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G5EFL0 (GLD4_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) RNA polymerase gld-4

EC=2.7.7.19
Alternative name(s):
Defective in germ line development protein 4
Germline development defective-4
Gene names
Name:gld-4
ORF Names:ZK858.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length845 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. The enzymatic activity is enhanced by its interaction with gls-1. Required, together with gld-2, for early meiotic progression in male and female germ cells and for gld-1 protein accumulation in the hermaphrodite germline. In the germline, forms a complex with gls-1 which directly binds to gld-1 mRNA and prevents its degradation. Ref.1

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1). Ref.1

Cofactor

Magnesium or manganese By similarity. UniProtKB O17087

Subunit structure

Interacts with gls-1 isoform C Ref.1

Subcellular location

Cytoplasm. Cytoplasmic granule. Cytoplasmperinuclear region. Note: Localizes to P granules. This association is less apparent during pachytene, becomes obvious in maturing oocytes and is most prominently visible in developing embryos. Ref.1

Tissue specificity

Germline-specific. Ref.1

Developmental stage

Expressed both maternally and zygotically throughout embryonic development and in adult hermaphrodites. Ref.1

Domain

In contrast to other poly(A) RNA polymerases, lacks any RNA-binding domain. Ref.1

Disruption phenotype

High embryonic lethality. Hermaphrodite animals are partially fertile and those that produce sperm and oocytes have reduced brood sizes and display smaller germlines. Hermaphrodite gld-4 and gld-2 double mutants are fully sterile and display either an earlier meiotic arrest than gld-2 single mutant or a failure to commit to meiotic progression and a return to mitosis. Ref.1

Miscellaneous

The gld-4 locus produces a single transcript that is SL-1 trans-spliced. Ref.1

Sequence similarities

Contains 1 PAP-associated domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 845845Poly(A) RNA polymerase gld-4
PRO_0000419046

Regions

Domain276 – 33560PAP-associated

Sites

Metal binding1391Magnesium or manganese; catalytic Probable UniProtKB O17087
Metal binding1411Magnesium or manganese; catalytic Probable UniProtKB O17087

Experimental info

Mutagenesis1391D → A: Loss of catalytic activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
G5EFL0 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: C4836B6F8E7CC372

FASTA84594,310
        10         20         30         40         50         60 
MNEDSRLSSS QQPSTSTPRS SIPSTMNSDE PNTCRRLSQS QEQPSTSRTC KSETPEFGYS 

        70         80         90        100        110        120 
DSLPFAPWRR KRYGLNIQGL HEEIVDMYHW IKPNEIESRL RTKVFEKVRD SVLRRWKQKT 

       130        140        150        160        170        180 
IKISMFGSLR TNLFLPTSDI DVLVECDDWV GTPGDWLAET ARGLEADNIA ESVMVYGGAF 

       190        200        210        220        230        240 
VPIVKMVDRD TRLSIDISFN TVQGVRAASY IAKVKEEFPL IEPLVLLLKQ FLHYRNLNQT 

       250        260        270        280        290        300 
FTGGLSSYGL VLLLVNFFQL YALNMRSRTI YDRGVNLGHL LLRFLELYSL EFNFEEMGIS 

       310        320        330        340        350        360 
PGQCCYIPKS ASGARYGHKQ AQPGNLALED PLLTANDVGR STYNFSSIAN AFGQAFQILL 

       370        380        390        400        410        420 
VAVTLRERKG KNHVAMRAYK GSLLHLIMPF TSKELTYRNW LMSGVLSMPG QEAPASYDLN 

       430        440        450        460        470        480 
QLHNTLVSPM VDLSRYAWLR KAPAKAEKRD SRPLTIVNPA DDRQTLAQQL KKQILEQTEA 

       490        500        510        520        530        540 
KKSLEKMPAC DDNKKEEELV ATRETDVELE AEDTESEGHH NGENDLILTG PPLPTSTQSV 

       550        560        570        580        590        600 
NTSATVSTAA SISEREDTDS PGLSSSMGNQ SSEEDEDNGI NNRNNSAVPV QFKKPFNEVV 

       610        620        630        640        650        660 
AQPARESKRT QTTSEDKMQD QFHFNGYSYP PPSRYAAGTA APSHKHRNAH PQRQRPSIRN 

       670        680        690        700        710        720 
LSQGSDGSDE YNVESWNNNI RQGRRASSNS PSPSRQQTNT RNCGPTNNIP YDSFRSQNKN 

       730        740        750        760        770        780 
STLDGSNNSS EEPITMYADV VKKKSSITTS TNTSTADVNV TNGNPIPANG IIPQSMAVVN 

       790        800        810        820        830        840 
VGRGSYRNAL TTSPMTPPSA HTSMQKQHHL RKDNECGFDN NSATSSTDLS HHQPQLVPPV 


NRLQR 

« Hide

References

« Hide 'large scale' references
[1]"Two conserved regulatory cytoplasmic poly(A) polymerases, GLD-4 and GLD-2, regulate meiotic progression in C. elegans."
Schmid M., Kuchler B., Eckmann C.R.
Genes Dev. 23:824-836(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH GLS-1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-139.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FJ610054 mRNA. Translation: ACO95123.1.
Z79759 Genomic DNA. Translation: CAB02138.3.
RefSeqNP_492446.3. NM_060045.4.
UniGeneCel.16131.

3D structure databases

ProteinModelPortalG5EFL0.
SMRG5EFL0. Positions 65-390.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEG5EFL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaZK858.1; ZK858.1; ZK858.1.
GeneID172735.
KEGGcel:CELE_ZK858.1.

Organism-specific databases

CTD172735.
WormBaseZK858.1; CE42850; WBGene00014115; gld-4.

Phylogenomic databases

KOK03514.
OMAKISMFGS.
OrthoDBEOG7X6KZP.

Family and domain databases

InterProIPR002934. Nucleotidyltransferase.
IPR002058. PAP_assoc.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio876795.

Entry information

Entry nameGLD4_CAEEL
AccessionPrimary (citable) accession number: G5EFL0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: December 14, 2011
Last modified: April 16, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Caenorhabditis elegans

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