PAPOB_MOUSE
ID PAPOB_MOUSE Reviewed; 642 AA.
AC Q9WVP6; Q9R1R3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Poly(A) polymerase beta {ECO:0000305};
DE Short=PAP-beta;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase beta;
DE AltName: Full=Testis-specific poly(A) polymerase;
GN Name=Papolb {ECO:0000312|MGI:MGI:1932115}; Synonyms=Papt, Tpap;
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], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=11150526; DOI=10.1016/s0014-5793(00)02367-x;
RA Lee Y.J., Lee Y., Chung J.H.;
RT "An intronless gene encoding a poly(A) polymerase is specifically expressed
RT in testis.";
RL FEBS Lett. 487:287-292(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ddY; TISSUE=Testis;
RX PubMed=11087630; DOI=10.1006/dbio.2000.9894;
RA Kashiwabara S., Zhuang T., Yamagata K., Noguchi J., Fukamizu A., Baba T.;
RT "Identification of a novel isoform of poly(A) polymerase, TPAP,
RT specifically present in the cytoplasm of spermatogenic cells.";
RL Dev. Biol. 228:106-115(2000).
RN [3]
RP INTERACTION WITH GSG1.
RX PubMed=18325338; DOI=10.1016/j.febslet.2008.01.065;
RA Choi H.-S., Lee S.-H., Kim H., Lee Y.;
RT "Germ cell-specific gene 1 targets testis-specific poly(A) polymerase to
RT the endoplasmic reticulum through protein-protein interactions.";
RL FEBS Lett. 582:1203-1209(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
CC -!- SUBUNIT: Interacts with GSG1. {ECO:0000269|PubMed:18325338}.
CC -!- INTERACTION:
CC Q9WVP6; Q8R1W2: Gsg1; NbExp=8; IntAct=EBI-7842113, EBI-7842142;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:11150526}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels in 2-week-old mice.
CC Abundantly expressed in 4-week-old and 6-week-old animals.
CC {ECO:0000269|PubMed:11150526}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43624.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF039957; AAD43624.1; ALT_INIT; mRNA.
DR EMBL; AB030729; BAA83086.1; -; mRNA.
DR CCDS; CCDS39362.1; -.
DR RefSeq; NP_064327.1; NM_019943.2.
DR AlphaFoldDB; Q9WVP6; -.
DR SMR; Q9WVP6; -.
DR BioGRID; 208033; 2.
DR IntAct; Q9WVP6; 4.
DR MINT; Q9WVP6; -.
DR STRING; 10090.ENSMUSP00000100595; -.
DR iPTMnet; Q9WVP6; -.
DR PhosphoSitePlus; Q9WVP6; -.
DR MaxQB; Q9WVP6; -.
DR PaxDb; Q9WVP6; -.
DR PRIDE; Q9WVP6; -.
DR ProteomicsDB; 288057; -.
DR Ensembl; ENSMUST00000099400; ENSMUSP00000100595; ENSMUSG00000074817.
DR GeneID; 56522; -.
DR KEGG; mmu:56522; -.
DR CTD; 56903; -.
DR MGI; MGI:1932115; Papolb.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000164307; -.
DR InParanoid; Q9WVP6; -.
DR OMA; ITAMHLR; -.
DR OrthoDB; 326577at2759; -.
DR BRENDA; 2.7.7.19; 3474.
DR BioGRID-ORCS; 56522; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q9WVP6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WVP6; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; ISA:MGI.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 1.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleus; Reference proteome;
KW RNA-binding; Transferase.
FT CHAIN 1..642
FT /note="Poly(A) polymerase beta"
FT /id="PRO_0000051623"
FT REGION 530..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 247..248
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 154
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 159
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 329
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 400
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT CONFLICT 202
FT /note="L -> F (in Ref. 1; AAD43624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 72329 MW; 3F00E71A399EE096 CRC64;
MMPFAVTTQG AQQPAPAPKQ FGISSPISLA APKDTDRELT QKLIETLQPF GVFEEEEELQ
RRILILQKLN NLVKEWIREI SESRNLPQAV IENVGGKIFT FGSYRLGVHT KGADIDALCV
APRHVDRNDF FTSFYDKLKL QEEVKDLRAV EEAFVPVIKL CFDGIEIDIL FARLALQTIP
EDLDLRDDSL LKNLDIRCIR SLNGCRVTDE ILHLVPNIDS FRLTLRAIKL WAKCHNIYSN
ILGFLGGVSW AMLVARTCQL YPNAIASTLV RKFFLVFSEW EWPNPVLLKE PEERNLNLPV
WDPRVNPSDR YHLMPIITPA YPQQNSTYNV SVSTRMVMIE EFKQGLAITH EILLNKAEWS
KLFEAPSFFQ KYKHYIVLLA SAPTEKQHLE WVGLVESKIR ILVGSLEKNE FITLAHVNPQ
SFPAPKETAD KEEFRTMWVI GLVLKKPENS EILSIDLTYD IQSFTDTVYR QAINSKMFEM
DMKIAAMHLR RKELHQLLPN HVLQKKETHL TESVRLTAVT DSSLLLSIDS ENSMTAPSPT
GTMKTGPLTG NPQGRNSPAL AVMAASVTNI QFPDVSLQHV NPIESSGIAL SESIPQIPSQ
PTISPPPKPT MTRVVSSTHL VNHPSRPSGN TATNIPNPIL GV
