UniProt: A0A1S3EG96

Database: UniProt
Entry: A0A1S3EG96_CICAR

LinkDB:  A0A1S3EG96_CICAR 
Original site:  A0A1S3EG96_CICAR

All links

Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (8)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
   SMART (1)   
All databases (18)   

Download RDF

ID   A0A1S3EG96_CICAR        Unreviewed;       230 AA.
AC   A0A1S3EG96;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
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   Name=LOC101488833 {ECO:0000313|RefSeq:XP_012574427.1,
GN   ECO:0000313|RefSeq:XP_012574428.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_012574428.1};
RN   [1] {ECO:0000313|RefSeq:XP_012574427.1, ECO:0000313|RefSeq:XP_012574428.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_012574427.1,
RC   ECO:0000313|RefSeq:XP_012574428.1};
RG   RefSeq;
RL   Submitted (NOV-2023) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_012574427.1; XM_012718973.2.
DR   RefSeq; XP_012574428.1; XM_012718974.2.
DR   STRING; 3827.A0A1S3EG96; -.
DR   GeneID; 101488833; -.
DR   KEGG; cam:101488833; -.
DR   OrthoDB; 276791at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000087171; Chromosome Ca8.
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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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:SF47; 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:UP000087171};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU369090};
KW   Transmembrane {ECO:0000256|RuleBase:RU369090};
KW   Transmembrane helix {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   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369090"
FT   DOMAIN          33..74
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          87..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   230 AA;  25087 MW;  83B839F5EF001403 CRC64;
     MSSGFGESTR SFPPNPSCSS GNNPNNDAGD FECNICFDLA QDPVITLCGH LFCWPCLYRW
     LHHHSHSQEC PVCKALVVEE KLVPLYGRGK SQTDPRTKSY PGMEIPRRPS GQRPQTAPPP
     PPPEANYAGF GLMGGFIPMA TARFGNFTLS TAFGGFIPSL LNIHFHGFQD ATVYGTTSGH
     PFGFNTFQGG NSRGFSSQAT GQVQRQEDNV LKNLLLLIGV FVLLTVIFVM
//

DBGET integrated database retrieval system