ID A0A2K5UN47_MACFA Unreviewed; 423 AA.
AC A0A2K5UN47;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN Name=RNF123 {ECO:0000313|Ensembl:ENSMFAP00000013848.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000013848.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000013848.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000013848.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 ---------------------------------------------------------------------------
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 AlphaFoldDB; A0A2K5UN47; -.
DR Ensembl; ENSMFAT00000064297.2; ENSMFAP00000013848.1; ENSMFAG00000028385.2.
DR VEuPathDB; HostDB:ENSMFAG00000028385; -.
DR GeneTree; ENSGT00940000155781; -.
DR Proteomes; UP000233100; Chromosome 2.
DR Bgee; ENSMFAG00000028385; Expressed in cerebellum and 13 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd16541; RING-HC_RNF123; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 366..404
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 423 AA; 47494 MW; 62B42B02D7CD5C88 CRC64;
MEHSYEETLT RLAAILAKHF ADTRIVGTDI RDSLMQALAS YVCYPHSLRA VERIPEEQRI
AMVRNLLAPY EQRPWAQTNW ILVRLWRGCG FGYRYTRLPH LLKTKLEDAN LPSLQKPCPS
TLLQQHMADL LQQGPDVAPS FLNSVLNQLN WAFSEFIGMI QEIQQAAERL ERNFVDSRQL
KVCATCFDLS VSLLRVLEMT ITLVPEIFLD WTRPTSEMLL RRLAQLLNQV LNRVTAERNL
FDRVVTLRLP GLESVDHYPI LVAVTGILVQ LLVRGPASER ERATSVLLAD PCFQLRSICY
LLGQPEPPAP GTALPAPDRK RFSLQSYADY ISADELAQVE QMLAHLTSAS AQAAAASLPT
SEEDLCPICY AHPISAVFQP CGHKSCKACI NQHLMNNKDC FFCKATIVSV EDWANTSTTS
SAA
//