TRI17_MOUSE
ID TRI17_MOUSE Reviewed; 477 AA.
AC Q7TPM3; A2AB82; Q99PP8;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM17;
DE EC=2.3.2.27 {ECO:0000269|PubMed:20559321};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM17 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 17;
GN Name=Trim17;
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].
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 383-477.
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [4]
RP FUNCTION, MUTAGENESIS OF CYS-16, CATALYTIC ACTIVITY, AND
RP AUTO-UBIQUITINATION.
RX PubMed=20559321; DOI=10.1038/cdd.2010.73;
RA Lassot I., Robbins I., Kristiansen M., Rahmeh R., Jaudon F., Magiera M.M.,
RA Mora S., Vanhille L., Lipkin A., Pettmann B., Ham J., Desagher S.;
RT "Trim17, a novel E3 ubiquitin-ligase, initiates neuronal apoptosis.";
RL Cell Death Differ. 17:1928-1941(2010).
RN [5]
RP FUNCTION.
RX PubMed=22976837; DOI=10.1038/cdd.2012.124;
RA Magiera M.M., Mora S., Mojsa B., Robbins I., Lassot I., Desagher S.;
RT "Trim17-mediated ubiquitination and degradation of Mcl-1 initiate apoptosis
RT in neurons.";
RL Cell Death Differ. 20:281-292(2013).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NFATC3 AND NFATC4, AND
RP INDUCTION BY NFATC3 AND JUN.
RX PubMed=25215946; DOI=10.1038/cdd.2014.141;
RA Mojsa B., Mora S., Bossowski J.P., Lassot I., Desagher S.;
RT "Control of neuronal apoptosis by reciprocal regulation of NFATc3 and
RT Trim17.";
RL Cell Death Differ. 22:274-286(2015).
RN [7]
RP FUNCTION, AND INTERACTION WITH TRIM41.
RX PubMed=30485814; DOI=10.1016/j.celrep.2018.11.002;
RA Lassot I., Mora S., Lesage S., Zieba B.A., Coque E., Condroyer C.,
RA Bossowski J.P., Mojsa B., Marelli C., Soulet C., Tesson C.,
RA Carballo-Carbajal I., Laguna A., Mangone G., Vila M., Brice A.,
RA Desagher S.;
RT "The E3 Ubiquitin Ligases TRIM17 and TRIM41 Modulate alpha-Synuclein
RT Expression by Regulating ZSCAN21.";
RL Cell Rep. 25:2484-2496.e9(2018).
CC -!- FUNCTION: E3 ubiquitin ligase that plays important roles in the
CC regulation of neuronal apoptosis, selective autophagy or cell
CC proliferation (PubMed:20559321, PubMed:22976837, PubMed:25215946).
CC Stimulates the degradation of kinetochore ZW10 interacting protein
CC ZWINT in a proteasome-dependent manner, leading to negative regulation
CC of cell proliferation. Inhibits autophagic degradation of diverse known
CC targets while contributing to autophagy of midbodies. Autophagy-
CC inhibitory activity involves MCL1, which TRIM17 assembles into
CC complexes with the key autophagy regulator BECN1 (By similarity).
CC Controls neuronal apoptosis by mediating ubiquitination and degradation
CC of MCL1 to initiate neuronal death (PubMed:22976837). In addition,
CC regulates NFAT transcription factors NFATC3 and NFATC4 activities by
CC preventing their nuclear localization, thus inhibiting their
CC transcriptional activities (PubMed:25215946). Decreases TRIM41-mediated
CC degradation of ZSCAN2 thereby stimulating alpha-synuclein/SNCA
CC transcription in neuronal cells (PubMed:30485814). Prevents the E3
CC ubiquitin-ligase activity of TRIM28 and its interaction with anti-
CC apoptotic BCL2A1, blocking TRIM28 from ubiquitinating BCL2A1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y577,
CC ECO:0000269|PubMed:20559321, ECO:0000269|PubMed:22976837,
CC ECO:0000269|PubMed:25215946, ECO:0000269|PubMed:30485814}.
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:0000269|PubMed:20559321};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts (via coiled coil) with TRIM44 (via coiled coil).
CC Interacts with TRIM28; this interaction prevents TRIM28 activity on
CC BCL2A1 (By similarity). Interacts with TRIM41; this interaction
CC prevents TRIM41 activity on ZSCAN2 (By similarity). Interacts with
CC BECN1 (By similarity). Interacts with NFATC3 and NFATC4; these
CC interactions prevent NFATC3 and NFATC4 nuclear localization
CC (PubMed:25215946). {ECO:0000250|UniProtKB:Q9Y577,
CC ECO:0000269|PubMed:25215946}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y577}.
