TRI39_RAT
ID TRI39_RAT Reviewed; 488 AA.
AC Q6MFZ5;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM39;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 23;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM39 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 39;
GN Name=Trim39; Synonyms=Rnf23;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15060004; DOI=10.1101/gr.1987704;
RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT "The genomic sequence and comparative analysis of the rat major
RT histocompatibility complex.";
RL Genome Res. 14:631-639(2004).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (By similarity). May facilitate
CC apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and
CC subsequent proteasome-mediated degradation of the pro-apoptotic protein
CC MOAP1 (By similarity). Regulates the G1/S transition of the cell cycle
CC and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (By
CC similarity). Positively regulates CDKN1A/p21 stability by competing
CC with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3
CC ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q9HCM9}.
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 -!- SUBUNIT: Interacts with MOAP1 (By similarity). Interacts with CDKN1A
CC (By similarity). {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9HCM9}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9HCM9}. Nucleus {ECO:0000250|UniProtKB:Q9HCM9}.
CC Note=Found predominantly in the cytosol. Partial shift from the cytosol
CC to the mitochondria when colocalized with MOAP1. Colocalizes with
CC CDKN1A in the nucleus. {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BX883050; CAE84052.1; -; Genomic_DNA.
DR RefSeq; NP_998727.1; NM_213562.1.
DR AlphaFoldDB; Q6MFZ5; -.
DR BMRB; Q6MFZ5; -.
DR SMR; Q6MFZ5; -.
DR STRING; 10116.ENSRNOP00000001021; -.
DR PaxDb; Q6MFZ5; -.
DR GeneID; 309591; -.
DR KEGG; rno:309591; -.
DR UCSC; RGD:1303115; rat.
DR CTD; 56658; -.
DR RGD; 1303115; Trim39.
DR VEuPathDB; HostDB:ENSRNOG00000000785; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q6MFZ5; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q6MFZ5; -.
DR TreeFam; TF342569; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q6MFZ5; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000785; Expressed in thymus and 19 other tissues.
DR ExpressionAtlas; Q6MFZ5; baseline and differential.
DR Genevisible; Q6MFZ5; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd13745; SPRY_PRY_TRIM39; 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; IPR035033; PRY/SPRY_TRIM39.
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; 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 3: Inferred from homology;
KW Apoptosis; Coiled coil; Cytoplasm; Metal-binding; Mitochondrion; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="E3 ubiquitin-protein ligase TRIM39"
FT /id="PRO_0000056259"
FT DOMAIN 289..484
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 29..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 102..143
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 268..307
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM9"
FT REGION 359..488
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM9"
FT COILED 181..250
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 488 AA; 56394 MW; 576A9FACB54B5F72 CRC64;
MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL
ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQTVKRK IRDESLCSQH HEPLSLFCYE
DQEAVCLICA ISHTHRAHTV VPMDDATQEY KEKLQKCLEP LEQKLQEITC CKASEERKPG
ELKRLVESRR QQILKEFEEL HRRLDEEQQT LLSRLEEEEQ DILQRLRENA AHLGDRRRDL
AHLAAEVEGK CLQSGFEMLK DVKSTLEKCE KVKTMEVTSV SIELEKNFSH FPRQYFALRK
ILKQLIADVT LDPETAHPNL VLSEDRKSVK FVETRLRDLP DTPQRFTFYP CVLATEGFTS
GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL TPLPETGYWR VRLWNGDKYA ATTTPFTPLH
IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT
IRPPTDWE
