MAEA_CHICK
ID MAEA_CHICK Reviewed; 396 AA.
AC Q5F398;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=RCJMB04_26n5;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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: Cytoplasm {ECO:0000250|UniProtKB:Q4VC33}.
CC Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q7L5Y9}. Nucleus matrix
CC {ECO:0000250|UniProtKB:Q4VC33}. Cell membrane
CC {ECO:0000250|UniProtKB:Q4VC33}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q4VC33}. Note=Detected in a nuclear, speckled-
CC like pattern (By similarity). Localized with condensed chromatin at
CC prophase; Detected in nuclear spindle poles at metaphase and in the
CC contractile ring during telophase and cytokinesis (By similarity).
CC Present in cytoplasm, nuclear matrix and at the cell surface in
CC macrophages; predominantly nuclear in immature macrophages and
CC predominantly detected at the cell surface in mature macrophages.
CC Colocalizes with F-actin in macrophages (By similarity).
CC {ECO:0000250|UniProtKB:Q4VC33, ECO:0000250|UniProtKB:Q7L5Y9}.
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}.
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DR EMBL; AJ851752; CAH65386.1; -; mRNA.
DR RefSeq; NP_001012622.1; NM_001012604.1.
DR AlphaFoldDB; Q5F398; -.
DR SMR; Q5F398; -.
DR STRING; 9031.ENSGALP00000021704; -.
DR PaxDb; Q5F398; -.
DR Ensembl; ENSGALT00000021740; ENSGALP00000021704; ENSGALG00000013310.
DR GeneID; 426024; -.
DR KEGG; gga:426024; -.
DR CTD; 10296; -.
DR VEuPathDB; HostDB:geneid_426024; -.
DR eggNOG; KOG0396; Eukaryota.
DR GeneTree; ENSGT00940000153203; -.
DR HOGENOM; CLU_027445_0_1_1; -.
DR InParanoid; Q5F398; -.
DR OMA; DVKYDEW; -.
DR OrthoDB; 1087488at2759; -.
DR PhylomeDB; Q5F398; -.
DR PRO; PR:Q5F398; -.
DR Proteomes; UP000000539; Chromosome 4.
DR Bgee; ENSGALG00000013310; Expressed in spermatid and 14 other tissues.
DR GO; GO:0005826; C:actomyosin contractile ring; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
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:0005819; C:spindle; IEA:Ensembl.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
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:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0048822; P:enucleate erythrocyte development; IEA:Ensembl.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IEA:Ensembl.
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_0000284941"
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 REGION 1..124
FT /note="Extracellular and involved in cell to cell contact"
FT /evidence="ECO:0000250|UniProtKB:Q7L5Y9"
FT SITE 314
FT /note="Essential for ubiquitin ligase activity"
FT /evidence="ECO:0000250|UniProtKB:P40492"
SQ SEQUENCE 396 AA; 45388 MW; EF6CE7137E099A4B CRC64;
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSS
CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK RRIEHLKEHS SDQPAAANMW
KKKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERQETMTCLA
WCHDNKSRLR KMKSCLEFSL RIQEFIELIR QNKRLDAVRH ARKHFSQAEG SQLDEVRQVM
GMLAFPSDTH ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNNSVFTITL QAGLSAIKTP
QCYKEDGSSK NPDCPVCSKS LNKLAQPLPM AHCANSRLVC KISGDVMNEN NPPMMLPNGY
VYGYNSLLSI RQDDKVICPR TKEVFNFSQA EKVYIM