CC Lysosome {ECO:0000250|UniProtKB:Q9Y577}.
CC -!- TISSUE SPECIFICITY: Almost exclusively in the testis.
CC -!- INDUCTION: By NFATC3 and JUN cooperation during neuronal apoptosis.
CC {ECO:0000269|PubMed:25215946}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:20559321}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AL662809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC055112; AAH55112.1; -; mRNA.
DR EMBL; AF220135; AAG53508.1; -; mRNA.
DR CCDS; CCDS24756.1; -.
DR RefSeq; NP_112449.1; NM_031172.3.
DR RefSeq; XP_006533874.1; XM_006533811.3.
DR RefSeq; XP_006533875.1; XM_006533812.3.
DR RefSeq; XP_011247459.1; XM_011249157.2.
DR AlphaFoldDB; Q7TPM3; -.
DR SMR; Q7TPM3; -.
DR BioGRID; 208111; 5.
DR STRING; 10090.ENSMUSP00000074639; -.
DR PhosphoSitePlus; Q7TPM3; -.
DR jPOST; Q7TPM3; -.
DR PaxDb; Q7TPM3; -.
DR PRIDE; Q7TPM3; -.
DR ProteomicsDB; 298295; -.
DR Antibodypedia; 20781; 170 antibodies from 24 providers.
DR DNASU; 56631; -.
DR Ensembl; ENSMUST00000075141; ENSMUSP00000074639; ENSMUSG00000036964.
DR GeneID; 56631; -.
DR KEGG; mmu:56631; -.
DR UCSC; uc007jcv.1; mouse.
DR CTD; 51127; -.
DR MGI; MGI:1861440; Trim17.
DR VEuPathDB; HostDB:ENSMUSG00000036964; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162155; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q7TPM3; -.
DR OMA; CAVGQKS; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q7TPM3; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56631; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Trim17; mouse.
DR PRO; PR:Q7TPM3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TPM3; protein.
DR Bgee; ENSMUSG00000036964; Expressed in seminiferous tubule of testis and 47 other tissues.
DR ExpressionAtlas; Q7TPM3; baseline and differential.
DR Genevisible; Q7TPM3; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor 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:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
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:0032880; P:regulation of protein localization; ISO:MGI.
DR CDD; cd15812; SPRY_PRY_TRIM17; 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; IPR003877; SPRY_dom.
DR InterPro; IPR032918; TRIM17.
DR InterPro; IPR035687; TRIM17_PRY/SPRY.
DR InterPro; IPR027370; Znf-RING_LisH.
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 PANTHER; PTHR24103:SF397; PTHR24103:SF397; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Lysosome; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..477
FT /note="E3 ubiquitin-protein ligase TRIM17"
FT /id="PRO_0000056225"
FT DOMAIN 276..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..66
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 94..135
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 135..226
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MUTAGEN 16
FT /note="C->A: Complete loss of auto-ubiquitination."
FT /evidence="ECO:0000269|PubMed:20559321"
SQ SEQUENCE 477 AA; 54863 MW; E05066304224A1AE CRC64;
MDAVELARRL QEEATCSICL DYFTDPVMTA CGHNFCRECI QMSWEKGKVK KGKKKQKGSF
PCPECREMSP QRNLRPNRLL TKVAEMARQH PGLQKRDLCQ AHQEPLKLFC QDDQSPICVV
CREAQEHRMH RVLPLDEAAR EYKLKLEEDI KYLREEMMKT ETLQAKEEQT LTEWQERVKE
RRERILEEFQ KVVLFLVEEE RRILQVLKKE EEDTLGKLQD SKASLDHQSR SLDLILLQLE
ERSQQEPLQM LQDVKDTLNR KESFSVQYPE VVLPAAIKTL CRVPGQIEVL KSFQEDVMPD
PSSAYPYLLL YESRQRRYLS PPPEGSAPYS KDRFVAYPCA VGQKSFSSGR HYWEVGMNLT
GDALWALGVC RDNVSRKDRV LKSPENGFWV VQLSKGKKQL SLLPNSTLVT LTEPPSHMGI
FLDFQAGEVS FYSVNDGSHL HSFSQAAFPG PLLPFFCLGA PKSGQMVIST VTMWVKG
