Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q6DFA8 (GLD2B_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 28, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) RNA polymerase GLD2-B
Short name=xGLD-2
EC=2.7.7.19
Alternative name(s):
PAP-associated domain-containing protein 4-B
Gene names
Name:papd4-b
Synonyms:gld2-b
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length509 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. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs during oocyte maturation. Plays a central role during oocyte maturation by mediating polyadenylation of dormant mRNAs, which contain 5'AAUAAA-3' sequence in their 3'-UTR. In immature oocytes, polyadenylation of poly(A) tails is counteracted by the ribonuclease parn. During maturation parn is excluded from the ribonucleoprotein complex, allowing poly(A) elongation and activation of mRNAs. May not play a role in replication-dependent histone mRNA degradation By similarity. Ref.1 Ref.4 Ref.5

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1). Ref.4

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Component of a complex at least composed of cpeb1, cpsf1, papd4/gld2, pabpc1/ePAB, parn and sympk. Following oocyte maturation, parn is expelled from the complex. Interacts with rbfox2. Interacts with sympk By similarity. Ref.1 Ref.2 Ref.5 Ref.6

Subcellular location

Cytoplasm Ref.1 Ref.4.

Developmental stage

Present in oocytes. Ref.4

Induction

Autoregulated; mediates its own polyadenylation and translational activation during frog oocyte maturation. Ref.7

Sequence similarities

Belongs to the DNA polymerase type-B-like family. GLD2 subfamily.

Contains 1 PAP-associated domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6DFA8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6DFA8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-98: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Poly(A) RNA polymerase GLD2-B
PRO_0000341554

Regions

Domain409 – 46254PAP-associated

Sites

Metal binding2401Magnesium or manganese; catalytic By similarity
Metal binding2421Magnesium or manganese; catalytic By similarity

Natural variations

Alternative sequence56 – 9843Missing in isoform 2.
VSP_034326

Experimental info

Mutagenesis2421D → A: Loss of activity. Ref.1
Sequence conflict281S → T in AAT98005. Ref.1
Sequence conflict1331G → S in AAT98005. Ref.1
Sequence conflict3761K → R in AAT98005. Ref.1
Sequence conflict4301I → V in AAT98005. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: 8FB3569E258252D7

FASTA50958,235
        10         20         30         40         50         60 
MYPNSPSLGR IPLPLPCARQ QQTSAYLSKV PVSVAPDLLS PEQFFQASLN IHKNANLPRL 

        70         80         90        100        110        120 
LMNGNVLTVP PLSSPPWSYL NHSPLISPGS PPSSFQNRKR RSDEGNSPYD VKRQRFQSPQ 

       130        140        150        160        170        180 
EQTVNHQAVP LRGDIRCSYP GSPAFPLLQS PSPPVLKGHS SNSGDCWLYD HIDTTLPVAK 

       190        200        210        220        230        240 
DKLSKQILDL FQALQQQVCD LKKKDICRAE LQREIQQIFP QSRLYLVGSS LNGFGIRSSD 

       250        260        270        280        290        300 
ADLCLVLKEE PMNQNTEARH ILSLLHKHFY TRLSYIERPQ FIRAKVPIVK FRDKVSGAEF 

       310        320        330        340        350        360 
DLNVNNVVGI RNTFLLRTYA YLDKRVRPLV LVIKKWANHH GINDASRGTL SSYTIVLMVL 

       370        380        390        400        410        420 
HYLQTLPEPI LPSLQKKYPE CFDRTMQLHL VHQAPRNIPQ FLSKNETPLG DLLLGFLKYF 

       430        440        450        460        470        480 
AVEFDWSKDI ISLREAKALP RTDDYEWRNK YICVEEPFDG SNTARAVYEK QKFDLIRAEF 

       490        500 
LKAWVALRDN RDLYSLLPVK GIMKKMHSL

« Hide

Isoform 2 [UniParc].

Checksum: 51E6DD2192BAEAB8
Show »

FASTA46653,570

References

« Hide 'large scale' references
[1]"Symplekin and xGLD-2 are required for CPEB-mediated cytoplasmic polyadenylation."
Barnard D.C., Ryan K., Manley J.L., Richter J.D.
Cell 119:641-651(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CPEB1; CPSF1 AND SYMPK, MUTAGENESIS OF ASP-242.
Tissue: Oocyte.
[2]"Xenopus Rbm9 is a novel interactor of XGld2 in the cytoplasmic polyadenylation complex."
Papin C., Rouget C., Mandart E.
FEBS J. 275:490-503(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RBFOX2.
Tissue: Oocyte.
[3]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Oocyte.
[4]"Vertebrate GLD2 poly(A) polymerases in the germline and the brain."
Rouhana L., Wang L., Buter N., Kwak J.E., Schiltz C.A., Gonzalez T., Kelley A.E., Landry C.F., Wickens M.
RNA 11:1117-1130(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[5]"Opposing polymerase-deadenylase activities regulate cytoplasmic polyadenylation."
Kim J.H., Richter J.D.
Mol. Cell 24:173-183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PARN.
[6]"RINGO/cdk1 and CPEB mediate poly(A) tail stabilization and translational regulation by ePAB."
Kim J.H., Richter J.D.
Genes Dev. 21:2571-2579(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PABPC1.
[7]"Autoregulation of GLD-2 cytoplasmic poly(A) polymerase."
Rouhana L., Wickens M.
RNA 13:188-199(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY655140 mRNA. Translation: AAT98005.1.
AM419010 mRNA. Translation: CAL91353.1.
BC076832 mRNA. Translation: AAH76832.1.
RefSeqNP_001086580.1. NM_001093111.1.
NP_001087078.1. NM_001093609.1.
UniGeneXl.63197.
Xl.75862.

3D structure databases

ProteinModelPortalQ6DFA8.
ModBaseSearch...

Proteomic databases

PRIDEQ6DFA8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID446415.
446914.
KEGGxla:446415.
xla:446914.

Organism-specific databases

CTD446415.
446914.
XenbaseXB-GENE-6256236. papd4.

Phylogenomic databases

HOVERGENHBG097533.
KOK14079.

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...

Entry information

Entry nameGLD2B_XENLA
AccessionPrimary (citable) accession number: Q6DFA8
Secondary accession number(s): A4F5G9, Q68PF4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: August 16, 2004
Last modified: November 28, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents