MAEA_RAT
ID MAEA_RAT Reviewed; 396 AA.
AC Q5RKJ1;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 enucleation during erythrocyte maturation and in the
CC development of mature macrophages (By similarity). Mediates the
CC attachment of erythroid cell to mature macrophages; this MAEA-mediated
CC contact inhibits erythroid cell apoptosis (By similarity). Participates
CC in erythroblastic island formation, which is the functional unit of
CC definitive erythropoiesis. Associates with F-actin to regulate actin
CC distribution in erythroblasts and macrophages (By similarity). May
CC contribute to nuclear architecture and cells division events (By
CC similarity). {ECO:0000250|UniProtKB:Q4VC33,
CC 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 GID4, RANBP9
CC and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog
CC RMND5B), GID8, ARMC8, WDR26 and YPEL5. Within this complex, MAEA,
CC RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9
CC and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and
CC YPEL5 have ancillary roles. Interacts with F-actin.
CC {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}.
CC -!- PTM: Autoubiquitinated as component of the CTLH E3 ubiquitin-protein
CC ligase complex (in vitro). {ECO:0000250|UniProtKB:Q7L5Y9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH85770.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC085770; AAH85770.1; ALT_INIT; mRNA.
DR RefSeq; NP_001008320.2; NM_001008319.2.
DR AlphaFoldDB; Q5RKJ1; -.
DR SMR; Q5RKJ1; -.
DR STRING; 10116.ENSRNOP00000007181; -.
DR jPOST; Q5RKJ1; -.
DR PaxDb; Q5RKJ1; -.
DR PRIDE; Q5RKJ1; -.
DR GeneID; 298982; -.
DR KEGG; rno:298982; -.
DR UCSC; RGD:1309877; rat.
DR CTD; 10296; -.
DR RGD; 1309877; Maea.
DR VEuPathDB; HostDB:ENSRNOG00000005397; -.
DR eggNOG; KOG0396; Eukaryota.
DR HOGENOM; CLU_027445_0_1_1; -.
DR InParanoid; Q5RKJ1; -.
DR OMA; DVKYDEW; -.
DR OrthoDB; 1087488at2759; -.
DR PhylomeDB; Q5RKJ1; -.
DR TreeFam; TF314273; -.
DR PRO; PR:Q5RKJ1; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000005397; Expressed in heart and 19 other tissues.
DR Genevisible; Q5RKJ1; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005826; C:actomyosin contractile ring; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0034657; C:GID complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0048822; P:enucleate erythrocyte development; ISO:RGD.
DR GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR GO; GO:0043249; P:erythrocyte maturation; IEA:UniProtKB-KW.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; ISO:RGD.
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 Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..396
FT /note="E3 ubiquitin-protein transferase MAEA"
FT /id="PRO_0000284940"
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"
FT MOD_RES 28
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7L5Y9"
SQ SEQUENCE 396 AA; 45336 MW; 686F1E086742B99B CRC64;
MAVQESAAQL SMTLKVQEYP TLKVPYETLN KRFRAAQKNI DRETSHVTMV VAELEKTLSS
CPAVDSVVSL LDGVVEKLSV LKRKAVESIQ AEDESAKLCK RRIEHLKEHS SDQPAAASMW
KRKRMDRMMV EHLLRCGYYN TAVKLARQSG IEDLVNIEMF LTAKEVEESL ERRETATCLA
WCHDNKSRLR KMKSCLEFSL RIQEFIELVR QNKRLDAVRH ARKHFSQAEG SQLDEVRQVM
GMLAFPPDTH ISPYKDLLDP ARWRMLIQQF RYDNYRLHQL GNSSVFTLTL QAGLSAIKTP
QCYKEDGSSK SPDCPVCSRS LNKLAQPLPM AHCANSRLVC KISGDVMNEN NPPMMLPNGY
VYGYNSLLSI RQDDKVVCPR TKEVFHFSQA EKVYIM
