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Database: UniProt
Entry: A4D1Z6_HUMAN
LinkDB: A4D1Z6_HUMAN
Original site: A4D1Z6_HUMAN 
ID   A4D1Z6_HUMAN            Unreviewed;       637 AA.
AC   A4D1Z6;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Poly(A) polymerase {ECO:0000256|PIRNR:PIRNR018425};
DE            EC=2.7.7.19 {ECO:0000256|PIRNR:PIRNR018425};
GN   Name=PAPOLB {ECO:0000313|EMBL:EAL23967.1};
GN   ORFNames=tcag7.894 {ECO:0000313|EMBL:EAL23967.1};
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|EMBL:EAL23967.1};
RN   [1] {ECO:0000313|EMBL:EAL23967.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J., Grzeschik K.H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Dohner H.,
RA   Dohner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [2] {ECO:0000313|EMBL:EAL23967.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Nusskern D., Zhang Q., Gu Z., Lu F., Zeesman S., Teshima I.,
RA   Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R.,
RA   Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.,
RA   Lococo F., Belloni E., Shaffer L.G., Morton C.C., Pober B., Gusella J.,
RA   Bruns G., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W.,
RA   Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M.,
RA   Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H.,
RA   Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.Angel.,
RA   Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P.,
RA   Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J.,
RA   Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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; CH236953; EAL23967.1; -; Genomic_DNA.
DR   RefSeq; NP_064529.4; NM_020144.4.
DR   AlphaFoldDB; A4D1Z6; -.
DR   SMR; A4D1Z6; -.
DR   MaxQB; A4D1Z6; -.
DR   PeptideAtlas; A4D1Z6; -.
DR   Antibodypedia; 24543; 88 antibodies from 20 providers.
DR   DNASU; 56903; -.
DR   GeneID; 56903; -.
DR   KEGG; hsa:56903; -.
DR   CTD; 56903; -.
DR   PharmGKB; PA32933; -.
DR   VEuPathDB; HostDB:ENSG00000218823; -.
DR   HOGENOM; CLU_011511_1_2_1; -.
DR   OMA; YSICKGS; -.
DR   OrthoDB; 1351913at2759; -.
DR   BioGRID-ORCS; 56903; 4 hits in 381 CRISPR screens.
DR   GenomeRNAi; 56903; -.
DR   ExpressionAtlas; A4D1Z6; baseline and differential.
DR   Genevisible; A4D1Z6; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:SF19; POLY(A) POLYMERASE BETA; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 1.
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   3: Inferred from homology;
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018425}.
FT   DOMAIN          22..215
FT                   /note="Poly(A) polymerase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20750"
FT   DOMAIN          220..364
FT                   /note="Poly(A) polymerase central"
FT                   /evidence="ECO:0000259|Pfam:PF04928"
FT   DOMAIN          367..434
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         114..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         114
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         114
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         116
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         116
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         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         168
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         229
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         247..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
SQ   SEQUENCE   637 AA;  71813 MW;  DEF83370A87D10B8 CRC64;
     MMPFPVTTQG PPQPAPPPNR YGVSSPISLA VPKETDCLLT QRLIETLRPF GVFEEEEELQ
     RRILVLEKLN NLVKEWIREI SESKSLPQSV IENVGGKIFT FGSYRLGVHT KGADIDALCV
     APSHVDRSDF FTSFYAKLKL QEEVKDLRAV EEAFVPVIKL CFDGIEIDIL FARLALQTIP
     EDLDLRDDSL LKNLDIRCIR SLNGCRVTDE ILHLVPNIDN FRLTLRAIKL WAKCHNIYSN
     ILGFLGGVSW AMLVARTCQL YPNAVASTLV RKFFLVFSEW EWPNPVLLKE PEERNLNLPV
     WDPRVNPSDR YHLMPIITPA YPQQNSTYNV SISTRMVMIE EFKQGLAITH EILLSKAEWS
     KLFEAPSFFQ KYKHYIVLLA SASTEKQHLE WVGLVESKIR ILVGSLEKNE FITLAHVNPQ
     SFPAPKENPD MEEFRTMWVI GLGLKKPDNS EILSIDLTYD IQSFTDTVYR QAVNSKMFEM
     GMKITAMHLR RKELHQLLPH HVLQDKKAHS TEGRRLTDLN DSSFDLSAGC ENSMSVPSST
     STMKTGPLIS SSQGRNSPAL AVMTASVANI QATEFSLQQV NTNESSGVAL NESIPHAVSQ
     PAISPSPKAM VARVVSSTCL ISHPDLQETQ QQTYLIL
//
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