ID   RPAP1_RAT               Reviewed;        1400 AA.
AC   Q3T1I9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=RNA polymerase II-associated protein 1;
GN   Name=Rpap1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Forms an interface between the RNA polymerase II enzyme and
CC       chaperone/scaffolding protein, suggesting that it is required to
CC       connect RNA polymerase II to regulators of protein complex formation.
CC       Required for interaction of the RNA polymerase II complex with
CC       acetylated histone H3 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of an RNA polymerase II complex that contains POLR2A,
CC       POLR2B, POLR2C, POLR2D, POLR2E, POLR2F, POLR2G, POLR2H, POLR2I, POLR2J,
CC       POLR2K, POLR2L, RPAP1, FCP1 plus the general transcription factors
CC       TFIIB and TFIIF. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RPAP1 family. {ECO:0000305}.
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DR   EMBL; BC101894; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001029171.1; NM_001033999.2.
DR   RefSeq; XP_006234833.1; XM_006234771.3.
DR   RefSeq; XP_006234834.1; XM_006234772.3.
DR   RefSeq; XP_006234835.1; XM_006234773.3.
DR   RefSeq; XP_017447220.1; XM_017591731.1.
DR   RefSeq; XP_017447221.1; XM_017591732.1.
DR   AlphaFoldDB; Q3T1I9; -.
DR   SMR; Q3T1I9; -.
DR   STRING; 10116.ENSRNOP00000007299; -.
DR   iPTMnet; Q3T1I9; -.
DR   PhosphoSitePlus; Q3T1I9; -.
DR   jPOST; Q3T1I9; -.
DR   PaxDb; Q3T1I9; -.
DR   PRIDE; Q3T1I9; -.
DR   Ensembl; ENSRNOT00000007299; ENSRNOP00000007299; ENSRNOG00000005483.
DR   GeneID; 311338; -.
DR   KEGG; rno:311338; -.
DR   UCSC; RGD:1590891; rat.
DR   CTD; 26015; -.
DR   RGD; 1590891; Rpap1.
DR   eggNOG; KOG1894; Eukaryota.
DR   eggNOG; KOG4732; Eukaryota.
DR   GeneTree; ENSGT00390000007594; -.
DR   HOGENOM; CLU_005296_1_0_1; -.
DR   InParanoid; Q3T1I9; -.
DR   OMA; RMDKAPK; -.
DR   OrthoDB; 25908at2759; -.
DR   PhylomeDB; Q3T1I9; -.
DR   TreeFam; TF324391; -.
DR   PRO; PR:Q3T1I9; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000005483; Expressed in skeletal muscle tissue and 18 other tissues.
DR   Genevisible; Q3T1I9; RN.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013929; RNA_pol_II_AP1_C.
DR   InterPro; IPR013930; RNA_pol_II_AP1_N.
DR   InterPro; IPR039913; RPAP1/Rba50.
DR   PANTHER; PTHR21483; PTHR21483; 1.
DR   Pfam; PF08620; RPAP1_C; 1.
DR   Pfam; PF08621; RPAP1_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; DNA-directed RNA polymerase; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription; Transferase.
FT   CHAIN           1..1400
FT                   /note="RNA polymerase II-associated protein 1"
FT                   /id="PRO_0000284843"
FT   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          60..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..54
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        518..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         329
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BWH6"
SQ   SEQUENCE   1400 AA;  154759 MW;  7E9A525448EBC6B3 CRC64;
     MMLSRPKPGE SEVDLLRFQS QFLEAGAAPA VQLVKGSRRR GDAHPDQLPP QDHRDVVMLD
     SLPDLPPALL PAPSKRARPS PGRPLPHDED PEERLNRHDE HITAVLSKIV ERDTSSVTVT
     LPVPSGVAFP PVFHRSQERQ VKPAASSKRS IFAQEIAARR VSDNRAPSAE QVVPSPDAPE
     GAVPCETPSS KDRGSQLPGR SHSFHRPNLI TGKGLRSQAA VQEVQTIHEE NVARLQAMDP
     EEILKEQQQL LAQLDPSLVA FLRAHNHTRE QTETKATKEQ NPERPSVPVS KEEPIMSTCT
     GESGTRDKLE DKLEDKLQPR TPALKLPMTP NKEWLHMDTV ELEKLHWTQD LPPLRRQQTQ
     ERMQARFSLQ GELLEPDVDL PTHLGLHHHG EEAERAGYSL QELFHLTRSQ VSQQRALALH
     VLSHIVGRAQ AGEFGDRLVG SVLRLLLDAG FLFLLRFSLD DRIDSVIAAA VRALRALLVA
     PGDEELLDST FSWYHGASVF PMMPSHDDKE DEDEDEELTK EKVNRKTPEE GSRPPPDLAR
     HDVIKGLLAT NLLPRFRYVL EVTCPGPSVV LDILAVLIRL ARHSLESAMR VLECPRLMET
     IVREFLPTSW SPIGVGPAPS LYKVPCAAAM KLLRVLASAG RNIAARLLSS FDVRSRLCRF
     IAEAPRDLAL PFEEAEILTT EAFRLWAVAA SYGQGGDLYR ELYPVLMRAL QTLPPELSTH
     PLQPLSMQRM ASLLTLLTQL TLAASTQPEA TSGSVESCVV AIPSSITWTH VSGLKPLVEP
     CLKQTLKFLR RPDVWNALGP VPSACLLFLG AYYQTWSQQS GLCPEDWLQD MERFLDEFLL
     PLLSQPPLGR MWDSLRDCSP LCNPLSCAST PEALPSLVSL GCAGGCPPLS VAGSASPFPF
     LTALLSLINT LGQIHKGLCR QLAVVLTAPG LQNYFLQCVA PAPAPQLTPF SAWALRHEYH
     LQYLVLSLAQ KAATSQPEPA ASTALHHVMA LVLLSRLLPG SEFLAHELLL SCVFRLGFLP
     ENASGGPEAA DFSDGLSLGN SGDPHCRRGA LLVQACQDLP SIRSCYLAHC SPARASLLTS
     QALYRGELPR VSSLLLPVPK EPLLPTDWPF QPLIHLYHRA SDTPSGLPAA DTVGITMRVL
     QWVLVLESWR PEALWAVPPA ARLARLMCVY LVDSELFRET PIQRLVAALL ARLCQPQVLP
     NLKLDCPLPG LTSFPDLYAS FLDHFEAVSF GDHLFGALVL LPLQRRFSVT LRLALFGEHV
     GVLRALGLPL AQLPVPLECY TEPAEDSLAL LQLYFRALVT GALHARWCPV LYTVAVAHVN
     SFVFCQDPKS SDEVKAARRS MLQKVWLLAD KDLRQHLLHY KLPNSSLPEG FELYPQLPRL
     RQQYLQTLPT EVLQNGGFKT