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Database: UniProt
Entry: G3HJG6_CRIGR
LinkDB: G3HJG6_CRIGR
Original site: G3HJG6_CRIGR 
ID   G3HJG6_CRIGR            Unreviewed;       362 AA.
AC   G3HJG6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|PIRNR:PIRNR002490};
GN   Name=Dcn {ECO:0000313|Ensembl:ENSCGRP00001020748.1,
GN   ECO:0000313|RefSeq:XP_027249931.1, ECO:0000313|RefSeq:XP_027249932.1};
GN   ORFNames=I79_010811 {ECO:0000313|EMBL:EGW02696.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW02696.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
RN   [2] {ECO:0000313|EMBL:EGW02696.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSCGRP00001020748.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [4] {ECO:0000313|RefSeq:XP_027249931.1, ECO:0000313|RefSeq:XP_027249932.1}
RP   IDENTIFICATION.
RC   STRAIN=17A/GY {ECO:0000313|RefSeq:XP_027249931.1,
RC   ECO:0000313|RefSeq:XP_027249932.1};
RC   TISSUE=Liver {ECO:0000313|RefSeq:XP_027249931.1,
RC   ECO:0000313|RefSeq:XP_027249932.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May affect the rate of fibrils formation.
CC       {ECO:0000256|PIRNR:PIRNR002490, ECO:0000256|RuleBase:RU364097}.
CC   -!- SUBUNIT: Binds to type I and type II collagen, fibronectin and TGF-
CC       beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT.
CC       {ECO:0000256|ARBA:ARBA00025855}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR002490,
CC       ECO:0000256|RuleBase:RU364097}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class I subfamily. {ECO:0000256|ARBA:ARBA00009811,
CC       ECO:0000256|PIRNR:PIRNR002490, ECO:0000256|RuleBase:RU364097}.
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DR   EMBL; JH000429; EGW02696.1; -; Genomic_DNA.
DR   RefSeq; XP_003503923.1; XM_003503875.3.
DR   RefSeq; XP_007627668.1; XM_007629478.1.
DR   RefSeq; XP_007627669.1; XM_007629479.1.
DR   RefSeq; XP_007642622.1; XM_007644432.1.
DR   RefSeq; XP_027249931.1; XM_027394130.2.
DR   RefSeq; XP_027249932.1; XM_027394131.2.
DR   STRING; 10029.G3HJG6; -.
DR   PaxDb; 10029-XP_007627668-1; -.
DR   Ensembl; ENSCGRT00001024992.1; ENSCGRP00001020748.1; ENSCGRG00001019795.1.
DR   GeneID; 100756152; -.
DR   KEGG; cge:100756152; -.
DR   CTD; 1634; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000158382; -.
DR   OMA; PFHQKGL; -.
DR   OrthoDB; 3953748at2759; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   Proteomes; UP000694386; Unplaced.
DR   Proteomes; UP001108280; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
DR   GO; GO:0005539; F:glycosaminoglycan binding; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR   GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   InterPro; IPR016352; SLRP_I_decor/aspor/byglycan.
DR   PANTHER; PTHR45712; AGAP008170-PA; 1.
DR   PANTHER; PTHR45712:SF14; DECORIN; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   PIRSF; PIRSF002490; SLRP_I; 1.
DR   SMART; SM00364; LRR_BAC; 4.
DR   SMART; SM00369; LRR_TYP; 7.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS51450; LRR; 2.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR002490-1};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW   ECO:0000256|PIRNR:PIRNR002490};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022974};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001075};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364097};
KW   Signal {ECO:0000256|PIRNR:PIRNR002490, ECO:0000256|RuleBase:RU364097}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT                   ECO:0000256|RuleBase:RU364097"
FT   CHAIN           17..362
FT                   /note="Decorin"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT                   ECO:0000256|RuleBase:RU364097"
FT                   /id="PRO_5041476988"
FT   DOMAIN          56..88
FT                   /note="LRRNT"
FT                   /evidence="ECO:0000259|SMART:SM00013"
FT   DISULFID        57..63
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT   DISULFID        61..70
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT   DISULFID        316..349
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ   SEQUENCE   362 AA;  40098 MW;  1CD63F9C55AD3DC4 CRC64;
     MKATLIFLLL AQVSWAGPFE QRGLFDFMLE DEASGVGPED SGFPPDLPHL EPLGPVCPFR
     CQCHLRVVQC SDLGLDKVPK DLPPDTTLLD LQNNKITEIK DGDFKNLKNL HTLILVNNKI
     NKISSGAFTP LVKLERLYLS KNQLKELPEK MPKTLQELRA HENEISKVRK TVFNGLNQMI
     VIELGTNPLK SSGIESGAFQ GMKRLSYIRI ADTNITAIPQ GLPPSLTELH LDGNKITKVD
     ASSLKGLTNL AKLGLSFNSI SAIDNGTLAN TPHLRELHLD NNKLIRVPGG LAEHKYIQVV
     YLHNNNISAV GSNDFCPPGY NTKKASYSGV SLFSNPVQYW EIQPSTFRCV YVRSAIQLGN
     YK
//
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