ID A0A099YT20_TINGU Unreviewed; 356 AA.
AC A0A099YT20;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|RuleBase:RU364097};
DE AltName: Full=Bone proteoglycan II {ECO:0000256|RuleBase:RU364097};
DE Flags: Fragment;
GN ORFNames=N309_04882 {ECO:0000313|EMBL:KGL73424.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL73424.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL73424.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL73424.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU364097}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498, 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|RuleBase:RU364097}.
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DR EMBL; KL885926; KGL73424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099YT20; -.
DR STRING; 94827.A0A099YT20; -.
DR Proteomes; UP000053641; Unassembled WGS sequence.
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 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; SM00365; LRR_SD22; 4.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002490-1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530,
KW 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:UP000053641};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364097};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..356
FT /note="Decorin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012768436"
FT DOMAIN 50..82
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DISULFID 51..57
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 55..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 310..343
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KGL73424.1"
FT NON_TER 356
FT /evidence="ECO:0000313|EMBL:KGL73424.1"
SQ SEQUENCE 356 AA; 39507 MW; D918D33AD66EC004 CRC64;
KLAFLFVLLL PVCLAKPFHQ KGLFDFMLED EGSADLPPTE DPVISGFGPI CPFRCQCHLR
VVQCSDLGLD KVPRDLPPDT TLLDLQNNKI TEIKEGDFKN LKNLHALILV NNKISKISPA
AFAPLKKLER LYLSKNNLKE LPENMPKSLQ EIRAHENEIS KLRKAVFNGL NQVIVLELGT
NPLKSSGIEN GAFQGMKRLS YIRIADTNIT SIPKGLPPSL TELHLDGNKI NKIDADSLSG
LTNLAKLGLS FNSISSVENG SLNNVPHLRE LHLNNNELPR VPGGLGDHKY IQVVYLHNNK
IASVGINDFC PLGYNTKKAT YSGVSLFSNP VQYWEIQPSA FRCIHERSAV QIGNYK
//
