PRP19_BOVIN
ID PRP19_BOVIN Reviewed; 504 AA.
AC Q08E38;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9UMS4};
DE AltName: Full=PRP19/PSO4 homolog;
DE AltName: Full=RING-type E3 ubiquitin transferase PRP19 {ECO:0000305};
GN Name=PRPF19;
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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-protein ligase which is a core component of several
CC complexes mainly involved pre-mRNA splicing and DNA repair. Required
CC for pre-mRNA splicing as component of the spliceosome (By similarity).
CC Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which
CC is part of the spliceosome and participates in its assembly, its
CC remodeling and is required for its activity. During assembly of the
CC spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4
CC spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its
CC recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-
CC snRNP spliceosomal complex. Recruited to RNA polymerase II C-terminal
CC domain (CTD) and the pre-mRNA, it may also couple the transcriptional
CC and spliceosomal machineries. The XAB2 complex, which contains PRPF19,
CC is also involved in pre-mRNA splicing, transcription and transcription-
CC coupled repair. Beside its role in pre-mRNA splicing PRPF19, as part of
CC the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR.
CC It is recruited to the sites of DNA damage by the RPA complex where
CC PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked
CC polyubiquitination of the RPA complex allows the recruitment of the
CC ATR-ATRIP complex and the activation of ATR, a master regulator of the
CC DNA damage response. May also play a role in DNA double-strand break
CC (DSB) repair by recruiting the repair factor SETMAR to altered DNA. As
CC part of the PSO4 complex may also be involved in the DNA interstrand
CC cross-links/ICLs repair process. In addition, may also mediate 'Lys-
CC 48'-linked polyubiquitination of substrates and play a role in
CC proteasomal degradation (By similarity). May play a role in the
CC biogenesis of lipid droplets (By similarity). May play a role in neural
CC differentiation possibly through its function as part of the
CC spliceosome (By similarity). {ECO:0000250|UniProtKB:Q99KP6,
CC ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q9UMS4};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- SUBUNIT: Homotetramer. Component of activated, catalytic and post-
CC catalytic spliceosomes (By similarity). Component of the Prp19
CC complex/PRP19C/Nineteen complex/NTC and related complexes described as
CC PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of
CC PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes.
CC The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core
CC complex. At least three less stably associated proteins CTNNBL1, CWC15
CC and HSPA8 are found in the Prp19 complex. The Prp19 complex associates
CC with the spliceosome during its assembly and remodeling recruiting
CC additional proteins. Component of the XAB2 complex, a multimeric
CC protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE.
CC Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Interacts
CC with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites
CC of DNA repair where it interacts with the replication protein A complex
CC (RPA). Interacts with SETMAR; required for SETMAR recruitment to site
CC of DNA damage. Interacts with U2AF2; the interaction is direct and
CC recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD)
CC and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and
CC PSMB4. Interacts with PSMC5 (By similarity). Interacts with KNSTRN (By
CC similarity). Interacts (via N-terminus) with CDC5L (By similarity).
CC Interacts with KHDC4 (By similarity). Interacts with USB1 (By
CC similarity). {ECO:0000250|UniProtKB:Q99KP6,
CC ECO:0000250|UniProtKB:Q9JMJ4, ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMS4}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q9UMS4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UMS4}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q9UMS4}. Note=Nucleoplasmic in interphase cells.
CC Irregularly distributed in anaphase cells. In prophase cells, uniformly
CC distributed, but not associated with condensing chromosomes. Found in
CC extrachromosomal regions in metaphase cells. Mainly localized to the
CC mitotic spindle apparatus when chromosomes segregate during anaphase.
CC When nuclei reform during late telophase, uniformly distributed in
CC daughter cells and displays no preferred association with decondensing
CC chromatin. Recruited on damaged DNA at sites of double-strand break.
CC {ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- DOMAIN: The 7 WD repeats are necessary and sufficient to support
CC interaction with the RPA complex. {ECO:0000250|UniProtKB:Q9UMS4}.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
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DR EMBL; BC123437; AAI23438.1; -; mRNA.
DR RefSeq; NP_001069108.1; NM_001075640.1.
DR AlphaFoldDB; Q08E38; -.
DR SMR; Q08E38; -.
DR STRING; 9913.ENSBTAP00000019100; -.
DR PaxDb; Q08E38; -.
DR PRIDE; Q08E38; -.
DR Ensembl; ENSBTAT00000019100; ENSBTAP00000019100; ENSBTAG00000014366.
DR GeneID; 513868; -.
DR KEGG; bta:513868; -.
DR CTD; 27339; -.
DR VEuPathDB; HostDB:ENSBTAG00000014366; -.
DR VGNC; VGNC:33372; PRPF19.
DR eggNOG; KOG0289; Eukaryota.
DR GeneTree; ENSGT00940000153662; -.
DR HOGENOM; CLU_023894_1_1_1; -.
DR InParanoid; Q08E38; -.
DR OMA; VTRVIYH; -.
DR OrthoDB; 1049599at2759; -.
DR TreeFam; TF105919; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000014366; Expressed in diaphragm and 104 other tissues.
DR ExpressionAtlas; Q08E38; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005662; C:DNA replication factor A complex; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:Ensembl.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR InterPro; IPR038959; Prp19.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43995; PTHR43995; 1.
DR Pfam; PF08606; Prp19; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW Lipid droplet; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Repeat; Spliceosome; Transferase; Ubl conjugation pathway; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT CHAIN 2..504
FT /note="Pre-mRNA-processing factor 19"
FT /id="PRO_0000329313"
FT DOMAIN 2..73
FT /note="U-box"
FT REPEAT 219..259
FT /note="WD 1"
FT REPEAT 262..301
FT /note="WD 2"
FT REPEAT 304..345
FT /note="WD 3"
FT REPEAT 348..387
FT /note="WD 4"
FT REPEAT 390..429
FT /note="WD 5"
FT REPEAT 433..472
FT /note="WD 6"
FT REPEAT 473..503
FT /note="WD 7"
FT REGION 68..223
FT /note="May mediate interaction with PSMC5"
FT /evidence="ECO:0000250|UniProtKB:Q99KP6"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT MOD_RES 122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KP6"
FT MOD_RES 244
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KP6"
FT MOD_RES 261
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UMS4"
SQ SEQUENCE 504 AA; 55195 MW; A79F7A7DD06BE48C CRC64;
MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE QLIDIKVAHP
IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR QELSHALYQH DAACRVIARL
TKEVTAAREA LATLKPQAGL IVPQAVPSSQ PSVVGAGEPM DLGELVGMTP EIIQKLQDKA
TVLTTERKKR GKTVPEELVK PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG
GADKNVVVFD KSSEQILATL KGHTKKVTSV VFHPSQELVF SASPDATIRI WSVPNASCVQ
VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG CSLTCAQFHP
DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF SENGYYLATA ADDSSVKLWD
LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL ALGGTDVQIY ICKQWTEILH FTEHSGLTTG
VAFGHHAKFI ASTGMDRSLK FYSL
