Q91YI6 (GLD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(A) RNA polymerase GLD2
Short name=mGLD-2
EC=2.7.7.19

Alternative name(s):
PAP-associated domain-containing protein 4

Gene names

Name:	Papd4
Synonyms:	Gld2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Does not play a role in replication-dependent histone mRNA degradation By similarity.
Catalytic activity	ATP + RNA(n) = diphosphate + RNA(n+1). Ref.4
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Interacts with CPEB1, CPEB2, CPSF1 and PABPC1. Ref.7
Subcellular location	Cytoplasm. Nucleus Ref.6.
Tissue specificity	Ubiquitous. In brain, it is highly expressed in the cerebral cortex, cerebellum, hippocampus and olfactory bulb. Ref.5 Ref.6
Developmental stage	Expressed in oocytes from metaphase I to metaphase II during oocyte maturation. Ref.6
Disruption phenotype	Mice are normal and healthy. Poly-A tail elongation in oocytes is not affected and mice are fertile. Ref.7
Sequence similarities	Belongs to the DNA polymerase type-B-like family. GLD2 subfamily. Contains 1 PAP-associated domain.
Sequence caution	The sequence BAC28170.1 differs from that shown. Reason: Frameshift at position 216.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA polyadenylation Inferred from electronic annotation. Source: Compara histone mRNA catabolic process Inferred from sequence or structural similarity. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.7. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide adenylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q91YI6-1)

