TRI38_BOVIN
ID TRI38_BOVIN Reviewed; 460 AA.
AC Q58DK8;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM38 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O00635};
DE AltName: Full=Tripartite motif-containing protein 38;
GN Name=TRIM38 {ECO:0000250|UniProtKB:O00635};
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as
CC a regulator of innate immunity. Acts as a negative regulator of type I
CC interferon IFN-beta production by catalyzing 'Lys-48'-linked
CC polyubiquitination of AZI2/NAP1, leading to its degradation. Mediates
CC 'Lys-48'-linked polyubiquitination and proteasomal degradation of the
CC critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon
CC signaling. Acts as positive regulator of the cGAS-STING pathway by
CC acting as a E3 SUMO-protein ligase: mediates sumoylation of CGAS and
CC STING, preventing their degradation and thereby activating the innate
CC immune response to DNA virus (By similarity). Also acts as a negative
CC regulator of NF-kappa-B signaling independently of its E3 protein
CC ligase activity by promoting lysosome-dependent degradation of TAB2 and
CC TAB3 adapters (By similarity). {ECO:0000250|UniProtKB:O00635,
CC ECO:0000250|UniProtKB:Q5SZ99}.
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:Q5SZ99};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q5SZ99}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000250|UniProtKB:Q5SZ99}.
CC -!- SUBUNIT: Interacts (via B30.2/SPRY domain) with TAB2 and TAB3.
CC {ECO:0000250|UniProtKB:Q5SZ99}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5SZ99}.
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DR EMBL; BT021589; AAX46436.1; -; mRNA.
DR EMBL; BC104589; AAI04590.1; -; mRNA.
DR RefSeq; NP_001029746.1; NM_001034574.1.
DR RefSeq; XP_010816785.1; XM_010818483.2.
DR RefSeq; XP_015315443.1; XM_015459957.1.
DR AlphaFoldDB; Q58DK8; -.
DR SMR; Q58DK8; -.
DR STRING; 9913.ENSBTAP00000024658; -.
DR PaxDb; Q58DK8; -.
DR PRIDE; Q58DK8; -.
DR Ensembl; ENSBTAT00000024658; ENSBTAP00000024658; ENSBTAG00000018523.
DR GeneID; 531022; -.
DR KEGG; bta:531022; -.
DR CTD; 10475; -.
DR VEuPathDB; HostDB:ENSBTAG00000018523; -.
DR VGNC; VGNC:36333; TRIM38.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160468; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q58DK8; -.
DR OMA; RPYFRVY; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF342569; -.
DR UniPathway; UPA00143; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000018523; Expressed in blood and 107 other tissues.
DR ExpressionAtlas; Q58DK8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd15815; SPRY_PRY_TRIM38; 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; IPR035790; SPRY/PRY_TRIM38.
DR InterPro; IPR003877; SPRY_dom.
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; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 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 2: Evidence at transcript level;
KW Cytoplasm; Immunity; Innate immunity; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..460
FT /note="E3 ubiquitin-protein ligase TRIM38"
FT /id="PRO_0000245025"
FT DOMAIN 270..460
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 12..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 84..125
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00635"
SQ SEQUENCE 460 AA; 52990 MW; 9C7C760528963E09 CRC64;
MASKKMREEA TCSICLHLMT NAVSISCGHS YCHVCIVSFF ENLNRMTPGL KTFSCPQCRA
PFTMASLRPN KQLGNLIEVI KEMDQEMSCE EHGEKLHLFC EDEGQLICWL CDRGAQHKGH
ATALVEEACQ GYKEKLQQAV TKLRQLEEEC MNLKVFTAEQ ITKWNEKIEF QKQKIQSDFK
TLQRFLHEEE KSYLWKLEKE KEQTLRRLRD NEANLEQKNH ELQSHILELE NKCQGSAQKL
LQDVKDTLSR SWAVKLEQPE ALSLDLHTVC NVSELYFDVK KMLRRHQVSV TLDPETAHYE
LILSEDRRQV IRGCPQENLD NSSRRFSALP CILGYEGFTS GKHYFEVDVG EGTGWDLGVC
MENVQRDTVM PQTPQSGFWA IRRCKEGYVA LTSPLTSIHL TEKPLVVGIF LDFEAGVVSF
YNMTTGSHIF TFPKASFSDT LRPYFQVYLY SPLFLPPPDE
