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   24-JAN-2024, entry version 159.
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; 10090-ENSMUSP00000100595; -.
DR   ProteomicsDB; 288057; -.
DR   Ensembl; ENSMUST00000099400.3; ENSMUSP00000100595.2; ENSMUSG00000074817.3.
DR   GeneID; 56522; -.
DR   KEGG; mmu:56522; -.
DR   AGR; MGI:1932115; -.
DR   CTD; 56903; -.
DR   MGI; MGI:1932115; Papolb.
DR   eggNOG; KOG2245; Eukaryota.
DR   GeneTree; ENSGT00940000164307; -.
DR   InParanoid; Q9WVP6; -.
DR   OMA; EWKWPQP; -.
DR   OrthoDB; 1351913at2759; -.
DR   BRENDA; 2.7.7.19; 3474.
DR   BioGRID-ORCS; 56522; 1 hit in 78 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:1990817; F:poly(A) RNA polymerase activity; ISS:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR007012; PolA_pol_cen_dom.
DR   InterPro; IPR048840; PolA_pol_NTPase.
DR   InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR   PANTHER; PTHR10682:SF19; POLY(A) POLYMERASE BETA; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 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
//