ID   TRI15_MACMU             Reviewed;         465 AA.
AC   Q5TM55;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Tripartite motif-containing protein 15;
GN   Name=TRIM15;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15269276; DOI=10.1093/molbev/msh216;
RA   Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT   "Rhesus macaque class I duplicon structures, organization, and evolution
RT   within the alpha block of the major histocompatibility complex.";
RL   Mol. Biol. Evol. 21:2079-2091(2004).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AB128049; BAD69771.1; -; Genomic_DNA.
DR   RefSeq; NP_001108420.1; NM_001114948.1.
DR   AlphaFoldDB; Q5TM55; -.
DR   SMR; Q5TM55; -.
DR   STRING; 9544.ENSMMUP00000003861; -.
DR   Ensembl; ENSMMUT00000004092; ENSMMUP00000003861; ENSMMUG00000002890.
DR   GeneID; 712497; -.
DR   KEGG; mcc:712497; -.
DR   CTD; 89870; -.
DR   VEuPathDB; HostDB:ENSMMUG00000002890; -.
DR   VGNC; VGNC:83958; TRIM15.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000162589; -.
DR   InParanoid; Q5TM55; -.
DR   OrthoDB; 423686at2759; -.
DR   Proteomes; UP000006718; Chromosome 4.
DR   Bgee; ENSMMUG00000002890; Expressed in colon and 1 other tissue.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
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:1901253; P:negative regulation of intracellular transport of viral material; IEA:Ensembl.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR   GO; GO:1900246; P:positive regulation of RIG-I signaling pathway; IEA:Ensembl.
DR   GO; GO:0032481; P:positive regulation of type I interferon production; IEA:Ensembl.
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:0044790; P:suppression of viral release by host; IEA:Ensembl.
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; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
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   Pfam; PF00097; zf-C3HC4; 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   3: Inferred from homology;
KW   Coiled coil; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..465
FT                   /note="Tripartite motif-containing protein 15"
FT                   /id="PRO_0000056219"
FT   DOMAIN          276..465
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         16..61
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         78..119
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          126..229
FT                   /evidence="ECO:0000255"
FT   BINDING         83
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         105
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"
SQ   SEQUENCE   465 AA;  52214 MW;  89ED1832FFFFD42F CRC64;
     MPSTPSLKVV HELPACTLCV GPLEDAVTAP CGHTFCRLCL PTLSQMGAQS SGKILLCPLC
     QEEEQAETPM APVPLGPLGE TYCEEHGEKI YFFCENDAEF LCVFCREGPT HQAHTVGFLD
     EAIQPYRDRL RSRLEALSME RDEIEDVKCR EDQKLQVLLT QIENKKHQVE AAFERLQQEL
     EQQRCLLLAR LRELEQQIWK ERDEYITKVS EEVSRLGAQV KELEEKCQQP ASELLQDIRV
     NQSRCEMKTF VSPEAISPDL VKKIRDFHRK ILTLPEMMRM FSENLAHHLE IDSGVITLDP
     QTASRSLVLS EDRKSVRYTR QKKNLPDSPL RFDGLPAVLG FPGFSSGRHR WQVDLQLGDG
     GGCTVGVAGE GVRRKGEMGL SAEDGVWAVI ISHQQCWAST SPGTDLPLSE IPRYVGVALD
     YEAGQVTLFN AQTQEPIFTF AASFSGKVFP FFAVWKKGSC LTLKG