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TRI15_PIG
ID   TRI15_PIG               Reviewed;         461 AA.
AC   Q9TSW0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Tripartite motif-containing protein 15;
DE   AltName: Full=Zinc finger protein B7;
GN   Name=TRIM15; Synonyms=ZNFB7;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Large white;
RX   PubMed=11685460; DOI=10.1007/s002510100348;
RA   Renard C., Vaiman M., Chiannilkulchai N., Cattolico L., Robert C.,
RA   Chardon P.;
RT   "Sequence of the pig major histocompatibility region containing the
RT   classical class I genes.";
RL   Immunogenetics 53:490-500(2001).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AJ251829; CAB63933.1; -; Genomic_DNA.
DR   RefSeq; NP_001116680.1; NM_001123208.1.
DR   AlphaFoldDB; Q9TSW0; -.
DR   SMR; Q9TSW0; -.
DR   STRING; 9823.ENSSSCP00000001314; -.
DR   PaxDb; Q9TSW0; -.
DR   PRIDE; Q9TSW0; -.
DR   Ensembl; ENSSSCT00000058047; ENSSSCP00000048593; ENSSSCG00000001235.
DR   Ensembl; ENSSSCT00000080618; ENSSSCP00000073963; ENSSSCG00000001235.
DR   Ensembl; ENSSSCT00025037781; ENSSSCP00025015883; ENSSSCG00025027873.
DR   Ensembl; ENSSSCT00045037467; ENSSSCP00045026043; ENSSSCG00045021870.
DR   Ensembl; ENSSSCT00050106144; ENSSSCP00050046840; ENSSSCG00050077143.
DR   Ensembl; ENSSSCT00055061315; ENSSSCP00055049181; ENSSSCG00055030740.
DR   GeneID; 100144461; -.
DR   KEGG; ssc:100144461; -.
DR   CTD; 89870; -.
DR   VGNC; VGNC:94395; TRIM15.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000162589; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q9TSW0; -.
DR   OMA; EDTKCRE; -.
DR   OrthoDB; 423686at2759; -.
DR   TreeFam; TF342569; -.
DR   Proteomes; UP000008227; Chromosome 7.
DR   Proteomes; UP000314985; Unplaced.
DR   Bgee; ENSSSCG00000001235; Expressed in epididymis and 10 other tissues.
DR   ExpressionAtlas; Q9TSW0; baseline.
DR   Genevisible; Q9TSW0; SS.
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:0051092; P:positive 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; 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; 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   3: Inferred from homology;
KW   Coiled coil; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..461
FT                   /note="Tripartite motif-containing protein 15"
FT                   /id="PRO_0000056221"
FT   DOMAIN          272..461
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         12..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         74..115
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          123..230
FT                   /evidence="ECO:0000255"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         82
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         107
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ   SEQUENCE   461 AA;  51578 MW;  41DCD74E623FB324 CRC64;
     MPLTPSHKGA VCSDCQGRLE DAVTAACGHT FCRLCLPLPP QMGAQPSSRV LLCPVCQEKE
     QTEPVLVPVP LGPLGETYCE EHGEKIYFFC ENDAEFLCVF CREGPSHQAH AVGFLDEAIQ
     PYRDRLRGRL EALITERDEI EDMKSREDQK LQVLLAQIES KKRHVEATFE RLQQELGEQQ
     RLLLARLTEL ERQIWKERDK YISKLSEEVA RLGTQVKELE EKCQQPASEL LQDVRVNQSR
     CETKTFVSPE AISPDLVKKI RDLHRKILTL PEMLRAFSEN LVHHLETDSG IVTLDPLTAS
     PSLVLSEDRK SVRYTRQKQN LPDSPLRFEG LPVVLGSPGF SSGRHRWQVE VQLGEGGGCT
     VGVVGEEVRR KGEQGLSAEE GVWAVILSHQ QCWASTSPGT DLPLSEIPRR VGVALDYEAG
     RVALLNAETR APIFTFAASF SGKVFPFFAV WKKGSCLTLK G
 
 
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