ID   RMD5A_XENLA             Reviewed;         391 AA.
AC   Q6GLP4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=E3 ubiquitin-protein ligase RMND5A {ECO:0000303|PubMed:25793641};
DE            EC=2.3.2.27 {ECO:0000269|PubMed:25793641};
DE   AltName: Full=Protein RMD5 homolog A;
GN   Name=rmnd5a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP   SUBUNIT, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF CYS-354.
RX   PubMed=25793641; DOI=10.1371/journal.pone.0120342;
RA   Pfirrmann T., Villavicencio-Lorini P., Subudhi A.K., Menssen R., Wolf D.H.,
RA   Hollemann T.;
RT   "RMND5 from Xenopus laevis is an E3 ubiquitin-ligase and functions in early
RT   embryonic forebrain development.";
RL   PLoS ONE 10:E0120342-E0120342(2015).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase component of the CTLH complex.
CC       {ECO:0000305|PubMed:25793641}.
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:0000269|PubMed:25793641};
CC   -!- SUBUNIT: Identified in the CTLH complex that contains at least RANBP9,
CC       MKLN1, MAEA, RMND5A, GID8 and ARMC8. {ECO:0000305|PubMed:25793641}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:25793641}. Cytoplasm {ECO:0000269|PubMed:25793641}.
CC   -!- DEVELOPMENTAL STAGE: Detected at constant levels throughout embryonic
CC       development (at protein level). Detected at high levels at the four
CC       cell stage of embryogenesis, followed by a steady decline until
CC       gastrulation. Detected at low levels throughout further stages of
CC       embryo development. Primarily expressed in the head region during
CC       gastrulation, and in the neuroectoderm during neurulation.
CC       {ECO:0000269|PubMed:25793641}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein disrupts
CC       normal development of the mesencephalon, the prosencephalon and the
CC       eyes. {ECO:0000269|PubMed:25793641}.
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DR   EMBL; BC074415; AAH74415.1; -; mRNA.
DR   RefSeq; NP_001086276.1; NM_001092807.1.
DR   AlphaFoldDB; Q6GLP4; -.
DR   SMR; Q6GLP4; -.
DR   DNASU; 444705; -.
DR   GeneID; 444705; -.
DR   KEGG; xla:444705; -.
DR   CTD; 444705; -.
DR   Xenbase; XB-GENE-5742072; rmnd5a.L.
DR   OrthoDB; 987270at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 444705; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA: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; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA: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   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS51867; ZF_RING_GID; 1.
PE   1: Evidence at protein 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_0000272650"
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"
FT   MUTAGEN         354
FT                   /note="C->S: Loss of ubiquitin ligase activity."
FT                   /evidence="ECO:0000269|PubMed:25793641"
SQ   SEQUENCE   391 AA;  43952 MW;  2D8BB556BA50F63F CRC64;
     MDQCGTVERE LEKVLHKFGG YGQLCERSLE ELIDYAGGLR REILQAAEQD GELSGTLSLV
     LTQCCKRIKD TVQKLASDHK DIHSSVSRVG KAIDKNFDAD ISSVGIDGCW QTDSQRILSE
     VMVEHFFRQG MLDVAEELCQ EASLSIDASQ KEPFVELNRI LEALKVRVLR PALEWAVSNR
     EMLMAQNSSL EFKLHRLYFI SLLMGGTVNQ QEALQYAKNF QPFAENHQKD IQVLMGSLVY
     LRQGIENSPY VHLLDANQWA DICDIFTRDA CSLLGLSVES PLSVSFSAGC VALPALINIK
     AVIEQRQCSG VWNQKDELPI EVDLGKKCWY HSIFACPILR QQTTENNPPM KLVCGHIISR
     DALNKMFNGS KLKCPYCPME QSPGDAKQIF F