RPAP1_BOVIN
ID RPAP1_BOVIN Reviewed; 1395 AA.
AC A0JN53;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=RNA polymerase II-associated protein 1;
GN Name=RPAP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC126520; AAI26521.1; -; mRNA.
DR RefSeq; NP_001071452.1; NM_001077984.2.
DR RefSeq; XP_005211635.1; XM_005211578.3.
DR RefSeq; XP_005211636.1; XM_005211579.2.
DR RefSeq; XP_005211637.1; XM_005211580.3.
DR AlphaFoldDB; A0JN53; -.
DR SMR; A0JN53; -.
DR STRING; 9913.ENSBTAP00000002220; -.
DR PaxDb; A0JN53; -.
DR PRIDE; A0JN53; -.
DR Ensembl; ENSBTAT00000081849; ENSBTAP00000071505; ENSBTAG00000001693.
DR GeneID; 531362; -.
DR KEGG; bta:531362; -.
DR CTD; 26015; -.
DR VEuPathDB; HostDB:ENSBTAG00000001693; -.
DR VGNC; VGNC:34098; RPAP1.
DR eggNOG; KOG1894; Eukaryota.
DR eggNOG; KOG4732; Eukaryota.
DR GeneTree; ENSGT00390000007594; -.
DR HOGENOM; CLU_005296_1_0_1; -.
DR InParanoid; A0JN53; -.
DR OMA; RMDKAPK; -.
DR OrthoDB; 25908at2759; -.
DR TreeFam; TF324391; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000001693; Expressed in choroid plexus and 104 other tissues.
DR ExpressionAtlas; A0JN53; baseline and differential.
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; 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.
PE 2: Evidence at transcript level;
KW DNA-binding; DNA-directed RNA polymerase; Nucleotidyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription; Transferase.
FT CHAIN 1..1395
FT /note="RNA polymerase II-associated protein 1"
FT /id="PRO_0000284840"
FT REGION 34..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..530
FT /note="Disordered"
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..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 321
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWH6"
SQ SEQUENCE 1395 AA; 152859 MW; 91236BA09B55F13A CRC64;
MLSRPKPGES EVDLLRFQSQ FLAAGATPAV QLVKKGSRRA GDANLEQPPL QDHRDVVMLD
SLPDLPPALV PAPPKRARPS PGHLLPEHED PEERLHRHDQ HITAVLTKII ERDTSSMPVN
LPVSSGVAFP PVFHRSQGRQ GKPVTAGKRS IFAQEIAARR ASGAKVSPVR EVESILDPPE
SAMTCEALTP REWGSQPPWN SYSFQGPHLV TGKGLKGQEA EQEAQTIHEE NVARLQALAP
EEILQEQQRL LAQLDPSLVA FLKSHSCTRE QAEEKATREQ RPGRPSAEVI GKEAIAPTSA
SVPRQENELE PETPALALPV TPQKEWLHMD TVELEKLHWT QDLPPLRRQQ TQERMQARFS
LQGELLAPDM DLPTHLGLHH HGEEAERAGY SLQELFHLTR SQVSQQRALA LHVLAQVIGR
AQAGEFGDRL VGSVLHLLLD AGFLFLLRFS LDDRVDGVIA AAVRALRALL VAPGDEELLD
STFSWYHGAL MFALMPSQED KEDEDEDEEP PAEKAKTKSP EEGNRPPSDL ARHDIIKGLL
ATNLLPRLRY VLEVTCPGPS VVLDILTVLI RLARHSLESA TRVLECPRLV ETVVREFLPT
SWSPMGSGPT SSLHRVPCAP AMKLLRVLAS ASRNIAARLL SGFDLRSRLS RFIAEDPQDL
ALPLEEAETL STEAFRLWAV AASYGLGSDL YRELYPVLMQ ALQDVPKELS SPPPRPLAVQ
RIASLLTLLT QLTLAAGHIA PEHNSHSAEA SLLAGSSSVT WTQVSGLQPL VEPCLRQTLK
LLPRPEMWSA LGPVPTACLL FLDAYYQAWS QQPGLCPEDW LQDMERLSEG LLLPLLKHPS
LGSLWDSLGC CSPLCNPQSC AVAPETISSL ASLGCAGGHP PLSLAGSASP FPFLTALLSL
LNTLGRIHKG LCGQLATVLA APGLQDYFLR CVAPVAALHL TPFSAWALRH EYHLQYLALT
LAQRAATLQP PMSGTDAALC HGMALALLGR LLPGSEHLAH ELMLSCVFRL EFLPERASGG
PEAADFSDRL SLGSGGDLGC GRGALLAQAC QDLPSIRSCY LTHCSLARAS LLASQALYRG
ELQRVPALLL PVPKEPLLPT DWPFLPLIQL YHRASDTPSG LPPADTVGTA LRALQWVLVL
ESWRPRALWA VSPAARLARL MCVFLVDSEL FRETPIQRLV AALLARLCQP EVLSNLNLDC
PLPGLTSFPD LYANFLEHFE AVSFGDHLFG ALILLPLQRR FSVTLRLALF GEHVGALRAL
GLPLTQLPVS LECYTAPPED NLALLQLYFR ALVTGALRPR WCPVLYAVAV AHVNSFIFSQ
DPNNSDEIKA ACRSMLQKTW LLTDEGLRQH LLHYKLPNSA LPEGFELYPQ LPPLRQQYLQ
KLRISGVLPN GVSDT
