ID A0A2K6PQJ9_RHIRO Unreviewed; 250 AA.
AC A0A2K6PQJ9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|RuleBase:RU364097};
DE AltName: Full=Bone proteoglycan II {ECO:0000256|RuleBase:RU364097};
GN Name=DCN {ECO:0000313|Ensembl:ENSRROP00000018803.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000018803.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000018803.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May affect the rate of fibrils formation.
CC {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|RuleBase:RU364097}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class I subfamily. {ECO:0000256|RuleBase:RU364097}.
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DR AlphaFoldDB; A0A2K6PQJ9; -.
DR Ensembl; ENSRROT00000042965.1; ENSRROP00000018803.1; ENSRROG00000033436.1.
DR GeneTree; ENSGT00940000158382; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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 PANTHER; PTHR45712; AGAP008170-PA; 1.
DR PANTHER; PTHR45712:SF14; DECORIN; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 1.
PE 3: Inferred from homology;
KW Extracellular matrix {ECO:0000256|RuleBase:RU364097};
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:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364097};
KW Signal {ECO:0000256|RuleBase:RU364097}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|RuleBase:RU364097"
FT CHAIN 17..250
FT /note="Decorin"
FT /evidence="ECO:0000256|RuleBase:RU364097"
FT /id="PRO_5014211487"
FT DOMAIN 53..84
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
SQ SEQUENCE 250 AA; 27435 MW; D3881328E1C844E7 CRC64;
MKVTIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEL PDDRDFEPPL GPVCPFRCQC
HLRVVQCSDL ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITSIPQGL PPSLTELHLD
GNKISRVDAA SLKGLNNLAK LGLSFNSIST VDNGSLANTP HLRELHLDNN KLTRVPGGLA
EHKYIQVVYL HNNNISVVGS SDFCPPGHNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV
RSAIQLGNYK
//
