MEX3C_MOUSE
ID MEX3C_MOUSE Reviewed; 652 AA.
AC Q05A36; Q2VPQ2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=RNA-binding E3 ubiquitin-protein ligase MEX3C;
DE EC=2.3.2.27;
DE AltName: Full=RING finger and KH domain-containing protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase MEX3C {ECO:0000305};
GN Name=Mex3c; Synonyms=Rkhd2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-652.
RC TISSUE=Brain;
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: RNA-binding protein. May be involved in post-transcriptional
CC regulatory mechanisms, modulating levels of some mRNAs by promoting
CC their degradation in a way involving ubiquitin ligase activity. May act
CC as suppressor of replication stress and chromosome missegregation.
CC {ECO:0000250}.
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;
CC -!- SUBUNIT: Interacts with USP7, which antagonizes the ability to degrade
CC mRNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Predominantly expressed in the cytoplasm and shuttles between the
CC cytoplasm and the nucleus through the CRM1 export pathway.
CC -!- DOMAIN: Binds RNA through its KH domains. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI25428.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC134447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108422; AAI08423.1; -; mRNA.
DR EMBL; BC125427; AAI25428.1; ALT_INIT; mRNA.
DR CCDS; CCDS50318.1; -.
DR RefSeq; NP_001034303.3; NM_001039214.4.
DR AlphaFoldDB; Q05A36; -.
DR SMR; Q05A36; -.
DR STRING; 10090.ENSMUSP00000089463; -.
DR iPTMnet; Q05A36; -.
DR PhosphoSitePlus; Q05A36; -.
DR EPD; Q05A36; -.
DR MaxQB; Q05A36; -.
DR PaxDb; Q05A36; -.
DR PRIDE; Q05A36; -.
DR ProteomicsDB; 292302; -.
DR Antibodypedia; 22729; 143 antibodies from 31 providers.
DR Ensembl; ENSMUST00000091852; ENSMUSP00000089463; ENSMUSG00000037253.
DR GeneID; 240396; -.
DR KEGG; mmu:240396; -.
DR UCSC; uc008fot.2; mouse.
DR CTD; 51320; -.
DR MGI; MGI:2652843; Mex3c.
DR VEuPathDB; HostDB:ENSMUSG00000037253; -.
DR eggNOG; KOG2113; Eukaryota.
DR GeneTree; ENSGT00940000160973; -.
DR HOGENOM; CLU_025598_2_0_1; -.
DR InParanoid; Q05A36; -.
DR OMA; MSNYRND; -.
DR OrthoDB; 814376at2759; -.
DR PhylomeDB; Q05A36; -.
DR TreeFam; TF315107; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 240396; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Mex3c; mouse.
DR PRO; PR:Q05A36; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q05A36; protein.
DR Bgee; ENSMUSG00000037253; Expressed in manus and 230 other tissues.
DR Genevisible; Q05A36; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0003415; P:chondrocyte hypertrophy; IMP:MGI.
DR GO; GO:0097009; P:energy homeostasis; IMP:MGI.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00013; KH_1; 2.
DR SMART; SM00322; KH; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF54791; SSF54791; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..652
FT /note="RNA-binding E3 ubiquitin-protein ligase MEX3C"
FT /id="PRO_0000278783"
FT DOMAIN 225..286
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 319..380
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT ZN_FING 601..641
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 15..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..133
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U5Q3"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U5Q3"
SQ SEQUENCE 652 AA; 68574 MW; 74CF20585E55FB9C CRC64;
MPSGSSAALA LALAAAPAPL PQPPPLPPPP PAGGPELEGD GLLLRERLAA LGLDDPSPAE
PGAPALRAAA VAAAAAAQCQ ARRATGLAPE EPGRLATSET AELELEVDEE EGEEAELDGE
LLEEEELEEA EEEDRPSLLL LSPPAATASQ TQPIPGGPLG SVLLPAAGFD AREAAAAGVL
YGGDDAQGMM AAMLSHAYGP GGGGAAAAAL NGEQAALLRR KSVNTTECVP VPSSEHVAEI
VGRQGCKIKA LRAKTNTYIK TPVRGEEPIF VVTGRKEDVA MAKREILSAA EHFSMIRASR
NKNGPALGGL SCSPNLPGQT TVQVRVPYRV VGLVVGPKGA TIKRIQQQTH TYIVTPSRDK
EPVFEVTGMP ENVDRAREEI EMHIAMRTGN YIELNEENDF HYNGTDVSFE GGTLGSAWLS
SNPVPPSRAR MMSNYRNDSS SSLGSGSTDS YFGSNRLADF SPTSPFSTGN FWFGDTLPSV
GSEDLTVDSP AFDSLPTSAQ TIWTPFEPVN PLSGFGSDPS GNMKTQRRGS QPSTPRLSPT
FPESIEHPLA RRVRSDPPST GNHVGLPIYI PAFSNGTNSY SSSNGGSTSS SPPESRRKHD
CVICFENEVI AALVPCGHNL FCMECANKIC EKRTPSCPVC QTAVTQAIQI HS
