ID A0A1S3G7G0_DIPOR Unreviewed; 504 AA.
AC A0A1S3G7G0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Pre-mRNA-processing factor 19 {ECO:0000256|ARBA:ARBA00015618, ECO:0000256|RuleBase:RU367101};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483, ECO:0000256|RuleBase:RU367101};
GN Name=Prpf19 {ECO:0000313|RefSeq:XP_012884746.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012884746.1};
RN [1] {ECO:0000313|RefSeq:XP_012884746.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012884746.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU367101}.
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:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367101};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367101}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU367101}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642}.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family.
CC {ECO:0000256|ARBA:ARBA00006388, ECO:0000256|RuleBase:RU367101}.
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DR RefSeq; XP_012884746.1; XM_013029292.1.
DR AlphaFoldDB; A0A1S3G7G0; -.
DR STRING; 10020.ENSDORP00000006476; -.
DR GeneID; 105995541; -.
DR KEGG; dord:105995541; -.
DR CTD; 27339; -.
DR InParanoid; A0A1S3G7G0; -.
DR OMA; AHKTWEE; -.
DR OrthoDB; 130592at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005662; C:DNA replication factor A complex; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0000974; C:Prp19 complex; IEA:UniProtKB-UniRule.
DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl.
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:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IEA:Ensembl.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:Ensembl.
DR GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IEA:Ensembl.
DR CDD; cd16656; RING-Ubox_PRP19; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR013915; Pre-mRNA_splic_Prp19.
DR InterPro; IPR038959; Prp19.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43995; PRE-MRNA-PROCESSING FACTOR 19; 1.
DR PANTHER; PTHR43995:SF1; PRE-MRNA-PROCESSING FACTOR 19; 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; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 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; 3.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU367101};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU367101};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|RuleBase:RU367101};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU367101};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367101};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|RuleBase:RU367101};
KW Transferase {ECO:0000256|RuleBase:RU367101};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU367101};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 1..73
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REPEAT 260..301
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 353..387
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 388..429
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 471..504
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
SQ SEQUENCE 504 AA; 55195 MW; C2E19C3FA9F29A06 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 WSVPNTSCVQ
VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDEASG CSLTCAQFHP
DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF SENGYYLATA ADDSSVKLWD
LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL ALGGTDVQIY ICKQWTEILH FTEHSGLTTG
VAFGHHAKFI ASTGMDRSLK FYSL
//
