TRI16_PONAB
ID TRI16_PONAB Reviewed; 564 AA.
AC Q5R760;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM16;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O95361};
GN Name=TRIM16;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin ligase that plays an essential role in the
CC organization of autophagic response and ubiquitination upon lysosomal
CC and phagosomal damages. Plays a role in the stress-induced biogenesis
CC and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2
CC signaling and particularly by modulating the ubiquitination levels and
CC thus stability of NRF2. Acts as a scaffold protein and facilitates
CC autophagic degradation of protein aggregates by interacting with
CC p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell
CC against oxidative stress-induced cell death as a consequence of
CC endomembrane damage. {ECO:0000250|UniProtKB:O95361}.
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:0000250|UniProtKB:O95361};
CC -!- SUBUNIT: Homodimerizes via its coiled-coil domain. Heterodimerizes with
CC MID1, TRIM24 and PML. Interacts with Galectin-3/LGALS3 in a ULK1-
CC dependent manner; this interaction mediates autophagy of damage
CC endomembranes. Interacts with BECN1. Interacts with ATG16L1. Interacts
CC with p62/SQSTM and LC3B/MAP1LC3B. {ECO:0000250|UniProtKB:O95361}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95361}.
CC -!- PTM: Phosphorylated by ULK1. {ECO:0000250|UniProtKB:O95361}.
CC -!- PTM: Auto-ubiquitinates via its B-Boxes.
CC {ECO:0000250|UniProtKB:O95361}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; CR860258; CAH92400.1; -; mRNA.
DR RefSeq; NP_001126416.1; NM_001132944.1.
DR AlphaFoldDB; Q5R760; -.
DR SMR; Q5R760; -.
DR STRING; 9601.ENSPPYP00000009005; -.
DR GeneID; 100173399; -.
DR KEGG; pon:100173399; -.
DR CTD; 10626; -.
DR eggNOG; ENOG502QRVY; Eukaryota.
DR InParanoid; Q5R760; -.
DR OrthoDB; 273204at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0019966; F:interleukin-1 binding; ISS:UniProtKB.
DR GO; GO:0032089; F:NACHT domain binding; ISS:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0060416; P:response to growth hormone; ISS:UniProtKB.
DR GO; GO:0046683; P:response to organophosphorus; ISS:UniProtKB.
DR GO; GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
DR Gene3D; 2.60.120.920; -; 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; IPR000315; Znf_B-box.
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; 2.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..564
FT /note="E3 ubiquitin-protein ligase TRIM16"
FT /id="PRO_0000314286"
FT DOMAIN 355..553
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 72..122
FT /note="B box-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 126..165
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..203
FT /evidence="ECO:0000255"
FT COILED 243..274
FT /evidence="ECO:0000255"
FT COILED 320..340
FT /evidence="ECO:0000255"
FT COMPBIAS 13..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95361"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95361"
SQ SEQUENCE 564 AA; 63965 MW; 55760717937D8213 CRC64;
MAELDLMAPG PLPRATAQPP APLSPDSGSP SPDSGSASPV EEEDVGSSEK LGRETEEQDS
DPAEQGDPAG EGKEVLCDFC LDDTRRVKAV KSCLTCMVNY CEEHLQPHQV NIKLQSHLLT
EPVKDHNWRY CPAHHSPLSA FCCPDQQCIC QDCCQEHSGH TIVSLDAARR DKEAELQCTQ
LDLERKLKLN ENAISRLQAN QKSVLVSVSE VKAVAEMQFG ELLAAVRKAQ ANVMLFLEEK
EQAALSQANG IKAHLEYRSA EMEKSKQELE RMAAISNTVQ FLEEYCKFKN TEDITFPSVY
VGLKDKLSGI RKVITESTVH LIQLLENYKK KLQEFSKEEE YDIRTQVSAV VQRKYWTSKP
EPSTREQFLQ YAYDITFDPD TAHKYLRLQE ENRKVTNTTP WEHPYPDLPS RFLHWRQVLS
QQSLYLHRYY FEVEIFGAGT YVGLTCKGID RKGEERNSCI SGNNFSWSLQ WNGKEFTAWY
SDMETPLKAG PFRRLGVYID FPGGILSFYG VEYDTMTLVH KFACKFSEPV YAAFWLSKKE
NAIRIVDLGE EPEKPAPSLV GTAP
