT 

       430        440        450        460        470        480 
QCFKSAWITS VLHDGFSVDK THNKFQSVST IAGQEVQWAL GAMIYHMRFF PLRDSSRNLI 

       490        500        510        520        530        540 
VKETHSSSES LWAPLFFLSA VFCLFVLVCA KEQSVLCFDD KRRSSFGMSR SQYSYKMLKE 

       550 
NRTSSSFLEN FA 

« Hide

References

« Hide 'large scale' references
[1]"An NDPase links ADAM protease glycosylation with organ morphogenesis in C. elegans."
Nishiwaki K., Kubota Y., Chigira Y., Roy S.K., Suzuki M., Schvarzstein M., Jigami Y., Hisamoto N., Matsumoto K.
Nat. Cell Biol. 6:31-37(2004) [PubMed: 14688791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-268 AND ASP-290.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"ire-1-dependent transcriptional up-regulation of a lumenal uridine diphosphatase from Caenorhabditis elegans."
Uccelletti D., O'Callaghan C., Berninsone P., Zemtseva I., Abeijon C., Hirschberg C.B.
J. Biol. Chem. 279:27390-27398(2004) [PubMed: 15102851] [Abstract]
Cited for: LACK OF INDUCTION BY STRESS.
[4]"The conserved oligomeric Golgi complex acts in organ morphogenesis via glycosylation of an ADAM protease in C. elegans."
Kubota Y., Sano M., Goda S., Suzuki N., Nishiwaki K.
Development 133:263-273(2006) [PubMed: 16354716] [Abstract]
Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases

AB126261 mRNA. Translation: BAD02168.1.
U39652 Genomic DNA. Translation: AAA80403.2.
PIRT16696.
RefSeqNP_508994.1.
UniGeneCel.6413

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblR07E4.4. Caenorhabditis elegans. [Contig view]
GeneID180860.
KEGGcel:R07E4.4.

Organism-specific databases

WormBaseWBGene00003254. mig-23.
WormPepR07E4.4. CE28748. [WorfDB]

Phylogenomic databases

OMAQ21815. SAWITSV.

Enzyme and pathway databases

BRENDA3.6.1.6. 672.

Gene expression databases

ArrayExpressQ21815.

Family and domain databases

InterProIPR000407. GDA1_CD39_NTPase.
[Graphical view]
PANTHERPTHR11782. GDA1_CD39_NTPase. 1 hit.
PfamPF01150. GDA1_CD39. 1 hit.
[Graphical view]
PROSITEPS01238. GDA1_CD39_NTPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio911292.

Entry information

Entry nameMIG23_CAEEL
AccessionPrimary (citable) accession number: Q21815
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents