Q9VD44 (GLD2A_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Poly(A) RNA polymerase gld-2 homolog A
Short name=DmGLD2
EC=2.7.7.19

Gene names

Name:	Gld2
ORF Names:	CG5732

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1364 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. Required for formation of long term memory. Ref.5
Catalytic activity	ATP + RNA(n) = diphosphate + RNA(n+1).
Cofactor	Magnesium or manganese By similarity.
Subunit structure	Interacts with Fmr1 and eIF-4E. Ref.5
Subcellular location	Cytoplasm. Nucleus. Note: Found in neuronal cytoplasm, present in discrete neuronal particles associated with mRNA control, and in nuclear puncta. Ref.5
Tissue specificity	Expressed in the brain. Ref.5
Developmental stage	Expressed in larvae, pupae and adults. Ref.5
Sequence similarities	Belongs to the DNA polymerase type-B-like family. GLD2 subfamily. Contains 1 PAP-associated domain.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding RNA-binding
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA polyadenylation Inferred from sequence or structural similarity. Source: UniProtKB long-term memory Inferred from mutant phenotype Ref.5. Source: FlyBase mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: FlyBase neuron projection Inferred from direct assay Ref.5. Source: FlyBase nucleoplasm Inferred from direct assay Ref.5. Source: FlyBase
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide adenylyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform A (identifier: Q9VD44-1)

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.

Note: No experimental confirmation available.

Isoform B (identifier: Q9VD44-2)

The sequence of this isoform differs from the canonical sequence as follows:
     881-1364: PEENNDDDEL...NSVADKPPIA → VGELKNVLLN...LIVHFIRFTK

