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Database: UniProt
Entry: G3XAH6_HUMAN
LinkDB: G3XAH6_HUMAN
Original site: G3XAH6_HUMAN 
ID   G3XAH6_HUMAN            Unreviewed;       724 AA.
AC   G3XAH6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Poly(A) polymerase {ECO:0000256|PIRNR:PIRNR018425};
DE            EC=2.7.7.19 {ECO:0000256|PIRNR:PIRNR018425};
GN   Name=PAPOLA {ECO:0000313|Ensembl:ENSP00000376716.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000376716.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000376716.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [2] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [3] {ECO:0007829|PubMed:19690332}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [4] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [5] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6] {ECO:0007829|PubMed:22223895}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [7] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [8] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9] {ECO:0000313|Ensembl:ENSP00000376716.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC       {ECO:0000256|PIRNR:PIRNR018425}.
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:0000256|ARBA:ARBA00024620,
CC         ECO:0000256|PIRNR:PIRNR018425};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR018425-2};
CC       Note=Binds 2 magnesium ions. Also active with manganese.
CC       {ECO:0000256|PIRSR:PIRSR018425-2};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR018425}.
CC   -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC       {ECO:0000256|ARBA:ARBA00010912, ECO:0000256|PIRNR:PIRNR018425}.
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DR   EMBL; AL163051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005267338.1; XM_005267281.1.
DR   AlphaFoldDB; G3XAH6; -.
DR   SMR; G3XAH6; -.
DR   EPD; G3XAH6; -.
DR   MassIVE; G3XAH6; -.
DR   MaxQB; G3XAH6; -.
DR   PeptideAtlas; G3XAH6; -.
DR   ProteomicsDB; 33751; -.
DR   Antibodypedia; 86; 175 antibodies from 22 providers.
DR   Ensembl; ENST00000392990.6; ENSP00000376716.2; ENSG00000090060.19.
DR   UCSC; uc010twv.3; human.
DR   HGNC; HGNC:14981; PAPOLA.
DR   VEuPathDB; HostDB:ENSG00000090060; -.
DR   GeneTree; ENSGT00940000154598; -.
DR   HOGENOM; CLU_011511_1_2_1; -.
DR   BioGRID-ORCS; 10914; 149 hits in 1161 CRISPR screens.
DR   ChiTaRS; PAPOLA; human.
DR   GenomeRNAi; 10914; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000090060; Expressed in colonic epithelium and 212 other cell types or tissues.
DR   ExpressionAtlas; G3XAH6; baseline and differential.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
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   InterPro; IPR014492; PolyA_polymerase.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR   PANTHER; PTHR10682:SF9; POLY(A) POLYMERASE ALPHA; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 2.
DR   PIRSF; PIRSF018425; PolyA_polymerase; 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR018425};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR018425-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR018425-2};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|PIRNR:PIRNR018425};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR018425};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR018425};
KW   Proteomics identification {ECO:0007829|EPD:G3XAH6,
KW   ECO:0007829|MaxQB:G3XAH6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018425}.
FT   DOMAIN          21..214
FT                   /note="Poly(A) polymerase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20750"
FT   DOMAIN          219..363
FT                   /note="Poly(A) polymerase central"
FT                   /evidence="ECO:0000259|Pfam:PF04928"
FT   DOMAIN          366..434
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   DOMAIN          426..506
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          523..565
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        652..672
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..690
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         100..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         109
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         113..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         113
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         167
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         228
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         246..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
SQ   SEQUENCE   724 AA;  80626 MW;  81465859D6E351F0 CRC64;
     MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCVLTQ KLIETLKPFG VFEEEEELQR
     RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA
     PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE
     DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI
     LGFLGGVSWA MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW
     DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE ILLSKAEWSK
     LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS
     FPAPKENPDK EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD
     MKIAAMHVKR KQLHQLLPNH VLQKKKKHST EGVKLTALND SSLDLSMDSD NSMSVPSPTS
     ATKTSPLNSS GSSQGRNSPA PAVTAASVTN IQATEVSVPQ VNSSESSGGT SSESIPQTAT
     QPAISPPPKP TVSRVVSSTR LVNPPPRSSG NAATSGNAAT KIPTPIVGVK RTSSPHKEES
     PKKTKTEEEQ LDTETSTTQS ETIQTAASLL ASQKTSSTDL SDIPALPANP IPVIKNSIKL
     RLNR
//
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