ID H0XM00_OTOGA Unreviewed; 362 AA.
AC H0XM00;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RFFL {ECO:0000313|Ensembl:ENSOGAP00000017140.1};
OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lorisiformes;
OC Galagidae; Otolemur.
OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000017140.1, ECO:0000313|Proteomes:UP000005225};
RN [1] {ECO:0000313|Proteomes:UP000005225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B.,
RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N.,
RA Walker B.J., Sharpe T., Hall G.;
RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby).";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSOGAP00000017140.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm,
CC cytosol {ECO:0000256|ARBA:ARBA00004514}.
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DR EMBL; AAQR03133408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAQR03133409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012665245.1; XM_012809791.1.
DR AlphaFoldDB; H0XM00; -.
DR STRING; 30611.ENSOGAP00000017140; -.
DR Ensembl; ENSOGAT00000028738.1; ENSOGAP00000017140.1; ENSOGAG00000024777.1.
DR GeneID; 100941486; -.
DR KEGG; oga:100941486; -.
DR CTD; 117584; -.
DR eggNOG; KOG4275; Eukaryota.
DR GeneTree; ENSGT00390000012719; -.
DR HOGENOM; CLU_041431_1_0_1; -.
DR InParanoid; H0XM00; -.
DR OMA; NWFCLNG; -.
DR OrthoDB; 383715at2759; -.
DR TreeFam; TF325195; -.
DR Proteomes; UP000005225; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR CDD; cd15770; FYVE_CARP2; 1.
DR CDD; cd16707; RING-HC_CARP2; 1.
DR Gene3D; 1.10.720.140; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR049320; CARP1_2_FYVE.
DR InterPro; IPR049322; CARP2_FYVE.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR14879:SF2; E3 UBIQUITIN-PROTEIN LIGASE RIFIFYLIN; 1.
DR Pfam; PF21272; FYVE_CARP1-2; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005225};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 315..350
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 17..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 40256 MW; C58252065246EE1D CRC64;
MWATCCNWFC LDGQPDEGPP PQGARTQAYS NPGYSSFPSP TGSEPSCKGC GAHFANTARK
QICLDCKKNF CMTCSSQEGN GPRLCLLCQR FRATAFQREE LMKMKVKDLR DYLSLHDIST
ETCREKEELV FLVLGQQPII SQEDRTRAPT LSPDFPEQQA FLSQLHTSMV PPTSPSASSS
AQATSVPPAQ APEHQQANGH VSQDYEESVY LESTARAPAE DETQSIDSED SFVPGRRASL
SDLTDLEDIE GLTVRQLKEI LARNFVNYKG CCEKWELMER VTRLYKDQKG LQHLVCGAED
QNGGAVPSGL EDNLCKICMD SPIDCVLLEC GHMVTCTKCG KRMNECPICR QYVIRAVHVF
RS
//
