RPAC2_HUMAN
ID RPAC2_HUMAN Reviewed; 133 AA.
AC P0DPB6; Q5TBX2; Q96BR3; Q9Y2S0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2017, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC2;
DE Short=RNA polymerases I and III subunit AC2;
DE AltName: Full=AC19;
DE AltName: Full=DNA-directed RNA polymerase I subunit D;
DE AltName: Full=RNA polymerase I 16 kDa subunit;
DE Short=RPA16;
DE AltName: Full=RPC16;
DE AltName: Full=hRPA19;
GN Name=POLR1D;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Ye M., Zhang Q., Fu G., Zhou J., Yu Y., Shen Y., Wu J., He K., Chen S.,
RA Mao M., Chen Z.;
RT "Human RNA polymerase I 16-kDa subunit.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 [4]
RP PROTEIN SEQUENCE OF 1-9 AND 88-98, ACETYLATION AT MET-1, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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., Buerckstuemmer 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [10]
RP VARIANTS TCS2 LYS-47; ILE-50; ARG-51; GLU-52; CYS-56; SER-82 AND SER-99.
RX PubMed=21131976; DOI=10.1038/ng.724;
RA Dauwerse J.G., Dixon J., Seland S., Ruivenkamp C.A., van Haeringen A.,
RA Hoefsloot L.H., Peters D.J., Boers A.C., Daumer-Haas C., Maiwald R.,
RA Zweier C., Kerr B., Cobo A.M., Toral J.F., Hoogeboom A.J., Lohmann D.R.,
RA Hehr U., Dixon M.J., Breuning M.H., Wieczorek D.;
RT "Mutations in genes encoding subunits of RNA polymerases I and III cause
RT Treacher Collins syndrome.";
RL Nat. Genet. 43:20-22(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common core component of RNA polymerases I and III which synthesize
CC ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs,
CC respectively.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase
CC III (Pol III) complexes consisting of at least 13 and 17 subunits,
CC respectively. {ECO:0000250}.
CC -!- INTERACTION:
CC P0DPB6; P55212: CASP6; NbExp=3; IntAct=EBI-359498, EBI-718729;
CC P0DPB6; P06396: GSN; NbExp=3; IntAct=EBI-359498, EBI-351506;
CC P0DPB6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-359498, EBI-21591415;
CC P0DPB6; O15160: POLR1C; NbExp=16; IntAct=EBI-359498, EBI-1055079;
CC P0DPB6; P62826: RAN; NbExp=3; IntAct=EBI-359498, EBI-286642;
CC P0DPB6; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-359498, EBI-741480;
CC P0DPB6; Q9Y649; NbExp=3; IntAct=EBI-359498, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0DPB6-1, Q9Y2S0-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P0DPB5-1; Sequence=External;
CC -!- DISEASE: Treacher Collins syndrome 2 (TCS2) [MIM:613717]: A form of
CC Treacher Collins syndrome, a disorder of craniofacial development.
CC Treacher Collins syndrome is characterized by a combination of
CC bilateral downward slanting of the palpebral fissures, colobomas of the
CC lower eyelids with a paucity of eyelashes medial to the defect,
CC hypoplasia of the facial bones, cleft palate, malformation of the
CC external ears, atresia of the external auditory canals, and bilateral
CC conductive hearing loss. {ECO:0000269|PubMed:21131976}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC polymerase subunit family. {ECO:0000305}.
CC -!- CAUTION: Contrary to isoform 2, isoform 1 contains an RNA polymerase
CC domain and has DNA-dependent RNA polymerase function. Synteny studies
CC in vertebrates suggest that this isoform has been created by a
CC mammalian-specific retrotransposition event of an ancestral gene which
CC has been lost later on in this lineage. {ECO:0000305}.
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DR EMBL; AF077044; AAD27777.1; -; mRNA.
DR EMBL; AL136439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000889; AAH00889.1; -; mRNA.
DR CCDS; CCDS9325.1; -.
DR RefSeq; NP_057056.1; NM_015972.3. [P0DPB6-1]
DR RefSeq; XP_005266469.1; XM_005266412.1.
DR PDB; 7A6H; EM; 3.30 A; K=1-133.
DR PDB; 7AE1; EM; 2.80 A; K=1-133.
DR PDB; 7AE3; EM; 3.10 A; K=1-133.
DR PDB; 7AEA; EM; 3.40 A; K=1-133.
DR PDB; 7AST; EM; 4.00 A; G=1-133.
DR PDB; 7D58; EM; 2.90 A; K=1-133.
DR PDB; 7D59; EM; 3.10 A; K=1-133.
