GLD2_MOUSE
ID GLD2_MOUSE Reviewed; 484 AA.
AC Q91YI6; A4F5H0; Q8CCH5;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Poly(A) RNA polymerase GLD2 {ECO:0000305};
DE Short=mGLD-2 {ECO:0000305};
DE EC=2.7.7.19 {ECO:0000269|PubMed:15070731};
DE AltName: Full=PAP-associated domain-containing protein 4;
DE AltName: Full=Terminal nucleotidyltransferase 2 {ECO:0000250|UniProtKB:Q6PIY7};
GN Name=Tent2;
GN Synonyms=Gld2 {ECO:0000303|PubMed:15070731, ECO:0000303|PubMed:15987818},
GN Papd4 {ECO:0000312|MGI:MGI:2140950};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=NIH Swiss;
RA Papin C.;
RT "XRbm9, a new XGld2-interacting protein, enhances translation in Xenopus
RT oocytes.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-484.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP ENZYME ACTIVITY.
RX PubMed=15070731; DOI=10.1073/pnas.0400779101;
RA Kwak J.E., Wang L., Ballantyne S., Kimble J., Wickens M.;
RT "Mammalian GLD-2 homologs are poly(A) polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:4407-4412(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15987818; DOI=10.1261/rna.2630205;
RA Rouhana L., Wang L., Buter N., Kwak J.E., Schiltz C.A., Gonzalez T.,
RA Kelley A.E., Landry C.F., Wickens M.;
RT "Vertebrate GLD2 poly(A) polymerases in the germline and the brain.";
RL RNA 11:1117-1130(2005).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF ASP-215.
RX PubMed=16325797; DOI=10.1016/j.ydbio.2005.10.017;
RA Nakanishi T., Kubota H., Ishibashi N., Kumagai S., Watanabe H.,
RA Yamashita M., Kashiwabara S., Miyado K., Baba T.;
RT "Possible role of mouse poly(A) polymerase mGLD-2 during oocyte
RT maturation.";
RL Dev. Biol. 289:115-126(2006).
RN [7]
RP DISRUPTION PHENOTYPE, AND INTERACTION WITH CPEB1; CPEB2; CPSF1 AND PABPC1.
RX PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M.,
RA Kashiwabara S., Baba T.;
RT "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT polyadenylation status in oocytes and somatic cells.";
RL Biochem. Biophys. Res. Commun. 364:14-19(2007).
CC -!- FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP
CC monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In
CC contrast to the canonical nuclear poly(A) RNA polymerase, it only adds
CC poly(A) to selected cytoplasmic mRNAs. Does not play a role in
CC replication-dependent histone mRNA degradation (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:15070731};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Interacts with CPEB1, CPEB2, CPSF1 and PABPC1.
CC {ECO:0000269|PubMed:17927953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16325797}. Nucleus
CC {ECO:0000269|PubMed:16325797}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91YI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91YI6-2; Sequence=VSP_034325;
CC -!- TISSUE SPECIFICITY: Ubiquitous. In brain, it is highly expressed in the
CC cerebral cortex, cerebellum, hippocampus and olfactory bulb.
CC {ECO:0000269|PubMed:15987818, ECO:0000269|PubMed:16325797}.
CC -!- DEVELOPMENTAL STAGE: Expressed in oocytes from metaphase I to metaphase
CC II during oocyte maturation. {ECO:0000269|PubMed:16325797}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal and healthy. Poly-A tail
CC elongation in oocytes is not affected and mice are fertile.
CC {ECO:0000269|PubMed:17927953}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family. GLD2
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28170.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AM419011; CAL91354.1; -; mRNA.
DR EMBL; BC016629; AAH16629.1; -; mRNA.
DR EMBL; AK033141; BAC28170.1; ALT_FRAME; mRNA.
DR CCDS; CCDS26686.1; -. [Q91YI6-1]
DR CCDS; CCDS88498.1; -. [Q91YI6-2]
DR RefSeq; NP_598666.1; NM_133905.2. [Q91YI6-1]
DR RefSeq; XP_006517573.1; XM_006517510.3. [Q91YI6-1]
DR RefSeq; XP_006517574.1; XM_006517511.3.
DR RefSeq; XP_017170820.1; XM_017315331.1.
DR PDB; 6LBJ; X-ray; 2.70 A; A/B=143-484.
DR PDBsum; 6LBJ; -.
DR AlphaFoldDB; Q91YI6; -.
DR SMR; Q91YI6; -.
DR BioGRID; 221516; 3.
