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Database: UniProt
Entry: RPAP3_RAT
LinkDB: RPAP3_RAT
Original site: 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   24-JAN-2024, entry version 119.
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   STRING; 10116.ENSRNOP00000074251; -.
DR   iPTMnet; Q68FQ7; -.
DR   PhosphoSitePlus; Q68FQ7; -.
DR   jPOST; Q68FQ7; -.
DR   GeneID; 300189; -.
DR   KEGG; rno:300189; -.
DR   UCSC; RGD:1303036; rat.
DR   AGR; RGD:1303036; -.
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   OrthoDB; 2294768at2759; -.
DR   PRO; PR:Q68FQ7; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000053405; Expressed in cerebellum and 20 other cell types or tissues.
DR   Genevisible; Q68FQ7; RN.
DR   GO; GO:0101031; C:protein folding 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; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR025986; RPAP3-like_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46423; RNA POLYMERASE II-ASSOCIATED PROTEIN 3; 1.
DR   PANTHER; PTHR46423:SF1; RNA POLYMERASE II-ASSOCIATED PROTEIN 3; 1.
DR   Pfam; PF13877; RPAP3_C; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; TPR-like; 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
//
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