RMD5A_XENTR
ID RMD5A_XENTR Reviewed; 391 AA.
AC Q640V2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=E3 ubiquitin-protein ligase RMND5A;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6GLP4};
DE AltName: Full=Protein RMD5 homolog A;
GN Name=rmnd5a; ORFNames=TGas140j12.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein ligase component of the CTLH complex.
CC {ECO:0000250|UniProtKB:Q6GLP4}.
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:0000250|UniProtKB:Q6GLP4};
CC -!- SUBUNIT: Identified in the CTLH complex that contains at least RANBP9,
CC MKLN1, MAEA, RMND5A, GID8 and ARMC8. {ECO:0000250|UniProtKB:Q9H871}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9H871}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H871}.
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DR EMBL; CR855626; CAJ82582.1; -; mRNA.
DR EMBL; BC082487; AAH82487.1; -; mRNA.
DR RefSeq; NP_001008169.1; NM_001008168.1.
DR AlphaFoldDB; Q640V2; -.
DR SMR; Q640V2; -.
DR STRING; 8364.ENSXETP00000004081; -.
DR PaxDb; Q640V2; -.
DR DNASU; 493531; -.
DR GeneID; 493531; -.
DR KEGG; xtr:493531; -.
DR CTD; 64795; -.
DR Xenbase; XB-GENE-5741891; rmnd5a.
DR eggNOG; KOG2817; Eukaryota.
DR InParanoid; Q640V2; -.
DR OrthoDB; 987270at2759; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR CDD; cd16794; dRING_RMD5A; 1.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR037680; RMD5A_dRING.
DR InterPro; IPR044063; ZF_RING_GID.
DR InterPro; IPR027370; Znf-RING_LisH.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR Pfam; PF10607; CLTH; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00757; CRA; 1.
DR SMART; SM00668; CTLH; 1.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50897; CTLH; 1.
DR PROSITE; PS50896; LISH; 1.
DR PROSITE; PS51867; ZF_RING_GID; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..391
FT /note="E3 ubiquitin-protein ligase RMND5A"
FT /id="PRO_0000272651"
FT DOMAIN 114..146
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 153..210
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 336..377
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
SQ SEQUENCE 391 AA; 43975 MW; 1D454866972FAC7A CRC64;
MDQCGTVERE LEKVLHKFGG YGQHCERSLE ELMEYAGGLR REILQAAEQD GELSGTLSLV
LTQCCKRIKD TVQKLASDHK DIHSSVSRVG KAIDKNFDAD ISSVGIDGCW QNDSQQILSE
VMVEHFFRQG MLDVAEELCQ EAGLSIDASQ KEPFVELNRI LEALKVRVLR PALEWAVSNR
EMLMAQNSSL EFKLHRLYFI SLLMGGTVNQ REALQYAKNF QPFAENHQKD IQVLMGSLVY
LRQGIENSPY VHLLDANQWA DICDIFTRDA CALLGLSVES PLSVSFSAGC VALPALINIK
AVIEQRQCTG VWNQKDELPI EVDLGKKCWY HSIFACPILR QQTTDNNPPM KLVCGHIISR
DALNKMFNGS KLKCPYCPME QSPGDAKQIF F