TRI17_BOVIN
ID TRI17_BOVIN Reviewed; 475 AA.
AC Q2T9Z0;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=Tripartite motif-containing protein 17;
GN Name=TRIM17;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q9Y577}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC111201; AAI11202.1; -; mRNA.
DR RefSeq; NP_001098481.1; NM_001105011.1.
DR AlphaFoldDB; Q2T9Z0; -.
DR SMR; Q2T9Z0; -.
DR STRING; 9913.ENSBTAP00000024853; -.
DR PaxDb; Q2T9Z0; -.
DR GeneID; 618634; -.
DR KEGG; bta:618634; -.
DR CTD; 51127; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q2T9Z0; -.
DR OrthoDB; 423686at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
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; IPR020457; Znf_B-box_chordata.
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; PR01406; BBOXZNFINGER.
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; Cytoplasm; Lysosome; Metal-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..475
FT /note="E3 ubiquitin-protein ligase TRIM17"
FT /id="PRO_0000247320"
FT DOMAIN 275..473
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..246
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 475 AA; 54888 MW; 8AC628A7805BF4ED CRC64;
MDAVELARKL QEEATCSICL DYFTDPVMTT CGHNFCRECI QLTWEKARGQ KKRRKRKGSF
PCPECRELSP QRNLRPNRLL TKVAEMVRQH PSPQSRDLCQ VHRELLKLFC EDDQRPICII
CRESQEHRPH RVVPIEEAVQ EYKLKLEEDM EHLREEMMKT EKLQAKEEHT LAEWQEKVKE
RRERIMVEFE KMGLFLMEEK QRLLQALKKE EEETVAKLQE STASLKQQSH SLERLLLQLE
DRNEHTPLQM LQDMKGLLSR KSSLSVQYPE ATSIMLKTIC RVPGQIEVLK SFQEDVVPDP
STAYPYLLLY ESRQRRYLST PMDGTPCGKD RFLAYPCAVG QEIYSSGRHY WEVGMNLTGD
ALWALGVCRD NVSRRNRVPK SPENGFWVVQ LCKGKRYAPA AFPPTPVTLA EPPSHMGIFL
DFEAGELAFY NANDGSHLHS YTQPAFPGPL QPFFCLGAPK SGQMVISTVT LWVKG
