TRI62_MOUSE
ID TRI62_MOUSE Reviewed; 475 AA.
AC Q80V85;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM62 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q9BVG3};
DE AltName: Full=Tripartite motif-containing protein 62 {ECO:0000303|PubMed:26488816};
GN Name=Trim62 {ECO:0000303|PubMed:26488816, ECO:0000312|MGI:MGI:1914775};
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic 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).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=26488816; DOI=10.1016/j.immuni.2015.10.005;
RA Cao Z., Conway K.L., Heath R.J., Rush J.S., Leshchiner E.S.,
RA Ramirez-Ortiz Z.G., Nedelsky N.B., Huang H., Ng A., Gardet A., Cheng S.C.,
RA Shamji A.F., Rioux J.D., Wijmenga C., Netea M.G., Means T.K., Daly M.J.,
RA Xavier R.J.;
RT "Ubiquitin ligase TRIM62 regulates CARD9-mediated anti-fungal immunity and
RT intestinal inflammation.";
RL Immunity 43:715-726(2015).
CC -!- FUNCTION: E3 ubiquitin ligase that plays a role in antifungal immunity
CC by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-
CC type lectin receptors; leading to CARD9 activation, followed by
CC activation of NF-kappa-B and MAP kinase p38 pathways (By similarity).
CC E3 ubiquitin ligase activity is dependent on E2 ubiquitin-conjugating
CC enzyme UBE2D2 (By similarity). {ECO:0000250|UniProtKB:Q9BVG3}.
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:Q9BVG3};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q9BVG3}.
CC -!- SUBUNIT: Interacts with the ubiquitin-conjugating enzyme, UBE2D2.
CC {ECO:0000250|UniProtKB:Q9BVG3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BVG3}.
CC -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC {ECO:0000250|UniProtKB:Q9BVG3}.
CC -!- PTM: Polyubiquitinated, autoubiquitinated in the presence of UBE2D2.
CC {ECO:0000250|UniProtKB:Q9BVG3}.
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to fungal infection.
CC {ECO:0000269|PubMed:26488816}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC049095; AAH49095.1; -; mRNA.
DR CCDS; CCDS18677.1; -.
DR RefSeq; NP_835211.1; NM_178110.2.
DR AlphaFoldDB; Q80V85; -.
DR SMR; Q80V85; -.
DR BioGRID; 212248; 1.
DR STRING; 10090.ENSMUSP00000039121; -.
DR iPTMnet; Q80V85; -.
DR PhosphoSitePlus; Q80V85; -.
DR PaxDb; Q80V85; -.
DR PRIDE; Q80V85; -.
DR ProteomicsDB; 259094; -.
DR Antibodypedia; 17083; 174 antibodies from 24 providers.
DR DNASU; 67525; -.
DR Ensembl; ENSMUST00000035667; ENSMUSP00000039121; ENSMUSG00000041000.
DR GeneID; 67525; -.
DR KEGG; mmu:67525; -.
DR UCSC; uc008uvo.1; mouse.
DR CTD; 55223; -.
DR MGI; MGI:1914775; Trim62.
DR VEuPathDB; HostDB:ENSMUSG00000041000; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158433; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q80V85; -.
DR OMA; TAHHRLI; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q80V85; -.
DR TreeFam; TF342569; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 67525; 6 hits in 73 CRISPR screens.
DR PRO; PR:Q80V85; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80V85; protein.
DR Bgee; ENSMUSG00000041000; Expressed in cerebellar cortex and 203 other tissues.
DR ExpressionAtlas; Q80V85; baseline and differential.
DR Genevisible; Q80V85; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:1905036; P:positive regulation of antifungal innate immune response; IMP:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR CDD; cd13744; SPRY_PRY_TRIM62; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR035830; PRY/SPRY_TRIM62.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Immunity; Innate immunity; Metal-binding;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..475
FT /note="E3 ubiquitin-protein ligase TRIM62"
FT /id="PRO_0000249575"
FT DOMAIN 277..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 11..54
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 88..128
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 121..241
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 475 AA; 54298 MW; C86750A926E8E434 CRC64;
MACSLKDELL CSICLSIYQD PVSLGCEHYF CRRCITEHWV RQEAQGARDC PECRRTFAEP
ALAPSLKLAN IVERYSAFPL DAILNARRAA RPCQAHDKVK LFCLTDRALL CFFCDEPALH
EQHQVTGIDD AFEELQRELK EQLQALQDSE REHTEALQLL KRQLAETKSS TKSLRTTIGE
AFERLHRLLR ERQKAMLEEL EADTARTLTD IEQKVQRYSQ QLRKVQEGAQ ILQERLAETD
RHTFLAGVAS LSERLKGKIH ETNLTYEDFP TSKYTGPLQY TIWKSLFQDI HPVPAALTMD
PGTAHQRLIL SDDCTIVAYG NLHPQPLQDS PKRFDVEVSV LGSEAFSSGV HYWEVVVAEK
TQWVIGLAHE AASRKGSIQI QPSRGFYCIV MHDGNQYSAC TEPWTRLNVR DKLDKVGVFL
DYDQGLLIFY NADDMSWLYT FREKFPGKLC SYFSPGQSHA NGKNVQPLRI NTVRI