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1364	1364	Poly(A) RNA polymerase gld-2 homolog A		PRO_0000341557
Regions
	Domain	1163 – 1224	62	PAP-associated
	Compositional bias	4 – 11	8	Poly-Ala
	Compositional bias	15 – 20	6	Poly-Ala
	Compositional bias	465 – 491	27	Ser-rich
	Compositional bias	599 – 645	47	Ala-rich
Sites
	Metal binding	993	1	Magnesium or manganese; catalytic By similarity
	Metal binding	995	1	Magnesium or manganese; catalytic By similarity
Natural variations
	Alternative sequence	881 – 1364	484	PEENN…KPPIA → VGELKNVLLNGQITKFISSK SYFFLSSVCLIVHFIRFTK in isoform B.		VSP_034331
Experimental info
	Mutagenesis	995	1	D → A: Destroys active site. Ref.5
	Sequence conflict	523	1	I → V in AAM52588. Ref.3
	Sequence conflict	523	1	I → V in ACH95257. Ref.4
	Sequence conflict	591	1	P → A in AAM52588. Ref.3
	Sequence conflict	591	1	P → A in ACH95257. Ref.4
	Sequence conflict	610	1	T → TAA in AAM52588. Ref.3
	Sequence conflict	610	1	T → TAA in ACH95257. Ref.4
	Sequence conflict	636	1	A → T in AAM52588. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified July 5, 2004. Version 3. Checksum: 9BAFCAE8D75083CA	FASTA	1,364	147,592
	10 20 30 40 50 60 MSTAMAMAAA ASSSAAAATA TTTAISNSTN TTASPATTNT INTTTKTITT SEVPLEPASN 70 80 90 100 110 120 MAPKALEIED SGRNEPEDLE HGAAKPLEQR KTTVVHTCPR PPGGYKYSME FLYGIGSGMA 130 140 150 160 170 180 GIPLNIPTPS SITPRTVRST APLLTTHMPL LTNMGVAPSR PSGIRYPGSA GGSNGTTVAA 190 200 210 220 230 240 STTPSTTVTT SSGSPGSGAE AITSSVSSSG LPAAGLQAAQ FICQGYMPTG PQRRLWHAEN 250 260 270 280 290 300 AVWQFDRNYP YNQAYSPPYG IPMMPVGFEH PYGQRIIYPG YYNQTPPGIN PAAVAGLTRT 310 320 330 340 350 360 NRPVTQQPHI LTQPAVGTTE SSEEAPATLG NAPQVSSTWR YGRPGTHRGR HAVPTAAAPA 370 380 390 400 410 420 LLHRDSKSFY NSIGSGMANG PRFKAPFVAN VRNFQAGAVA TVAAGGAATT AVVGTSAPAT 430 440 450 460 470 480 GAASSSDQNV ATKRNHQGAA TQNNHRNRHN AKKGGKNSVG KELTSNSSES LSNSSSKSQL 490 500 510 520 530 540 NKRPSSSSSI SPIKHPHRNY RNRMRYTATE PTEQKAATTT VPISNYQPPQ QSTSTVRRTS 550 560 570 580 590 600 KFQGSNAYQA HTAAGRQQSR FYQSRHMDGY VFQSGHYMVY AAGAPPVGLR PGKSPVSEAT 610 620 630 640 650 660 GAPPGAAAAT AAAATAVAAT AAAAEGGGAA EGGGAAAAPV TASSATLEGE QPLDSDFDQR 670 680 690 700 710 720 QEFADLGLDP ANGGFSSDLE PNGIKQDTSE LDTHSCLISH PNSEVDGDDN QSLASFAPSV 730 740 750 760 770 780 ESDDSDSELS DASVESVARD ILVSCLAVAT GAEEPDFSGP NLVPYGDMHY LKELDKKNPP 790 800 810 820 830 840 TNGYRSHRPY HQSHYAYHSQ MSPRGLSCCG DMLNQHSEDL VFKLDQNQPD GIESGKNIFL 850 860 870 880 890 900 REITEQPDNI SVASNLSCSP SASSSKSVLA PMASKSNITM PEENNDDDEL PLVVHNRYWR 910 920 930 940 950 960 EFFGYTPADR FLLRAKFVEM RRPPKVMGCK NKWDPLSLSV WKKFLESQQT RHVYKIKMRL 970 980 990 1000 1010 1020 WRAIYTVAMK NYPRYGLYLV GSSISYFGSK CSDMDICMLA CTNPNIDSRM EAVYHLHVMK 1030 1040 1050 1060 1070 1080 ELLGRTNMFQ DFNLIEARVP ILRFTDRCHK VEVDINFNNS VGIRNTHLLY CYSQLDWRVR 1090 1100 1110 1120 1130 1140 PMALTVKQWA QYHNINNAKN MTISSYSLML MVIHFLQVGA SPPVLPCLHN LYPEKFGLLQ 1150 1160 1170 1180 1190 1200 PNDFGYVDMN EVMAPYQSDN SQTLGDLLLS FLHYYSVFDY GKYAISIRVG GVLPIEVCRA 1210 1220 1230 1240 1250 1260 ATAPKNDIHQ WNELCIEEPF DQTNTARSVY DTDTFERIKT IFVASYRRLD STRNLSAIFE 1270 1280 1290 1300 1310 1320 DYDGPTILMQ QPSVDSEIEL YEGQHHRLLP NRGSSRSNSA IPSPRPSILM VDKATTAIWD 1330 1340 1350 1360 DINNKPDHPV LSHSNNYDAT NECTGNGSLM GLKDNSVADK PPIA
