TRI58_MOUSE
ID TRI58_MOUSE Reviewed; 485 AA.
AC Q5NCC9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM58;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM58 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 58;
GN Name=Trim58; Synonyms=Gm16;
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 TISSUE SPECIFICITY.
RX PubMed=25241935; DOI=10.1016/j.devcel.2014.07.021;
RA Thom C.S., Traxler E.A., Khandros E., Nickas J.M., Zhou O.Y., Lazarus J.E.,
RA Silva A.P., Prabhu D., Yao Y., Aribeana C., Fuchs S.Y., Mackay J.P.,
RA Holzbaur E.L., Weiss M.J.;
RT "Trim58 degrades Dynein and regulates terminal erythropoiesis.";
RL Dev. Cell 30:688-700(2014).
CC -!- FUNCTION: E3 ubiquitin ligase induced during late erythropoiesis.
CC Directly binds and ubiquitinates the intermediate chain of the
CC microtubule motor dynein (DYNC1LI1/DYNC1LI2), stimulating the
CC degradation of the dynein holoprotein complex. May participate in the
CC erythroblast enucleation process through regulation of nuclear
CC polarization. {ECO:0000250|UniProtKB:Q8NG06}.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8NG06}.
CC -!- TISSUE SPECIFICITY: Expressed in erythroblasts.
CC {ECO:0000269|PubMed:25241935}.
CC -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC {ECO:0000250|UniProtKB:Q8NG06}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AL645802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24738.1; -.
DR RefSeq; NP_001034136.1; NM_001039047.1.
DR AlphaFoldDB; Q5NCC9; -.
DR SMR; Q5NCC9; -.
DR BioGRID; 229784; 1.
DR STRING; 10090.ENSMUSP00000074594; -.
DR iPTMnet; Q5NCC9; -.
DR PhosphoSitePlus; Q5NCC9; -.
DR MaxQB; Q5NCC9; -.
DR PaxDb; Q5NCC9; -.
DR PRIDE; Q5NCC9; -.
DR ProteomicsDB; 258978; -.
DR Antibodypedia; 20850; 109 antibodies from 19 providers.
DR DNASU; 216781; -.
DR Ensembl; ENSMUST00000075084; ENSMUSP00000074594; ENSMUSG00000037124.
DR GeneID; 216781; -.
DR KEGG; mmu:216781; -.
DR UCSC; uc007jby.1; mouse.
DR CTD; 25893; -.
DR MGI; MGI:2684862; Trim58.
DR VEuPathDB; HostDB:ENSMUSG00000037124; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162246; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q5NCC9; -.
DR OMA; FFICDTT; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q5NCC9; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 216781; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q5NCC9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5NCC9; protein.
DR Bgee; ENSMUSG00000037124; Expressed in bone marrow and 10 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045504; F:dynein heavy chain binding; IDA:UniProtKB.
DR GO; GO:0045505; F:dynein intermediate chain binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0061931; P:positive regulation of erythrocyte enucleation; IMP:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:1902838; P:regulation of nuclear migration along microtubule; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR CDD; cd16606; RING-HC_TRIM58_C-IV; 1.
DR CDD; cd15816; SPRY_PRY_TRIM58; 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; IPR035787; SPRY/PRY_TRIM58.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042699; TRIM58_RING-HC.
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; SM00336; BBOX; 1.
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; Metal-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="E3 ubiquitin-protein ligase TRIM58"
FT /id="PRO_0000272302"
FT DOMAIN 271..466
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 90..131
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 192..241
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 485 AA; 55371 MW; 4D9CD7B28BEC16BE CRC64;
MATAPGERLQ EEARCSVCLD FLQEPISVDC GHSFCLRCIS EFCEKSDSAQ GVYACPQCRG
PFRPASFRPN RQLASLVDSV RQLGLGTGHA GSRQCARHGE DLSHFCEEDQ TMLCWVCDTS
PEHRSHRTET LQEAASRYQR MLRASLELVK KEMEEALTQE ANVGKKTIIW KEKVEMQRQR
FRLEFEKHRG FLAQEEQLQL RRLEEEERAT LQRLRDSRNR LAQQNKALKE LAEELEERSQ
RPAPGLLEGA RGVLTRCEAI TRLEPEAVPM DLKTVCRIPG MREMLRKFQV DVKLDPATAH
PSLLLTADLR SVQDAEVWRD VPSNPERFDT WPCILGLQGF SSGRHYWEVI VGERAEWGLG
VCRDSVLRKG ETTPSPENGV WAMWLLRGNE YMVLSSPSVP VLQDERPRRI GIFLDYEAGE
ISFYNVTNGS YIYTFNHLFS GVLRPYFFVC DTTPLILPPM TEAAPGNWTP RGIFDLAAAA
RNEEY
