PR19B_ARATH
ID PR19B_ARATH Reviewed; 525 AA.
AC O22785; C1KE07; Q3EBP5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 3.
DT 25-MAY-2022, entry version 164.
DE RecName: Full=Pre-mRNA-processing factor 19 homolog 2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:18393940};
DE AltName: Full=MOS4-associated complex protein 3B;
DE Short=MAC protein 3B;
DE AltName: Full=Plant U-box protein 60;
DE AltName: Full=RING-type E3 ubiquitin transferase PRP19 2 {ECO:0000305};
DE AltName: Full=U-box domain-containing protein 60;
GN Name=PRP19B; Synonyms=MAC3B, PUB60; OrderedLocusNames=At2g33340;
GN ORFNames=F4P9.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION,
RP SUBCELLULAR LOCATION, AND COMPONENT OF THE MAC COMPLEX.
RC STRAIN=cv. Columbia;
RX PubMed=19629177; DOI=10.1371/journal.ppat.1000526;
RA Monaghan J., Xu F., Gao M., Zhao Q., Palma K., Long C., Chen S., Zhang Y.,
RA Li X.;
RT "Two Prp19-like U-box proteins in the MOS4-associated complex play
RT redundant roles in plant innate immunity.";
RL PLoS Pathog. 5:E1000526-E1000526(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18393940; DOI=10.1042/bj20071568;
RA Wiborg J., O'Shea C., Skriver K.;
RT "Biochemical function of typical and variant Arabidopsis thaliana U-box E3
RT ubiquitin-protein ligases.";
RL Biochem. J. 413:447-457(2008).
RN [6]
RP DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
CC -!- FUNCTION: Probable ubiquitin-protein ligase which is mainly involved
CC pre-mRNA splicing and DNA repair (By similarity). Component of the MAC
CC complex that probably regulates defense responses through
CC transcriptional control and thereby is essential for plant innate
CC immunity. {ECO:0000250|UniProtKB:Q9UMS4, ECO:0000269|PubMed:18393940,
CC ECO:0000269|PubMed:19629177}.
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:0000269|PubMed:18393940};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:18393940}.
CC -!- SUBUNIT: Homotetramer. Component of the multiprotein assembly MOS4-
CC associated complex (MAC) at least composed of MOS4, CDC5, PRL1 and
CC PRP19 which is related to the PRP19C/Prp19 complex/NTC/Nineteen complex
CC identified in other organisms. Associated with the spliceosome.
CC {ECO:0000250|UniProtKB:P32523, ECO:0000250|UniProtKB:Q9UMS4,
CC ECO:0000269|PubMed:19629177}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19629177}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O22785-1; Sequence=Displayed;
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat PRP19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB80652.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AY080868; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; FJ820118; ACO38702.1; -; mRNA.
DR EMBL; AC002332; AAB80652.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC08817.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08818.1; -; Genomic_DNA.
DR EMBL; AY080868; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; C84744; C84744.
DR RefSeq; NP_850206.4; NM_179875.7. [O22785-1]
DR RefSeq; NP_850207.4; NM_179876.5. [O22785-1]
DR AlphaFoldDB; O22785; -.
DR SMR; O22785; -.
DR BioGRID; 3244; 40.
DR IntAct; O22785; 3.
DR STRING; 3702.AT2G33340.1; -.
DR iPTMnet; O22785; -.
DR PaxDb; O22785; -.
DR PRIDE; O22785; -.
DR ProteomicsDB; 234842; -. [O22785-1]
DR EnsemblPlants; AT2G33340.1; AT2G33340.1; AT2G33340. [O22785-1]
DR EnsemblPlants; AT2G33340.2; AT2G33340.2; AT2G33340. [O22785-1]
DR GeneID; 817897; -.
DR Gramene; AT2G33340.1; AT2G33340.1; AT2G33340. [O22785-1]
DR Gramene; AT2G33340.2; AT2G33340.2; AT2G33340. [O22785-1]
DR KEGG; ath:AT2G33340; -.
DR Araport; AT2G33340; -.
DR TAIR; locus:2051094; AT2G33340.
DR eggNOG; KOG0289; Eukaryota.
DR HOGENOM; CLU_023894_1_0_1; -.
DR InParanoid; O22785; -.
DR OMA; GAKRMRH; -.
DR OrthoDB; 1049599at2759; -.
DR PhylomeDB; O22785; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O22785; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22785; baseline and differential.
DR Genevisible; O22785; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000974; C:Prp19 complex; IBA:GO_Central.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IBA:GO_Central.
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:0042742; P:defense response to bacterium; IGI:TAIR.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
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; IPR001680; WD40_repeat.
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; PF00400; WD40; 4.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; Immunity; Innate immunity;
KW mRNA processing; mRNA splicing; Nucleus; Plant defense; Reference proteome;
KW Repeat; Spliceosome; Transferase; Ubl conjugation pathway; WD repeat.
FT CHAIN 1..525
FT /note="Pre-mRNA-processing factor 19 homolog 2"
FT /id="PRO_0000322138"
FT DOMAIN 1..70
FT /note="U-box"
FT REPEAT 220..261
FT /note="WD 1"
FT REPEAT 262..301
FT /note="WD 2"
FT REPEAT 307..346
FT /note="WD 3"
FT REPEAT 351..390
FT /note="WD 4"
FT REPEAT 393..431
FT /note="WD 5"
FT REPEAT 433..469
FT /note="WD 6"
FT REPEAT 478..517
FT /note="WD 7"
FT MOTIF 409..424
FT /note="DWD box"
SQ SEQUENCE 525 AA; 56728 MW; 9994B7554B2DA2C2 CRC64;
MNCAISGEVP VEPVVSTKSG LLFERRLIER HISDYGKCPV TGEPLTIDDI VPIKTGEIIK
PKTLHTASIP GLLGTFQNEW DGLMLSNFAL EQQLHTARQE LSHALYQHDS ACRVIARLKK
ERDEARQLLA EVERHIPAAP EAVTANAALS NGKRAAVDEE LGPDAKKLCP GISAEIITEL
TDCNAALSQK RKKRQIPQTL ASIDTLERFT QLSSHPLHKT NKPGICSMDI LHSKDVIATG
GVDATAVLFD RPSGQILSTL TGHSKKVTSV KFVGDSDLVL TASADKTVRI WRNPGDGNYA
CGYTLNDHSA EVRAVTVHPT NKYFVSASLD GTWCFYDLSS GSCLAQVSDD SKNVDYTAAA
FHPDGLILGT GTSQSVVKIW DVKSQANVAK FDGHTGEVTA ISFSENGYFL ATAAEDGVRL
WDLRKLRNFK SFLSADANSV EFDPSGSYLG IAASDIKVYQ TASVKAEWNL IKTLPDLSGT
GKATCVKFGS DAQYVAVGSM DRNLRIFGLP GDEKANVDDD SAQDS
