C3H41_ORYSJ
ID C3H41_ORYSJ Reviewed; 368 AA.
AC Q5ZA07; B7F5N8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=E3 ubiquitin-protein ligase makorin;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase makorin {ECO:0000305};
DE AltName: Full=Zinc finger CCCH domain-containing protein 41;
DE Short=OsC3H41;
GN Name=MKRN; OrderedLocusNames=Os06g0318700, LOC_Os06g21390;
GN ORFNames=OsJ_21146 {ECO:0000312|EMBL:EEE65606.1}, P0468A12.33, P0592B08.7;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17870591; DOI=10.1016/j.plaphy.2007.07.006;
RA Arumugam T.U., Davies E., Morita E.H., Abe S.;
RT "Sequence, expression and tissue localization of a gene encoding a makorin
RT RING zinc-finger protein in germinating rice (Oryza sativa L. ssp.
RT Japonica) seeds.";
RL Plant Physiol. Biochem. 45:767-780(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP NOMENCLATURE.
RX PubMed=18221561; DOI=10.1186/1471-2164-9-44;
RA Wang D., Guo Y., Wu C., Yang G., Li Y., Zheng C.;
RT "Genome-wide analysis of CCCH zinc finger family in Arabidopsis and rice.";
RL BMC Genomics 9:44-44(2008).
CC -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment of
CC ubiquitin moieties onto substrate proteins. {ECO:0000250}.
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:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- TISSUE SPECIFICITY: Expressed in primary roots and leaves. Detected in
CC vascular bundle tissues. {ECO:0000269|PubMed:17870591}.
CC -!- DEVELOPMENTAL STAGE: Expressed in dry seeds. Increased expression
CC throughout imbibition and germination and when radicle and shoots are
CC emerging. Up-regulated during cell differentiation.
CC {ECO:0000269|PubMed:17870591}.
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DR EMBL; AP003507; BAD61579.1; -; Genomic_DNA.
DR EMBL; AP003543; BAD61603.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF19419.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS97489.1; -; Genomic_DNA.
DR EMBL; CM000143; EEE65606.1; -; Genomic_DNA.
DR EMBL; AK120250; BAG99935.1; -; mRNA.
DR RefSeq; XP_015643585.1; XM_015788099.1.
DR AlphaFoldDB; Q5ZA07; -.
DR STRING; 4530.OS06T0318700-01; -.
DR PaxDb; Q5ZA07; -.
DR PRIDE; Q5ZA07; -.
DR EnsemblPlants; Os06t0318700-01; Os06t0318700-01; Os06g0318700.
DR GeneID; 4340884; -.
DR Gramene; Os06t0318700-01; Os06t0318700-01; Os06g0318700.
DR KEGG; osa:4340884; -.
DR eggNOG; KOG1039; Eukaryota.
DR HOGENOM; CLU_040815_1_0_1; -.
DR InParanoid; Q5ZA07; -.
DR OMA; RYDHIRL; -.
DR OrthoDB; 1388677at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; Q5ZA07; OS.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0044260; P:cellular macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11224; PTHR11224; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Metal-binding; Reference proteome; Repeat; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..368
FT /note="E3 ubiquitin-protein ligase makorin"
FT /id="PRO_0000346835"
FT ZN_FING 2..29
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 30..57
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 147..174
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 216..274
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 303..332
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 58..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..202
FT /note="Makorin-type Cys-His"
FT COMPBIAS 62..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 368 AA; 41673 MW; 3AA74380BB12BFB7 CRC64;
MSTKRVLCKF FMHGACLKGE YCEFSHDWND QPNNVCTFYQ KGSCSYGSRC RYDHVKVSRN
PTVAPPPSSS TTTRASSSLQ PLSFGRPHHV GYQADSSNPR QQISMDVLAH SGSKPVWRND
FQHESVLEDG IDWSISPTVQ NQTTLSPADL PICSFAAGGN CPYGEECPQM HGDLCTTCGK
MCLHPYRPDE REEHTKLCEK NHKRLESLKR SQEIECSVCL DRVLSKPTAA ERKFGLLSEC
DHPFCISCIR NWRNNSPTSG MDVNSALRAC PICRKLSYYV IPSVLWYFSK EEKLEIIDNY
KAKLKSIDCK YFDFGTGTCP FGSSCFYKHA YRDGRLEEVI LRHLDADDGS TVIAKNIRLS
DFLSRLHL
