RPAP3_RAT
ID RPAP3_RAT Reviewed; 659 AA.
AC Q68FQ7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=RNA polymerase II-associated protein 3;
GN Name=Rpap3;
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=Testis;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP 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 {ECO:0000250|UniProtKB:Q9H6T3}.
CC -!- SUBUNIT: Tightly associated with the RNA polymerase II complex (By
CC similarity). Component of the R2TP complex composed at least of RUVBL1,
CC RUVBL2, RPAP3 and PIHD1 (By similarity). Component of the PAQosome
CC complex which is responsible for the biogenesis of several protein
CC complexes and which consists of R2TP complex members RUVBL1, RUVBL2,
CC RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1
CC as well as ASDURF, POLR2E and DNAAF10/WDR92 (By similarity). Interacts
CC with PIH1D1 (By similarity). Interacts with TSC1 and TSC2 (By
CC similarity). Interacts with PRPF8 and EFTUD2 in a ZNHIT2-dependent
CC manner (By similarity). {ECO:0000250|UniProtKB:Q9H6T3}.
CC -!- SIMILARITY: Belongs to the RPAP3 family. {ECO:0000305}.
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DR EMBL; BC079414; AAH79414.1; -; mRNA.
DR RefSeq; NP_001004243.1; NM_001004243.1.
DR RefSeq; XP_008763912.1; XM_008765690.2.
DR RefSeq; XP_017450273.1; XM_017594784.1.
DR RefSeq; XP_017450274.1; XM_017594785.1.
DR AlphaFoldDB; Q68FQ7; -.
DR SMR; Q68FQ7; -.
DR BioGRID; 256480; 1.
DR IntAct; Q68FQ7; 1.
DR MINT; Q68FQ7; -.
DR iPTMnet; Q68FQ7; -.
DR PhosphoSitePlus; Q68FQ7; -.
DR jPOST; Q68FQ7; -.
DR PRIDE; Q68FQ7; -.
DR GeneID; 300189; -.
DR KEGG; rno:300189; -.
DR UCSC; RGD:1303036; rat.
DR CTD; 79657; -.
DR RGD; 1303036; Rpap3.
DR VEuPathDB; HostDB:ENSRNOG00000053405; -.
DR eggNOG; KOG4648; Eukaryota.
DR HOGENOM; CLU_023272_1_0_1; -.
DR InParanoid; Q68FQ7; -.
DR OMA; GTAQFHV; -.
DR OrthoDB; 1617844at2759; -.
DR PRO; PR:Q68FQ7; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000053405; Expressed in cerebellum and 20 other tissues.
DR Genevisible; Q68FQ7; RN.
DR GO; GO:0101031; C:chaperone complex; IBA:GO_Central.
DR GO; GO:0097255; C:R2TP complex; ISO:RGD.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:RGD.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR025986; RPAP3-like_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF13877; RPAP3_C; 1.
DR Pfam; PF00515; TPR_1; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 5.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT CHAIN 2..659
FT /note="RNA polymerase II-associated protein 3"
FT /id="PRO_0000302796"
FT REPEAT 8..41
FT /note="TPR 1"
FT REPEAT 133..166
FT /note="TPR 2"
FT REPEAT 168..200
FT /note="TPR 3"
FT REPEAT 201..234
FT /note="TPR 4"
FT REPEAT 282..315
FT /note="TPR 5"
FT REPEAT 317..349
FT /note="TPR 6"
FT REPEAT 350..383
FT /note="TPR 7"
FT REGION 39..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H6T3"
SQ SEQUENCE 659 AA; 74645 MW; 519D6C55825593B0 CRC64;
MTSTSKAVEL QLQVKHNAEE LQDFMRDLEH WEKTMRQKDL ELRRQSGVPE ENLPPIRNGS
FRKKKKRKTK DSSKKTKEEN TKNRIKSFDY DAWAKLDVDS ILDELDKEDS THDSVSQESE
SDEDGVRVDS QKALVLKEKG NKYFKQGKYD EAIECYTKGM DADPYNPVLP TNRASAYFRL
KKFAVAESDC NLAIALSRSY TKAYARRGAA RFALQKLEDA RKDYVKVLEL EPDNFEATNE
LRKIDQALTS KENSHPKDIA AVIKPAEGER KANEDQRGRQ KAIAEKDLGN GFFKEGKYEQ
AIECYTRGIA ADSTNALLPA NRAMAYLKVQ KYEEAERDCT QAILLDGSYS KAFARRGTAR
TFLGKINEAK QDFETVLLLE PGNKQAVTEL SRIKKELIEK GRWDDVFLDS TQRHNVVKPV
DSPHRGSPKA LKKVFIEETG NLIESVDAPE SSATVPESDR AAVAVDTGRK KDFSQGDSVS
SGETPRAKVL KIEAVGDSSA PQAQVDVKQG VRQSVSEKTS VRVAQTPGQL AAVVLPPVPA
NSFQLESDFR QLRSSPEMLY QYVKKIEPSL YPKLFQKNLD PDVFNQIIKI LHDFYVEREK
PALIFEVLER LSQLRRFDMA VMFMSGTERE LTKVLFNHLE KSELKEDSVE ELKKRYGGG
