ID   CNPY3_XENLA             Reviewed;         243 AA.
AC   Q6GN40;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Protein canopy homolog 3;
DE   Flags: Precursor;
GN   Name=cnpy3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Toll-like receptor (TLR)-specific co-chaperone for HSP90B1.
CC       Required for proper TLR folding and hence controls TLR exit from the
CC       endoplasmic reticulum. Consequently, required for immune responses (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the canopy family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH73680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BC073680; AAH73680.1; ALT_INIT; mRNA.
DR   RefSeq; XP_018118274.1; XM_018262785.1.
DR   AlphaFoldDB; Q6GN40; -.
DR   GeneID; 443685; -.
DR   KEGG; xla:443685; -.
DR   AGR; Xenbase:XB-GENE-6251984; -.
DR   CTD; 443685; -.
DR   Xenbase; XB-GENE-6251984; cnpy3.L.
DR   OMA; CTNHVLK; -.
DR   OrthoDB; 2910833at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 443685; Expressed in gastrula and 19 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
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; Immunity;
KW   Innate immunity; Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..243
FT                   /note="Protein canopy homolog 3"
FT                   /id="PRO_0000313784"
FT   DOMAIN          27..236
FT                   /note="Saposin B-type"
FT   REGION          186..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          136..160
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        186..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        29..188
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..176
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..148
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   243 AA;  28170 MW;  58A8B3DA628BDB8C CRC64;
     MWFLFLLLPL WAGCAEPGDS EWVHLPSKCE VCKYVALELK SSFDETSRTR ELIDTRYGFL
     EDDKKKKKIK YTTSDIRLIE VTEGLCSRLL EYNLHKERTG SNRFAKGMSE TFQTLHHLVH
     KGVKVVMDIP YELWNETSAE VADMKKQCDV MMENYEEVIE DWYRNHQDED LSEFLCARHV
     LKGQDQSCLS EQGDSRKGDT GPSTGTKKQK KQGEKKNKSK KQNSGSKEEK KQMDQPMAAK
     EEL
//