ID TRI17_RAT Reviewed; 477 AA.
AC Q9WV59;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM17;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM17 {ECO:0000305};
DE AltName: Full=Testis RING finger protein;
DE AltName: Full=Tripartite motif-containing protein 17;
GN Name=Trim17; Synonyms=Terf;
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 [MRNA].
RC TISSUE=Testis;
RX PubMed=9792805; DOI=10.1006/bbrc.1998.9502;
RA Ogawa S., Goto W., Orimo A., Hosoi T., Ouchi Y., Muramatsu M., Inoue S.;
RT "Molecular cloning of a novel RING finger-B box-coiled coil (RBCC) protein,
RT terf, expressed in the testis.";
RL Biochem. Biophys. Res. Commun. 251:515-519(1998).
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).
CC -!- FUNCTION: E3 ubiquitin ligase that plays important roles in the
CC regulation of neuronal apoptosis, selective autophagy or cell
CC proliferation. Stimulates the degradation of kinetochore ZW10
CC interacting protein ZWINT in a proteasome-dependent manner, leading to
CC negative regulation of cell proliferation. Inhibits autophagic
CC degradation of diverse known targets while contributing to autophagy of
CC midbodies. Autophagy-inhibitory activity involves MCL1, which TRIM17
CC assembles into complexes with the key autophagy regulator BECN1 (By
CC similarity). Controls neuronal apoptosis by mediating ubiquitination
CC and degradation of MCL1 to initiate neuronal death. In addition,
CC regulates NFAT transcription factors NFATC3 and NFATC4 activities by
CC preventing their nuclear localization, thus inhibiting their
CC transcriptional activities. Decreases TRIM41-mediated degradation of
CC ZSCAN2 thereby stimulating alpha-synuclein/SNCA transcription in
CC neuronal cells (By similarity). Prevents the E3 ubiquitin-ligase
CC activity of TRIM28 and its interaction with anti-apoptotic BCL2A1,
CC blocking TRIM28 from ubiquitinating BCL2A1 (By similarity).
CC {ECO:0000250|UniProtKB:Q7TPM3, ECO:0000250|UniProtKB:Q9Y577}.
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 (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 (By
CC similarity). {ECO:0000250|UniProtKB:Q7TPM3,
CC ECO:0000250|UniProtKB:Q9Y577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y577}.
CC Lysosome {ECO:0000250|UniProtKB:Q9Y577}.
CC -!- TISSUE SPECIFICITY: Expressed almost exclusively in the testis.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9Y577}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF156272; AAD40287.1; -; mRNA.
DR EMBL; BC078819; AAH78819.1; -; mRNA.
DR PIR; JE0343; JE0343.
DR RefSeq; NP_073635.1; NM_022798.2.
DR AlphaFoldDB; Q9WV59; -.
DR SMR; Q9WV59; -.
DR STRING; 10116.ENSRNOP00000060549; -.
DR PhosphoSitePlus; Q9WV59; -.
DR PaxDb; 10116-ENSRNOP00000003885; -.
DR Ensembl; ENSRNOT00000003885.6; ENSRNOP00000003885.3; ENSRNOG00000022983.6.
DR Ensembl; ENSRNOT00055051794; ENSRNOP00055042731; ENSRNOG00055029889.
DR Ensembl; ENSRNOT00060053900; ENSRNOP00060044706; ENSRNOG00060031045.
DR Ensembl; ENSRNOT00065013108; ENSRNOP00065009688; ENSRNOG00065008261.
DR GeneID; 64702; -.
DR KEGG; rno:64702; -.
DR UCSC; RGD:69290; rat.
DR AGR; RGD:69290; -.
DR CTD; 51127; -.
DR RGD; 69290; Trim17.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162155; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9WV59; -.
DR OMA; YPCVVGQ; -.
DR OrthoDB; 3453019at2759; -.
DR PhylomeDB; Q9WV59; -.
DR TreeFam; TF338674; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9WV59; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000022983; Expressed in testis and 19 other cell types or tissues.
DR ExpressionAtlas; Q9WV59; baseline and differential.
DR Genevisible; Q9WV59; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:RGD.
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:RGD.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
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:RGD.
DR CDD; cd19762; Bbox2_TRIM7-like; 1.
DR CDD; cd16595; RING-HC_TRIM17_C-IV; 1.
DR CDD; cd15812; SPRY_PRY_TRIM17; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR035687; TRIM17_PRY/SPRY.
DR InterPro; IPR027370; Znf-RING_euk.
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; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF397; E3 UBIQUITIN-PROTEIN LIGASE TRIM17; 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; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57850; RING/U-box; 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; 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_0000056226"
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..225
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"
SQ SEQUENCE 477 AA; 54954 MW; 1AAB42BB02615ADF CRC64;
MDAVELARRL QEEATCSICL DYFTDPVMTA CGHNFCRECI QMSWEKGKGK KGKKKQKGSF
PCPECREMSP QRNLRPNRLL TKVAEMARQH PGLHKRDLCQ IHQEPLKLFC QDDQTPICVV
CREAQEHRMH RVLPLDEAAR EYKLRLEEDI KYLREEMMKT ETLQAKEEQT LTEWQERVKE
RRERILEEFQ KVVLFLVEEE RRLLQILKKE EDDTLGKLQD SKASLDHQSR SLDLILLQLE
EQTQQEPLQM LQDVKDTLTR KESLSMQYPE VVLPVAIKTV CRVPGQIEVL KSFQEDVVPD
PSTAYPYLLL YESRQRRYLS PPPEGSAPYS KDRFLAYPCA VGQKSFSSGR HYWEVGMNLT
GDALWALGVC RDNVSRKDRV LKSPENGFWV VQLSKGKKHL PLLPNSIPVT LTEPPSHMGI
FLDFQAGEVS FYSVNDGSHL HSFSQVAFPG PLLPFFCLGS PKSGQMVIST VTMWVKG
//
