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CNPY3_BOVIN
ID   CNPY3_BOVIN             Reviewed;         282 AA.
AC   Q0P5N1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Protein canopy homolog 3;
DE   Flags: Precursor;
GN   Name=CNPY3;
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].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Toll-like receptor (TLR)-specific co-chaperone for HSP90B1.
CC       Required for proper TLR folding, except that of TLR3, and hence
CC       controls TLR exit from the endoplasmic reticulum. Consequently,
CC       required for both innate and adaptive immune responses (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with HSP90B1; this interaction is disrupted in the
CC       presence of ATP. Interacts with TLR1, TLR2, TLR4 and TLR9 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the canopy family. {ECO:0000305}.
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DR   EMBL; BC119829; AAI19830.1; -; mRNA.
DR   RefSeq; NP_001068907.1; NM_001075439.2.
DR   AlphaFoldDB; Q0P5N1; -.
DR   STRING; 9913.ENSBTAP00000021132; -.
DR   PRIDE; Q0P5N1; -.
DR   Ensembl; ENSBTAT00000021132; ENSBTAP00000021132; ENSBTAG00000015900.
DR   GeneID; 510220; -.
DR   KEGG; bta:510220; -.
DR   CTD; 10695; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015900; -.
DR   VGNC; VGNC:27527; CNPY3.
DR   eggNOG; KOG4052; Eukaryota.
DR   GeneTree; ENSGT00390000014072; -.
DR   InParanoid; Q0P5N1; -.
DR   OMA; DKACLDE; -.
DR   OrthoDB; 1412562at2759; -.
DR   Proteomes; UP000009136; Chromosome 23.
DR   Bgee; ENSBTAG00000015900; Expressed in monocyte and 106 other tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR021852; DUF3456.
DR   Pfam; PF11938; DUF3456; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Coiled coil; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Immunity; Innate immunity; Reference proteome; Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..282
FT                   /note="Protein canopy homolog 3"
FT                   /id="PRO_0000313779"
FT   DOMAIN          53..275
FT                   /note="Saposin B-type"
FT   REGION          221..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          159..185
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        250..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        55..212
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..200
FT                   /evidence="ECO:0000250"
FT   DISULFID        110..172
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  31388 MW;  5B06EF4D265335E7 CRC64;
     MEPLPEPASG PRPRPHRLLL LSLLLLLLPL LPAPELGPRQ ARAEDTDWVR LPSKCEVCKY
     VAVELKSAFE ETGKTKEVID TGYGILDRKA SGVKYTKSDL RLIEVTETIC KRLLDYSLHK
     ERTGSNRFAK GMSETFETLH NLVHKGVKVV MDIPYELWNE TSAEVADLKK QCDVLVEEFE
     EVIEDWYRNH QEEDLTQFLC ANHVLKGKDA SCLAEQWSGK KGDTAALGGK KSKKKSGRAK
     GLGGGSSKQR KELGDLDGDP SPEEDEGIQK ASPLTHSPPD EL
 
 
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