DR PDB; 7DN3; EM; 3.50 A; K=1-133.
DR PDB; 7DU2; EM; 3.35 A; K=1-133.
DR PDB; 7FJI; EM; 3.60 A; K=1-133.
DR PDB; 7FJJ; EM; 3.60 A; K=1-133.
DR PDB; 7OB9; EM; 2.70 A; K=1-133.
DR PDB; 7OBA; EM; 3.10 A; K=1-133.
DR PDB; 7OBB; EM; 3.30 A; K=1-133.
DR PDB; 7VBA; EM; 2.89 A; K=1-133.
DR PDB; 7VBB; EM; 2.81 A; K=1-133.
DR PDB; 7VBC; EM; 3.01 A; K=1-133.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; P0DPB6; -.
DR SMR; P0DPB6; -.
DR IntAct; P0DPB6; 30.
DR MINT; P0DPB6; -.
DR STRING; 9606.ENSP00000302478; -.
DR GlyGen; P0DPB6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0DPB6; -.
DR MetOSite; P0DPB6; -.
DR PhosphoSitePlus; P0DPB6; -.
DR BioMuta; POLR1D; -.
DR SWISS-2DPAGE; P0DPB6; -.
DR EPD; P0DPB6; -.
DR jPOST; P0DPB6; -.
DR MassIVE; P0DPB6; -.
DR PeptideAtlas; P0DPB6; -.
DR PRIDE; P0DPB6; -.
DR Antibodypedia; 22678; 113 antibodies from 25 providers.
DR DNASU; 51082; -.
DR Ensembl; ENST00000302979.5; ENSP00000302478.4; ENSG00000186184.20. [P0DPB6-1]
DR GeneID; 51082; -.
DR KEGG; hsa:51082; -.
DR MANE-Select; ENST00000302979.5; ENSP00000302478.4; NM_015972.4; NP_057056.1.
DR CTD; 51082; -.
DR DisGeNET; 51082; -.
DR GeneCards; POLR1D; -.
DR GeneReviews; POLR1D; -.
DR HGNC; HGNC:20422; POLR1D.
DR HPA; ENSG00000186184; Low tissue specificity.
DR MalaCards; POLR1D; -.
DR MIM; 613715; gene.
DR MIM; 613717; phenotype.
DR neXtProt; NX_P0DPB6; -.
DR OpenTargets; ENSG00000186184; -.
DR VEuPathDB; HostDB:ENSG00000186184; -.
DR eggNOG; KOG3438; Eukaryota.
DR GeneTree; ENSGT00550000075160; -.
DR OMA; MRIQMYD; -.
DR OrthoDB; 1398114at2759; -.
DR PathwayCommons; P0DPB6; -.
DR SignaLink; P0DPB6; -.
DR SIGNOR; P0DPB6; -.
DR ChiTaRS; POLR1D; human.
DR Pharos; P0DPB6; Tbio.
DR Proteomes; UP000005640; Chromosome 13.
DR Bgee; ENSG00000186184; Expressed in body of pancreas and 205 other tissues.
DR ExpressionAtlas; P0DPB6; baseline and differential.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd07029; RNAP_I_III_AC19; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR009025; RBP11-like_dimer.
DR InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR InterPro; IPR033898; RNAP_AC19.
DR Pfam; PF13656; RNA_pol_L_2; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; DNA-directed RNA polymerase; Nucleus; Reference proteome;
KW Transcription.
FT CHAIN 1..133
FT /note="DNA-directed RNA polymerases I and III subunit
FT RPAC2"
FT /id="PRO_0000149316"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.4, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT VARIANT 47
FT /note="E -> K (in TCS2; dbSNP:rs767196650)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064892"
FT VARIANT 50
FT /note="T -> I (in TCS2)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064893"
FT VARIANT 51
FT /note="L -> R (in TCS2; dbSNP:rs1593275448)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064894"
FT VARIANT 52
FT /note="G -> E (in TCS2)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064895"
FT VARIANT 56
FT /note="R -> C (in TCS2; dbSNP:rs1014369151)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064896"
FT VARIANT 82
FT /note="L -> S (in TCS2)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064897"
FT VARIANT 99
FT /note="G -> S (in TCS2)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064898"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 79..90
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 94..128
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 133 AA; 15237 MW; 715DAEF2B22B1C76 CRC64;
MEEDQELERK ISGLKTSMAE GERKTALEMV QAAGTDRHCV TFVLHEEDHT LGNSLRYMIM
KNPEVEFCGY TTTHPSESKI NLRIQTRGTL PAVEPFQRGL NELMNVCQHV LDKFEASIKD
YKDQKASRNE STF
