ID M1B9U5_SOLTU Unreviewed; 408 AA.
AC M1B9U5;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
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};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040399, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400040399}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400040399};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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}.
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DR AlphaFoldDB; M1B9U5; -.
DR STRING; 4113.M1B9U5; -.
DR PaxDb; 4113-PGSC0003DMT400040399; -.
DR EnsemblPlants; PGSC0003DMT400040399; PGSC0003DMT400040399; PGSC0003DMG400015643.
DR Gramene; PGSC0003DMT400040399; PGSC0003DMT400040399; PGSC0003DMG400015643.
DR eggNOG; KOG0823; Eukaryota.
DR InParanoid; M1B9U5; -.
DR OMA; TPIYGNA; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; M1B9U5; baseline.
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; IBA:GO_Central.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 PANTHER; PTHR12313:SF79; E3 UBIQUITIN-PROTEIN LIGASE RMA; 1.
DR PANTHER; PTHR12313; E3 UBIQUITIN-PROTEIN LIGASE RNF5-RELATED; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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|RuleBase:RU369090};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|RuleBase:RU369090}; Zinc {ECO:0000256|RuleBase:RU369090};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175,
KW ECO:0000256|RuleBase:RU369090}.
FT DOMAIN 120..161
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 46..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 408 AA; 44669 MW; A50B6029B865057C CRC64;
MDLDLNHEPM ESSALGLGSL SNTRIEQRIL HLEAVAARWR QVHNSAPDTA HNSANEAPNS
AANEAPNSAA DTGHNSVQHH NCLGKGKGCK RDRSHLVAKA LEMDVVVKKV DKNGPSFFDC
NICFDIAKEP ILTCCGHLYC WSCFYNLPYV DSTTKECPEC KGEVTDANIT PIYGNAHSYC
SKQVHSAFEL PPRPKANRVE SVRQQRVTRG LSHIPVAEAL RRIRNSIGLG DHPQQLDTGG
VSSTSLNGSQ ELQNTEATGS QRPRSRVFSR VLSEGAASLS SELENVQRLF EDITASITDR
IHERSNLQVS PIGHVVADEG NSLRRDAAII QSEHQTLDSI ADASSVVSLP SSSQSNEVSD
AALQLENLTT DTANLPVILS PYSRRRSGFS RRSDLDSEIL PETRRRFS
//
