ID A0A2I3HVB9_NOMLE Unreviewed; 359 AA.
AC A0A2I3HVB9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|PIRNR:PIRNR002490};
GN Name=DCN {ECO:0000313|Ensembl:ENSNLEP00000047554.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000047554.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000047554.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000047554.1}
RP IDENTIFICATION.
RG Ensembl;
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; ADFV01186548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01186549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01186550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3HVB9; -.
DR STRING; 61853.ENSNLEP00000047554; -.
DR Ensembl; ENSNLET00000041023.1; ENSNLEP00000047554.1; ENSNLEG00000005597.2.
DR GeneTree; ENSGT00940000158382; -.
DR InParanoid; A0A2I3HVB9; -.
DR OMA; PFHQKGL; -.
DR OrthoDB; 3953748at2759; -.
DR Proteomes; UP000001073; Chromosome 10.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 6.
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:UP000001073};
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..359
FT /note="Decorin"
FT /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT ECO:0000256|RuleBase:RU364097"
FT /id="PRO_5013987982"
FT DOMAIN 53..85
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DISULFID 54..60
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 58..67
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 313..346
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ SEQUENCE 359 AA; 39787 MW; 1605E0814303121D CRC64;
MKATIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEV PDDRDFEPPL GPVCPFRCQC
HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKV
SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKVTF NGLNQMIVIE
LGTNPLKSSG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS
LKGLNNLAKL GLSFNSISAV DNGSLANMPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH
NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYK
//
