ID PRP6_RAT Reviewed; 941 AA.
AC A1A5S1;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=Pre-mRNA-processing factor 6;
DE AltName: Full=PRP6 homolog;
DE AltName: Full=U5 snRNP-associated 102 kDa protein;
DE Short=U5-102 kDa protein;
GN Name=Prpf6;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway; TISSUE=Heart;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, 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: Involved in pre-mRNA splicing as component of the U4/U6-U5
CC tri-snRNP complex, one of the building blocks of the spliceosome.
CC Enhances dihydrotestosterone-induced transactivation activity of AR, as
CC well as dexamethasone-induced transactivation activity of NR3C1, but
CC does not affect estrogen-induced transactivation.
CC {ECO:0000250|UniProtKB:O94906}.
CC -!- SUBUNIT: Identified in the spliceosome B complex. Identified in the
CC spliceosome C complex. Associates with the U5 snRNP particle. Component
CC of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs
CC and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A,
CC SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39, LSm
CC proteins LSm2-8 and Sm proteins. Interacts with ARAF1. Interacts with
CC AR and NR3C1, but not ESR1, independently of the presence of hormones.
CC Interacts with USH1G. {ECO:0000250|UniProtKB:O94906}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:O94906}. Nucleus speckle
CC {ECO:0000250|UniProtKB:O94906}. Note=Localized in splicing speckles.
CC {ECO:0000250|UniProtKB:O94906}.
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DR EMBL; CH474066; EDL88695.1; -; Genomic_DNA.
DR EMBL; BC128779; AAI28780.1; -; mRNA.
DR RefSeq; NP_001073234.1; NM_001079766.1.
DR AlphaFoldDB; A1A5S1; -.
DR SMR; A1A5S1; -.
DR BioGRID; 265839; 2.
DR STRING; 10116.ENSRNOP00000073536; -.
DR iPTMnet; A1A5S1; -.
DR PhosphoSitePlus; A1A5S1; -.
DR jPOST; A1A5S1; -.
DR PaxDb; 10116-ENSRNOP00000021723; -.
DR PeptideAtlas; A1A5S1; -.
DR Ensembl; ENSRNOT00000083423.2; ENSRNOP00000073536.1; ENSRNOG00000051498.2.
DR Ensembl; ENSRNOT00055002264; ENSRNOP00055001749; ENSRNOG00055001387.
DR Ensembl; ENSRNOT00060002475; ENSRNOP00060001602; ENSRNOG00060001630.
DR Ensembl; ENSRNOT00065024191; ENSRNOP00065018880; ENSRNOG00065014637.
DR GeneID; 366276; -.
DR KEGG; rno:366276; -.
DR UCSC; RGD:1307103; rat.
DR AGR; RGD:1307103; -.
DR CTD; 24148; -.
DR RGD; 1307103; Prpf6.
DR eggNOG; KOG0495; Eukaryota.
DR GeneTree; ENSGT00550000075016; -.
DR HOGENOM; CLU_007010_0_0_1; -.
DR InParanoid; A1A5S1; -.
DR OrthoDB; 655233at2759; -.
DR PhylomeDB; A1A5S1; -.
DR TreeFam; TF105743; -.
DR Reactome; R-RNO-72165; mRNA Splicing - Minor Pathway.
DR PRO; PR:A1A5S1; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000051498; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR Genevisible; A1A5S1; RN.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; ISO:RGD.
DR GO; GO:0005682; C:U5 snRNP; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; ISO:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006403; P:RNA localization; ISO:RGD.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISO:RGD.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR010491; PRP1_N.
DR InterPro; IPR045075; Syf1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR11246; PRE-MRNA SPLICING FACTOR; 1.
DR PANTHER; PTHR11246:SF1; PRE-MRNA-PROCESSING FACTOR 6; 1.
DR Pfam; PF06424; PRP1_N; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SMART; SM00386; HAT; 13.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Spliceosome.
FT CHAIN 1..941
FT /note="Pre-mRNA-processing factor 6"
FT /id="PRO_0000413096"
FT REPEAT 384..416
FT /note="HAT 1"
FT REPEAT 418..444
FT /note="HAT 2"
FT REPEAT 445..476
FT /note="HAT 3"
FT REPEAT 554..586
FT /note="HAT 4"
FT REPEAT 588..620
FT /note="HAT 5"
FT REPEAT 622..654
FT /note="HAT 6"
FT REPEAT 689..721
FT /note="HAT 7"
FT REPEAT 723..755
FT /note="HAT 8"
FT REPEAT 855..887
FT /note="HAT 9"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94906"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94906"
FT MOD_RES 275
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O94906"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94906"
SQ SEQUENCE 941 AA; 106764 MW; 12F1405BD6433254 CRC64;
MNKKKKPFLG MPAPLGYVPG LGRGATGFTT RSDIGPARDA NDPVDDRHAP PGKRTVGDQM
KKNQAADDDD EDLNDTNYDE FNGYAGSLFS SGPYEKDDEE ADAIYAALDK RMDERRKERR
EQREKEEIEK YRMERPKIQQ QFSDLKRKLA EVTEEEWLSI PEVGDARNKR QRNPRYEKLT
PVPDSFFAKH LQTGENHTSV DPRQTQFGGL NTPYPGGLNT PYPGGMTPGL MTPGTGELDM
RKIGQARNTL MDMRLSQVSD SVSGQTVVDP KGYLTDLNSM IPTHGGDIND IKKARLLLKS
VRETNPHHPP AWIASARLEE VTGKLQVARN LIMKGTEMCP KSEDVWLEAA RLQPGDTAKA
VVAQAVRHLP QSVRIYIRAA ELETDIRAKK RVLRKALEHV PNSVRLWKAA VELEEPEDAR
IMLSRAVECC PTSVELWLAL ARLETYENAR KVLNKARENI PTDRHIWITA AKLEEANGNT
QMVEKIIDRA ITSLRANGVE INREQWIQDA EECDRAGSVA TCQAVMRAVI GIGIEEEDRK
HTWMEDADSC VAHNALECAR AIYAYALQVF PSKKSVWLRA AYFEKNHGTR ESLEALLQRA
VAHCPKAEVL WLMGAKSKWL AGDVPAARSI LALAFQANPN SEEIWLAAVK LESENNEYER
ARRLLAKARS SAPTARVFMK SVKLEWVLGN ITAAQELCEE ALRHYEDFPK LWMMKGQIEE
QGELMERARE AYNQGLKKCP HSTPLWLLLS RLEEKIGQLT RARAILEKSR LKNPKNPGLW
LESVRLEYRA GLKNIANTLM AKALQECPNS GILWSEAVFL EARPQRKTKS VDALKKCEHD
PHVLLAVAKL FWSERKITKA REWFHRTVKI DSDLGDAWAF FYKFELQHGT EEQQEEVRKR
CENAEPRHGE LWCAVSKDIT NWQRKIGEIL VLVAARIKNT F
//