	Isoform B [UniParc]. Checksum: 35B7D4D987E439A2	FASTA	919	96,248
	10 20 30 40 50 60 MSTAMAMAAA ASSSAAAATA TTTAISNSTN TTASPATTNT INTTTKTITT SEVPLEPASN 70 80 90 100 110 120 MAPKALEIED SGRNEPEDLE HGAAKPLEQR KTTVVHTCPR PPGGYKYSME FLYGIGSGMA 130 140 150 160 170 180 GIPLNIPTPS SITPRTVRST APLLTTHMPL LTNMGVAPSR PSGIRYPGSA GGSNGTTVAA 190 200 210 220 230 240 STTPSTTVTT SSGSPGSGAE AITSSVSSSG LPAAGLQAAQ FICQGYMPTG PQRRLWHAEN 250 260 270 280 290 300 AVWQFDRNYP YNQAYSPPYG IPMMPVGFEH PYGQRIIYPG YYNQTPPGIN PAAVAGLTRT 310 320 330 340 350 360 NRPVTQQPHI LTQPAVGTTE SSEEAPATLG NAPQVSSTWR YGRPGTHRGR HAVPTAAAPA 370 380 390 400 410 420 LLHRDSKSFY NSIGSGMANG PRFKAPFVAN VRNFQAGAVA TVAAGGAATT AVVGTSAPAT 430 440 450 460 470 480 GAASSSDQNV ATKRNHQGAA TQNNHRNRHN AKKGGKNSVG KELTSNSSES LSNSSSKSQL 490 500 510 520 530 540 NKRPSSSSSI SPIKHPHRNY RNRMRYTATE PTEQKAATTT VPISNYQPPQ QSTSTVRRTS 550 560 570 580 590 600 KFQGSNAYQA HTAAGRQQSR FYQSRHMDGY VFQSGHYMVY AAGAPPVGLR PGKSPVSEAT 610 620 630 640 650 660 GAPPGAAAAT AAAATAVAAT AAAAEGGGAA EGGGAAAAPV TASSATLEGE QPLDSDFDQR 670 680 690 700 710 720 QEFADLGLDP ANGGFSSDLE PNGIKQDTSE LDTHSCLISH PNSEVDGDDN QSLASFAPSV 730 740 750 760 770 780 ESDDSDSELS DASVESVARD ILVSCLAVAT GAEEPDFSGP NLVPYGDMHY LKELDKKNPP 790 800 810 820 830 840 TNGYRSHRPY HQSHYAYHSQ MSPRGLSCCG DMLNQHSEDL VFKLDQNQPD GIESGKNIFL 850 860 870 880 890 900 REITEQPDNI SVASNLSCSP SASSSKSVLA PMASKSNITM VGELKNVLLN GQITKFISSK 910 SYFFLSSVCL IVHFIRFTK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). Strain: Berkeley. Tissue: Testis.
[4]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: Berkeley. Tissue: Testis.
[5]	"GLD2 poly(A) polymerase is required for long-term memory." Kwak J.E., Drier E., Barbee S.A., Ramaswami M., Yin J.C.P., Wickens M. Proc. Natl. Acad. Sci. U.S.A. 105:14644-14649(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FMR1 AND EIF-4E, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF ASP-995.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAF55959.3. AY122076 mRNA. Translation: AAM52588.1. BT044483 mRNA. Translation: ACH95257.1.
RefSeq	NP_001262829.1. NM_001275900.1. NP_651012.2. NM_142755.4.
3D structure databases
ProteinModelPortal	Q9VD44.
SMR	Q9VD44. Positions 941-1251.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VD44. 2 interactions.
MINT	MINT-1691551.
Proteomic databases
PaxDb	Q9VD44.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0305038; FBpp0293575; FBgn0038934. FBtr0310204; FBpp0301888; FBgn0038934.
GeneID	42602.
KEGG	dme:Dmel_CG5732.
UCSC	CG5732-RA. d. melanogaster.
Organism-specific databases
CTD	42602.
FlyBase	FBgn0038934. Gld2.
Phylogenomic databases
eggNOG	COG5260.
GeneTree	ENSGT00550000074490.
InParanoid	Q9VD44.
KO	K14079.
OMA	RYWREFF.
OrthoDB	EOG40GB69.
PhylomeDB	Q9VD44.
Gene expression databases
Bgee	Q9VD44.
Family and domain databases
InterPro	IPR002058. PAP_assoc. [Graphical view]
Pfam	PF03828. PAP_assoc. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	42602.
NextBio	829642.

Entry information

Entry name

GLD2A_DROME

Accession

Primary (citable) accession number: Q9VD44
Secondary accession number(s): B5RJK9, Q8MR77

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project