ID A0A161YK92_DAUCS Unreviewed; 418 AA.
AC A0A161YK92;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=E3 ubiquitin-protein ligase RMA {ECO:0000256|RuleBase:RU369090};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU369090};
DE AltName: Full=Protein RING membrane-anchor {ECO:0000256|RuleBase:RU369090};
DE AltName: Full=RING-type E3 ubiquitin transferase RMA {ECO:0000256|RuleBase:RU369090};
GN ORFNames=DCAR_017034 {ECO:0000313|EMBL:KZM93789.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM93789.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM93789.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM93789.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase. {ECO:0000256|RuleBase:RU369090}.
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:RU369090};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369090}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU369090}; Single-pass type IV membrane protein
CC {ECO:0000256|RuleBase:RU369090}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 ligase
CC activity. {ECO:0000256|RuleBase:RU369090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZM93789.1}.
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DR EMBL; LNRQ01000005; KZM93789.1; -; Genomic_DNA.
DR RefSeq; XP_017253396.1; XM_017397907.1.
DR AlphaFoldDB; A0A161YK92; -.
DR STRING; 79200.A0A161YK92; -.
DR EnsemblPlants; KZM93789; KZM93789; DCAR_017034.
DR GeneID; 108223586; -.
DR Gramene; KZM93789; KZM93789; DCAR_017034.
DR KEGG; dcr:108223586; -.
DR OMA; QRWRWRH; -.
DR OrthoDB; 901818at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000077755; Chromosome 5.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:EnsemblPlants.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd16745; RING-HC_AtRMA-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045103; RNF5/RNF185-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR PANTHER; PTHR12313:SF71; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU369090};
KW Membrane {ECO:0000256|RuleBase:RU369090};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU369090};
KW Reference proteome {ECO:0000313|Proteomes:UP000077755};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369090};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU369090};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 141..182
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 194..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 46928 MW; EA4504499362B285 CRC64;
MGDEMPNANT MNLDLNLGPV VNPDEEIGSG ESMNLEEWLG RPVNRLRETF MRQRASRPRA
GQRWRSVWRP VPIPPETRDL ALELMAGAGL EMGEGSVAPA ERPSEETKVC DTNNGYLENE
ALGKKDNDEK GNGEDGSFFD CNICLDLAKE PVVTCCGHLF CWPCLYRWLH LHSDAKECPI
CKGEVTMKNL TPIYGRGNNS KQEPEDESSL KIPQRPQARR VESWRQAFQR NAFTIPMEEM
IRRLGNRFDL SRDVAQGNPR NTGSPRVSPE RSNLLLNRFL TSRGMRREQN VGLPSEEAVD
LSQSSPTNSE VVESLRVLRR SHPHRAAVIS NFTSALSSAE RLVESYFRSH PAENVDDRDS
VSSIAAVIQS ESQTVDTAVE IDSRVSLSTS SSRRRHDASR ISDVDSGDSR APRRRRLN
//
