TRI15_PANTR
ID TRI15_PANTR Reviewed; 465 AA.
AC Q7YR33; Q1XHU6;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Tripartite motif-containing protein 15;
DE AltName: Full=Zinc finger protein B7;
GN Name=TRIM15; Synonyms=ZNFB7;
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].
RX PubMed=12799463; DOI=10.1073/pnas.1230533100;
RA Anzai T., Shiina T., Kimura N., Yanagiya K., Kohara S., Shigenari A.,
RA Yamagata T., Kulski J.K., Naruse T.K., Fujimori Y., Fukuzumi Y.,
RA Yamazaki M., Tashiro H., Iwamoto C., Umehara Y., Imanishi T., Meyer A.,
RA Ikeo K., Gojobori T., Bahram S., Inoko H.;
RT "Comparative sequencing of human and chimpanzee MHC class I regions unveils
RT insertions/deletions as the major path to genomic divergence.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7708-7713(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BA000041; BAC78184.1; -; Genomic_DNA.
DR EMBL; AB210201; BAE92822.1; -; Genomic_DNA.
DR EMBL; AB210202; BAE92824.1; -; Genomic_DNA.
DR RefSeq; NP_001038973.1; NM_001045508.1.
DR AlphaFoldDB; Q7YR33; -.
DR SMR; Q7YR33; -.
DR STRING; 9598.ENSPTRP00000044121; -.
DR PaxDb; Q7YR33; -.
DR Ensembl; ENSPTRT00000045204; ENSPTRP00000044121; ENSPTRG00000017920.
DR GeneID; 471954; -.
DR KEGG; ptr:471954; -.
DR CTD; 89870; -.
DR VGNC; VGNC:12728; TRIM15.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000162589; -.
DR InParanoid; Q7YR33; -.
DR OMA; EDTKCRE; -.
DR OrthoDB; 423686at2759; -.
DR TreeFam; TF342569; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000017920; Expressed in bone marrow 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; 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; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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_0000056220"
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; 52230 MW; B39A1392A9BC33A4 CRC64;
MPATPSLKVV HELPACTLCA GPLEDAVTVP CGHTFCRLCL PALSQMGAQS SGKILLCPLC
QEEEQAETPM APVPLGPLGE TYCEEHGEKI YFFCENDAEF LCVFCREGPT HQAHTVGFLD
EAIQPYRDRL RSRLEALSME RDEIEDVKCR EDQKLQVLLT QIESKKHQVE TAFERLQQEL
EQQRCLLLAR LRELEQQIWK ERDEYITKVS EEVTRLGAQV KELEEKCQQP ASELLQDVRV
NQSRCEMKTF VSPEAISPDL VKKIRDFHRK ILTLPEMMRM FSENLAHHLE IDSGVITLDP
QTASRSLVLS EDRKSVRYTR QKKNLPDSPL RFDGLPAVLG FPGFSSGRHR WQVDVQLGDG
GGCTVGVAGE GVRRKGEMGL SAEDGVWAVI ISHQQCWAST SPGTDLPLSE IPRGVRVALD
YEAGQVTLHN AQTQEPIFTF TASFSGKVFP FFAVWKKGSY LTLKG
