ID A0A0D9R7B4_CHLSB Unreviewed; 418 AA.
AC A0A0D9R7B4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE AltName: Full=RING-type E3 ubiquitin transferase makorin-1 {ECO:0000256|ARBA:ARBA00042581};
GN Name=MKRN1 {ECO:0000313|Ensembl:ENSCSAP00000004503.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000004503.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000004503.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000004503.1}
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}.
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DR EMBL; AQIB01020935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01020936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01020937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01020938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01020939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01020940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007981345.1; XM_007983154.1.
DR AlphaFoldDB; A0A0D9R7B4; -.
DR STRING; 60711.ENSCSAP00000004503; -.
DR Ensembl; ENSCSAT00000006298.1; ENSCSAP00000004503.1; ENSCSAG00000008246.1.
DR eggNOG; KOG1039; Eukaryota.
DR GeneTree; ENSGT00950000183077; -.
DR OMA; QQTNVEM; -.
DR OrthoDB; 2906101at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 103227015; 0 hits in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 21.
DR Bgee; ENSCSAG00000008246; Expressed in blood and 7 other cell types or tissues.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
DR CDD; cd16730; RING-HC_MKRN1_3; 1.
DR Gene3D; 2.30.30.1190; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR031644; MKRN1_C.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11224:SF37; E3 UBIQUITIN-PROTEIN LIGASE MAKORIN-1; 1.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR Pfam; PF15815; MKRN1_C; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF14608; zf-CCCH_2; 2.
DR Pfam; PF18044; zf-CCCH_4; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR SUPFAM; SSF90229; CCCH zinc finger; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50103; ZF_C3H1; 4.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 1..18
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 20..47
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 144..171
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 217..271
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 300..329
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT ZN_FING 1..18
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 20..47
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 144..171
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 300..329
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 418 AA; 47652 MW; D84B22CE0237AC2D CRC64;
MHGVCKEGDN CRYSHDLSDS PYSVVCKYFQ RGYCIYGDRC RYEHSKPLKQ EEATATELNT
KSSLAASSSL SSIVGPLVEM NTGEAESRNS NFATVGAGSE DWVNAIEFVP GQPYCGRTAP
SCTEAPLQGS VTKEESEKEQ TAVETKKQLC PYAAVGECRY GENCVYLHGD SCDMCGLQVL
HPMDAAQRSQ HIKSCIEAHE KDMELSFAVQ RSKDMVCGIC MEVVYEKANP SERRFGILSN
CNHTYCLKCI RKWRSAKQFE SKIIKSCPEC RITSNFVIPS EYWVEEKEEK QKLILKYKEA
MSNKACRYFD EGRGSCPFGG NCFYKHAYPD GRREEPQRQK VGTSSRYRAQ RRNHFWELIE
ERENSNPFDN DEEEVVTFEL GEMLLMLLAA GGDDELTDSE DEWDLFHDEL EDFYDLDL
//