MAEA_DANRE
ID MAEA_DANRE Reviewed; 396 AA.
AC Q7SXR3;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=E3 ubiquitin-protein transferase MAEA;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q7L5Y9};
DE AltName: Full=Macrophage erythroblast attacher;
GN Name=maea; ORFNames=zgc:63708;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Core component of the CTLH E3 ubiquitin-protein ligase
CC complex that selectively accepts ubiquitin from UBE2H and mediates
CC ubiquitination and subsequent proteasomal degradation of the
CC transcription factor HBP1. MAEA and RMND5A are both required for
CC catalytic activity of the CTLH E3 ubiquitin-protein ligase complex.
CC MAEA is required for normal cell proliferation. The CTLH E3 ubiquitin-
CC protein ligase complex is not required for the degradation of enzymes
CC involved in gluconeogenesis, such as FBP1 (By similarity). Plays a role
CC in erythroblast maturation and in the development of mature macrophages
CC (By similarity). Mediates the attachment of erythroid cell to mature
CC macrophages; this MAEA-mediated contact inhibits erythroid cell
CC apoptosis (By similarity). Participates in erythroblastic island
CC formation, which is the functional unit of definitive erythropoiesis.
CC Associates with F-actin to regulate actin distribution in erythroblasts
CC and macrophages (By similarity). May contribute to nuclear architecture
CC and cells division events (By similarity).
CC {ECO:0000250|UniProtKB:Q4VC33, ECO:0000250|UniProtKB:Q7L5Y9}.
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:Q7L5Y9};
CC -!- SUBUNIT: Identified in the CTLH complex that contains at least MAEA,
CC RMND5A, GID8, WDR26, and RANBP9 and/or RANBP10 as the catalytic core.
CC Interacts with F-actin. {ECO:0000250|UniProtKB:Q7L5Y9}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q4VC33}.
CC Cell membrane {ECO:0000250|UniProtKB:Q4VC33}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q4VC33}. Note=Migration from nuclear matrix in
CC immature macrophages to cell surface in mature ones.
CC {ECO:0000250|UniProtKB:Q4VC33}.
CC -!- DOMAIN: The expected RING-type zinc finger domain is highly divergent
CC and most of the expected Cys residues are not conserved. Still, the
CC protein is required for CTLH complex E3 ubiquitin-protein transferase
CC activity. In addition, the conserved Cys-314 in this highly divergent
CC region is required for ubiquitination by the yeast GID complex,
CC suggesting a direct role in catalyzing ubiquitination.
CC {ECO:0000250|UniProtKB:Q7L5Y9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55388.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC055388; AAH55388.1; ALT_INIT; mRNA.
DR RefSeq; NP_955843.2; NM_199549.2.
DR AlphaFoldDB; Q7SXR3; -.
DR SMR; Q7SXR3; -.
DR STRING; 7955.ENSDARP00000070240; -.
DR PaxDb; Q7SXR3; -.
DR Ensembl; ENSDART00000075759; ENSDARP00000070240; ENSDARG00000053691.
DR GeneID; 321575; -.
DR KEGG; dre:321575; -.
DR CTD; 10296; -.
DR ZFIN; ZDB-GENE-030131-294; maea.
DR eggNOG; KOG0396; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_027445_0_1_1; -.
DR InParanoid; Q7SXR3; -.
DR OMA; DVKYDEW; -.
DR OrthoDB; 1087488at2759; -.
DR PhylomeDB; Q7SXR3; -.
DR TreeFam; TF314273; -.
DR PRO; PR:Q7SXR3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 14.
DR Bgee; ENSDARG00000053691; Expressed in cleaving embryo and 28 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR013144; CRA_dom.
DR InterPro; IPR024964; CTLH/CRA.
DR InterPro; IPR006595; CTLH_C.
DR InterPro; IPR027714; Fyv10/MAEA.
DR InterPro; IPR045098; Fyv10_fam.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR044063; ZF_RING_GID.
DR PANTHER; PTHR12170; PTHR12170; 1.
DR PANTHER; PTHR12170:SF2; PTHR12170:SF2; 1.
DR Pfam; PF10607; CLTH; 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 Actin-binding; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Cytoskeleton; Erythrocyte maturation; Membrane; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..396
FT /note="E3 ubiquitin-protein transferase MAEA"
FT /id="PRO_0000284942"
FT DOMAIN 121..153
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT DOMAIN 159..216
FT /note="CTLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00058"
FT ZN_FING 314..381
FT /note="RING-Gid-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01215"
FT SITE 314
FT /note="Essential for ubiquitin ligase activity"
FT /evidence="ECO:0000250|UniProtKB:P40492"
SQ SEQUENCE 396 AA; 45342 MW; FCE3489C2E82C7B8 CRC64;
MAVQETAAQL SMALKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSS
FPVVDTVVSL LDGVVEKLSA LKRKAAESIQ AEDESAKLCK RRIEHLKEHS SDQPASVNVW
KKKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERQETATCLA
WCHDNKSRLR KMKSCLEFSL RIQEFIELIR QNKRMDAVRH ARKHFSQAEG GQLDEVRQVM
GMLAFPSDTH ISPYKDLLDP ARWKMLIQQF RYDNYRLHQL GNNSVFTITL QAGLSAIKTP
QCYKEDGTSK NPDCPVCSKS LNKLAQPLPM AHCANSRLVC KISGEVMNEN NPPMMLPNGY
VYGYNSLLSI RQDDKVICPR TKEVFNFSQA EKVYIM
