ID   RPB4_DROME              Reviewed;         139 AA.
AC   Q9VEA5; Q4V3P8; Q8I0A4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 5.
DT   25-JAN-2012, entry version 77.
DE   RecName: Full=DNA-directed RNA polymerase II 16 kDa polypeptide;
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase II accessory factor rpb4;
GN   Name=Rpb4; ORFNames=CG33520;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX   MEDLINE=22371511; PubMed=12482983; DOI=10.1128/MCB.23.1.306-321.2003;
RA   Muratoglu S., Georgieva S., Papai G., Scheer E., Enunlu I.,
RA   Komonyi O., Cserpan I., Lebedeva L., Nabirochkina E., Udvardy A.,
RA   Tora L., Boros I.;
RT   "Two different Drosophila ADA2 homologues are present in distinct GCN5
RT   histone acetyltransferase-containing complexes.";
RL   Mol. Cell. Biol. 23:306-321(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC   STRAIN=Berkeley;
RX   MEDLINE=22426069; PubMed=12537572;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   MEDLINE=22584206; PubMed=12697829;
RX   DOI=10.1128/MCB.23.9.3305-3319.2003;
RA   Kusch T., Guelman S., Abmayr S.M., Workman J.L.;
RT   "Two Drosophila Ada2 homologues function in different multiprotein
RT   complexes.";
RL   Mol. Cell. Biol. 23:3305-3319(2003).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Associates with POLR2G.
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: RNA polymerase II consists of 12 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=D;
CC         IsoId=Q9VEA5-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q7KSD8-1; Sequence=External;
CC         Note=No experimental confirmation available;
CC       Name=A;
CC         IsoId=Q7KSD8-2; Sequence=External;
CC         Note=No experimental confirmation available;
CC       Name=C; Synonyms=ADA2A-SV2;
CC         IsoId=Q7KSD8-3; Sequence=External;
CC       Name=E; Synonyms=ADA2A-SV1;
CC         IsoId=Q7KSD8-4; Sequence=External;
CC   -!- MISCELLANEOUS: Three distinct zinc-containing RNA polymerases are
CC       found in eukaryotic nuclei: polymerase I for the ribosomal RNA
CC       precursor, polymerase II for the mRNA precursor, and polymerase
CC       III for 5S and tRNA genes.
CC   -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC       family.
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DR   EMBL; AF544019; AAN88031.1; -; mRNA.
DR   EMBL; AF544020; AAN88032.1; -; mRNA.
DR   EMBL; AE014297; AAF55522.5; -; Genomic_DNA.
DR   EMBL; BT022168; AAY51562.1; -; mRNA.
DR   EMBL; BT023308; AAY55724.1; -; mRNA.
DR   EMBL; BT023309; AAY55725.1; -; mRNA.
DR   RefSeq; NP_001014633.2; NM_001014633.2.
DR   UniGene; Dm.13710; -.
DR   HSSP; O15514; 2C35.
DR   ProteinModelPortal; Q9VEA5; -.
DR   SMR; Q9VEA5; 11-138.
DR   IntAct; Q9VEA5; 3.
DR   MINT; MINT-764159; -.
DR   STRING; Q9VEA5; -.
DR   PRIDE; Q9VEA5; -.
DR   EnsemblMetazoa; FBtr0300246; FBpp0289479; FBgn0053520.
DR   GeneID; 326128; -.
DR   KEGG; dme:Dmel_CG33520; -.
DR   UCSC; CG33520-RA; d. melanogaster.
DR   CTD; 326128; -.
DR   FlyBase; FBgn0053520; Rpb4.
DR   eggNOG; inNOG08964; -.
DR   GeneTree; EMGT00070000025801; -.
DR   InParanoid; Q9VEA5; -.
DR   OrthoDB; EOG4FXPPS; -.
DR   NextBio; 847197; -.
DR   Bgee; Q9VEA5; -.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR   GO; GO:0043189; C:H4/H2A histone acetyltransferase complex; IDA:FlyBase.
DR   GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008283; P:cell proliferation; IDA:FlyBase.
DR   GO; GO:0043966; P:histone H3 acetylation; IDA:FlyBase.
DR   GO; GO:0007095; P:mitotic cell cycle G2/M transition DNA damage checkpoint; IGI:FlyBase.
DR   GO; GO:0035065; P:regulation of histone acetylation; IDA:FlyBase.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   InterPro; IPR010997; HRDC-like.
DR   InterPro; IPR005574; RNA_pol_II_Rpb4.
DR   InterPro; IPR006590; RNA_pol_II_Rpb4_core.
DR   KO; K03012; -.
DR   Pfam; PF03874; RNA_pol_Rpb4; 1.
DR   SMART; SM00657; RPOL4c; 1.
DR   SUPFAM; SSF47819; HRDC_like; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW   Transferase.
FT   CHAIN         1    139       DNA-directed RNA polymerase II 16 kDa
FT                                polypeptide.
FT                                /FTId=PRO_0000283732.
FT   CONFLICT    124    126       LRQ -> ARE (in Ref. 1; AAN88031/
FT                                AAN88032).
SQ   SEQUENCE   139 AA;  16212 MW;  F7541C9A08C23CB1 CRC64;
     MSFMNPVDMV DEDAADLQFP KEFENAETLL ISEVHMLLDH RKRQNESADE EQEFSEVFMK
     TYAYTDSFRK FKNKETIMSA RSLLMQKKLH KFELAALGNL CPEAPEEAKA LIPSLEGRFE
     DEELRQILDD IGTKRSLQY
//