ID   TRI40_PANTR             Reviewed;         229 AA.
AC   Q1XHT8; Q1XHT9;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=E3 ubiquitin ligase TRIM40;
DE            EC=2.3.2.27 {ECO:0000250|UniProtKB:Q6P9F5};
DE   AltName: Full=Probable E3 NEDD8-protein ligase;
GN   Name=TRIM40;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LYS-5.
RX   PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA   Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA   Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA   Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA   Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA   Inoko H., Bahram S.;
RT   "Rapid evolution of major histocompatibility complex class I genes in
RT   primates generates new disease alleles in humans via hitchhiking
RT   diversity.";
RL   Genetics 173:1555-1570(2006).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in the
CC       limitation of the innate immune response. Mediates inhibition of the
CC       RLR signaling pathway by ubiquitinating DDX58 and IFIH1 receptors,
CC       leading to their proteasomal degradation. Promotes also the neddylation
CC       of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B
CC       nuclear translocation and activation. {ECO:0000250|UniProtKB:Q6P9F5}.
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:Q6P9F5};
CC   -!- SUBUNIT: Interacts with NEDD8. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AB210209; BAE92831.1; -; Genomic_DNA.
DR   EMBL; AB210210; BAE92832.1; -; Genomic_DNA.
DR   RefSeq; NP_001065286.1; NM_001071818.1.
DR   AlphaFoldDB; Q1XHT8; -.
DR   SMR; Q1XHT8; -.
DR   PaxDb; Q1XHT8; -.
DR   GeneID; 742243; -.
DR   KEGG; ptr:742243; -.
DR   CTD; 135644; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   HOGENOM; CLU_013137_3_0_1; -.
DR   InParanoid; Q1XHT8; -.
DR   TreeFam; TF333491; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
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   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00184; RING; 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   Coiled coil; Metal-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..229
FT                   /note="E3 ubiquitin ligase TRIM40"
FT                   /id="PRO_0000235191"
FT   ZN_FING         14..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         66..107
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          107..154
FT                   /evidence="ECO:0000255"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   VARIANT         5
FT                   /note="Q -> K"
FT                   /evidence="ECO:0000269|PubMed:16702430"
FT                   /id="VAR_026387"
SQ   SEQUENCE   229 AA;  26004 MW;  F9DA1E85FB6DE153 CRC64;
     MIPLQKDNQE EGVCPICQES LKEAVSTNCG HLFCRVCLTQ HVEKASASGV FCCPLCRKPC
     SEEVLGTGYI CPNHQKRVCR FCEESRLLLC VECLVSPEHM SHHELTIENA LSHYKERLNR
     RSRKLRKDIA ELQRLKAQQE KKLQALQQWL GQLEHMPAEA ARILDISRAV TQLSSLVIDL
     ERTAKELDTN TLKNAGDLLN RSAPQKLEVI YPQLEKGVSE LLLQPPQKL