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