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: Q91YI6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     225-228: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 484	484	Poly(A) RNA polymerase GLD2		PRO_0000341550
Regions
	Domain	386 – 440	55	PAP-associated
	Motif	76 – 92	17	Nuclear localization signal Potential
Sites
	Metal binding	213	1	Magnesium or manganese; catalytic By similarity
	Metal binding	215	1	Magnesium or manganese; catalytic By similarity
Amino acid modifications
	Modified residue	62	1	Phosphoserine By similarity
	Modified residue	69	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	225 – 228	4	Missing in isoform 2.		VSP_034325
Experimental info
	Mutagenesis	215	1	D → A: Loss of enzyme activity. Ref.6
	Sequence conflict	357	1	P → T in BAC28170. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C60D799AA5F14CB6	FASTA	484	55,934
	10 20 30 40 50 60 MFPNSILGRP PFTPTHQQHN NFFALSPTLY SHQQLIDAQF NFQNVDLSRA VSLQPLTYGT 70 80 90 100 110 120 VSPIQTSTSP LFRGRKRISD EKAFPLDGKR QRFHSPHQEP TIINQLVPLS GDRRYSMPPL 130 140 150 160 170 180 FHTHYIPDIV RCVPPLREIP LLEPREITLP EAKDKLSQQI LELFETCQQQ ASDLKKKELC 190 200 210 220 230 240 RAQLQREIQL LFPQSRLFLV GSSLNGFGAR SSDGDLCLVV KEEPCFFQVN QKTEARHILT 250 260 270 280 290 300 LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNTVGIRN TFLLRTYAYL 310 320 330 340 350 360 ENRVRPLVLV IKKWASHHDI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SLQKIYPESF 370 380 390 400 410 420 STSVQLHLVH HAPCNVPPYL SKNESSLGDL LLGFLKYYAT EFDWNTQMIS VREAKAIPRP 430 440 450 460 470 480 DDMEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWQRLKNKRD LNSVLPLRAA TLKR
	Isoform 2 [UniParc]. Checksum: 7CD85BCCF29AB625	FASTA	480	55,408
	10 20 30 40 50 60 MFPNSILGRP PFTPTHQQHN NFFALSPTLY SHQQLIDAQF NFQNVDLSRA VSLQPLTYGT 70 80 90 100 110 120 VSPIQTSTSP LFRGRKRISD EKAFPLDGKR QRFHSPHQEP TIINQLVPLS GDRRYSMPPL 130 140 150 160 170 180 FHTHYIPDIV RCVPPLREIP LLEPREITLP EAKDKLSQQI LELFETCQQQ ASDLKKKELC 190 200 210 220 230 240 RAQLQREIQL LFPQSRLFLV GSSLNGFGAR SSDGDLCLVV KEEPVNQKTE ARHILTLVHK 250 260 270 280 290 300 HFCTRLSGYI ERPQLIRAKV PIVKFRDKVS CVEFDLNVNN TVGIRNTFLL RTYAYLENRV 310 320 330 340 350 360 RPLVLVIKKW ASHHDINDAS RGTLSSYSLV LMVLHYLQTL PEPILPSLQK IYPESFSTSV 370 380 390 400 410 420 QLHLVHHAPC NVPPYLSKNE SSLGDLLLGF LKYYATEFDW NTQMISVREA KAIPRPDDME 430 440 450 460 470 480 WRNKYICVEE PFDGTNTARA VHEKQKFDMI KDQFLKSWQR LKNKRDLNSV LPLRAATLKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"XRbm9, a new XGld2-interacting protein, enhances translation in Xenopus oocytes." Papin C. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: NIH Swiss.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N. Tissue: Mammary tumor.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-484. Strain: C57BL/6J. Tissue: Testis.
[4]	"Mammalian GLD-2 homologs are poly(A) polymerases." Kwak J.E., Wang L., Ballantyne S., Kimble J., Wickens M. Proc. Natl. Acad. Sci. U.S.A. 101:4407-4412(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME ACTIVITY.
[5]	"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: TISSUE SPECIFICITY.
[6]	"Possible role of mouse poly(A) polymerase mGLD-2 during oocyte maturation." Nakanishi T., Kubota H., Ishibashi N., Kumagai S., Watanabe H., Yamashita M., Kashiwabara S., Miyado K., Baba T. Dev. Biol. 289:115-126(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF ASP-215.
[7]	"Disruption of mouse poly(A) polymerase mGLD-2 does not alter polyadenylation status in oocytes and somatic cells." Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M., Kashiwabara S., Baba T. Biochem. Biophys. Res. Commun. 364:14-19(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE, INTERACTION WITH CPEB1; CPEB2; CPSF1 AND PABPC1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM419011 mRNA. Translation: CAL91354.1. BC016629 mRNA. Translation: AAH16629.1. AK033141 mRNA. Translation: BAC28170.1. Frameshift.
IPI	IPI00130216. IPI00896066.
RefSeq	NP_598666.1. NM_133905.2.
UniGene	Mm.242865.
3D structure databases
ProteinModelPortal	Q91YI6.
SMR	Q91YI6. Positions 162-469.
ModBase	Search...
PTM databases
PhosphoSite	Q91YI6.
Proteomic databases
PRIDE	Q91YI6.
Protocols and materials databases
DNASU	100715.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000048702; ENSMUSP00000048124; ENSMUSG00000042167.
GeneID	100715.
KEGG	mmu:100715.
UCSC	uc007rkz.1. mouse. uc007rla.1. mouse.
Organism-specific databases
CTD	167153.
MGI	MGI:2140950. Papd4.
Phylogenomic databases
eggNOG	COG5260.
GeneTree	ENSGT00550000074490.
HOGENOM	HOG000088606.
HOVERGEN	HBG097533.
InParanoid	Q91YI6.
KO	K14079.
OMA	NQKTEAR.
OrthoDB	EOG4P2Q22.
Gene expression databases
Bgee	Q91YI6.
Genevestigator	Q91YI6.
Family and domain databases
InterPro	IPR002058. PAP_assoc. [Graphical view]
Pfam	PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PAPD4. mouse.
NextBio	354606.
SOURCE	Search...

Entry information

Entry name

GLD2_MOUSE

Accession

Primary (citable) accession number: Q91YI6
Secondary accession number(s): A4F5H0, Q8CCH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program