PRP19_CHICK
ID PRP19_CHICK Reviewed; 505 AA.
AC Q5ZMA2; P84167;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; ORFNames=RCJMB04_2m2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAG31141.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB {ECO:0000312|EMBL:CAG31141.1};
RC TISSUE=Bursa of Fabricius {ECO:0000312|EMBL:CAG31141.1};
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2] {ECO:0000305}
RP IDENTIFICATION, AND MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:16287166};
RX PubMed=16287166; DOI=10.1002/pmic.200402056;
RA Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J.,
RA Schneider J., Palomar M.A., Linares R.;
RT "Proteomic analysis of the Gallus gallus embryo at stage-29 of
RT development.";
RL Proteomics 5:4946-4957(2005).
CC -!- FUNCTION: Ubiquitin-protein ligase which is mainly involved pre-mRNA
CC splicing and DNA repair. Required for pre-mRNA splicing as component of
CC the spliceosome. Core component of the PRP19C/Prp19
CC complex/NTC/Nineteen complex which is part of the spliceosome and
CC participates in its assembly, its remodeling and is required for its
CC activity. {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. Component of the NTC complex (or PRP19-
CC associated complex) which is associated with the spliceosome. Interacts
CC with KHDC4 (By similarity). {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}.
CC -!- MASS SPECTROMETRY: Mass=55603; Mass_error=5; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16287166};
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
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DR EMBL; AJ719482; CAG31141.1; -; mRNA.
DR RefSeq; NP_001034420.2; NM_001039331.2.
DR AlphaFoldDB; Q5ZMA2; -.
DR SMR; Q5ZMA2; -.
DR STRING; 9031.ENSGALP00000022525; -.
DR GeneID; 430767; -.
DR KEGG; gga:430767; -.
DR CTD; 27339; -.
DR VEuPathDB; HostDB:geneid_430767; -.
DR eggNOG; KOG0289; Eukaryota.
DR InParanoid; Q5ZMA2; -.
DR OrthoDB; 1049599at2759; -.
DR PhylomeDB; Q5ZMA2; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5ZMA2; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; IEA:InterPro.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; DNA damage; DNA repair; Lipid droplet;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat;
KW Spliceosome; Transferase; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..505
FT /note="Pre-mRNA-processing factor 19"
FT /id="PRO_0000223504"
FT DOMAIN 1..73
FT /note="U-box"
FT REPEAT 220..260
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 263..302
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 305..346
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 349..388
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 391..430
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 434..473
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 474..505
FT /note="WD 7"
FT /evidence="ECO:0000255"
SQ SEQUENCE 505 AA; 55135 MW; 03C769FEA49D3649 CRC64;
MALICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PVNNQPLSEE QLIDIKVAHP
IRPRPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR QELSHALYQH DAACRVIARL
TKEVTAAREA LATLKPQAGL IVPQAVPSSQ PNVAGAGESM DLGELAGMTP EIIQKPQDKA
TVLTTERKKR GKTVPEELVE ARGAQQVPGR SPRMWGLHSA SIPGILALDL CPSDTNKILT
GGADKNVIVF DKSSEQILAT LKGHSKKVTS VVFHPSQDLV FSASPDATIR IWSVPNASCV
QVVRAHEGSV TGLSLHATGD YLLSSSDDQY WAFSDIQTGR VLTKVTDESS GCALTCAQFH
PDGLIFGTGT MDSQIKIWDL KERTNVANFP GHSGPITSIA FSENGYYLAT AADDSSVKLW
DLRKLKNFKT LQLDNNFEVK SLIFDQSGTY LALGGTDVQI YICKQWTEIL HFTEHSGLTT
GVAFGHHAKF IASTGMDRSL KFYSL