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Database: UniProt
Entry: A0A2K5UN47_MACFA
LinkDB: A0A2K5UN47_MACFA
Original site: A0A2K5UN47_MACFA 
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};
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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
//
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