DR IntAct; Q91YI6; 2.
DR STRING; 10090.ENSMUSP00000048124; -.
DR PhosphoSitePlus; Q91YI6; -.
DR EPD; Q91YI6; -.
DR MaxQB; Q91YI6; -.
DR PaxDb; Q91YI6; -.
DR PeptideAtlas; Q91YI6; -.
DR PRIDE; Q91YI6; -.
DR ProteomicsDB; 267449; -. [Q91YI6-1]
DR ProteomicsDB; 267450; -. [Q91YI6-2]
DR Antibodypedia; 24569; 108 antibodies from 20 providers.
DR DNASU; 100715; -.
DR Ensembl; ENSMUST00000048702; ENSMUSP00000048124; ENSMUSG00000042167. [Q91YI6-1]
DR Ensembl; ENSMUST00000225868; ENSMUSP00000153703; ENSMUSG00000042167. [Q91YI6-2]
DR GeneID; 100715; -.
DR KEGG; mmu:100715; -.
DR UCSC; uc007rkz.1; mouse. [Q91YI6-2]
DR UCSC; uc007rla.1; mouse. [Q91YI6-1]
DR CTD; 167153; -.
DR MGI; MGI:2140950; Tent2.
DR VEuPathDB; HostDB:ENSMUSG00000042167; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000156640; -.
DR HOGENOM; CLU_046147_0_0_1; -.
DR InParanoid; Q91YI6; -.
DR OMA; LNRKELC; -.
DR OrthoDB; 803033at2759; -.
DR PhylomeDB; Q91YI6; -.
DR TreeFam; TF315661; -.
DR BRENDA; 2.7.7.19; 3474.
DR BioGRID-ORCS; 100715; 0 hits in 69 CRISPR screens.
DR ChiTaRS; Papd4; mouse.
DR PRO; PR:Q91YI6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q91YI6; protein.
DR Bgee; ENSMUSG00000042167; Expressed in uterus and 68 other tissues.
DR ExpressionAtlas; Q91YI6; baseline and differential.
DR Genevisible; Q91YI6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0034062; F:5'-3' RNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0070566; F:adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISO:MGI.
DR GO; GO:1990603; P:dark adaptation; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:2000626; P:negative regulation of miRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; ISO:MGI.
DR GO; GO:0043489; P:RNA stabilization; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Magnesium;
KW Manganese; Metal-binding; mRNA processing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..484
FT /note="Poly(A) RNA polymerase GLD2"
FT /id="PRO_0000341550"
FT DOMAIN 386..440
FT /note="PAP-associated"
FT MOTIF 76..92
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIY7"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIY7"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIY7"
FT VAR_SEQ 225..228
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034325"
FT MUTAGEN 215
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:16325797"
FT CONFLICT 357
FT /note="P -> T (in Ref. 3; BAC28170)"
FT /evidence="ECO:0000305"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 171..191
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 234..248
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 254..260
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 286..300
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 304..317
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 357..360
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 366..369
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 370..375
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 404..406
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 407..410
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 411..414
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 423..426
FT /evidence="ECO:0007829|PDB:6LBJ"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:6LBJ"
FT TURN 441..444
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 448..467
FT /evidence="ECO:0007829|PDB:6LBJ"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:6LBJ"
SQ SEQUENCE 484 AA; 55934 MW; C60D799AA5F14CB6 CRC64;
MFPNSILGRP PFTPTHQQHN NFFALSPTLY SHQQLIDAQF NFQNVDLSRA VSLQPLTYGT
VSPIQTSTSP LFRGRKRISD EKAFPLDGKR QRFHSPHQEP TIINQLVPLS GDRRYSMPPL
FHTHYIPDIV RCVPPLREIP LLEPREITLP EAKDKLSQQI LELFETCQQQ ASDLKKKELC
RAQLQREIQL LFPQSRLFLV GSSLNGFGAR SSDGDLCLVV KEEPCFFQVN QKTEARHILT
LVHKHFCTRL SGYIERPQLI RAKVPIVKFR DKVSCVEFDL NVNNTVGIRN TFLLRTYAYL
ENRVRPLVLV IKKWASHHDI NDASRGTLSS YSLVLMVLHY LQTLPEPILP SLQKIYPESF
STSVQLHLVH HAPCNVPPYL SKNESSLGDL LLGFLKYYAT EFDWNTQMIS VREAKAIPRP
DDMEWRNKYI CVEEPFDGTN TARAVHEKQK FDMIKDQFLK SWQRLKNKRD LNSVLPLRAA
TLKR
