ID G3Q8G6_GASAC Unreviewed; 331 AA.
AC G3Q8G6;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|PIRNR:PIRNR002490};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000026180.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000026180.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000026180.1}
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.
CC {ECO:0000256|RuleBase:RU364097}.
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 AlphaFoldDB; G3Q8G6; -.
DR Ensembl; ENSGACT00000026231.1; ENSGACP00000026180.1; ENSGACG00000019806.1.
DR GeneTree; ENSGT00940000158382; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000019806; Expressed in zone of skin and 12 other cell types or tissues.
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; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
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:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU364097}.
FT DOMAIN 23..55
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DISULFID 24..30
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 28..37
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 283..316
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ SEQUENCE 331 AA; 36575 MW; EDD28679296EB2A1 CRC64;
MMEDEAGSGV PETPVPDINS GPRCPFRCQC HLRVIQCSDL GLTTIPEDIP DDTTLLDLQN
NKITEIKEND FKNLKGLHAL ILVNNKITII HAKALSPLTK LQRLYLSKNM LKEMPANMPK
SLQELRIHEN DITKIKKTSF QGLANIIVME LGSNPLRSAG IEASAFSDLK RVSYIRIADT
NITEIPKGLP SSLSELHLDG NKISKVTAGS LKGLKNLAKL GLSYNEISSV ENGTLANVPH
MRELHLDNNA LISVPAGLSD HKYIQVVYLH ANKIAAVGTE DFCPPGLNQK KAMYSGISLF
SNPVPYWEIP PITFRCVFDR SAIQLGNYRK K
//
