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Database: UniProt
Entry: A0A340WQB2_LIPVE
LinkDB: A0A340WQB2_LIPVE
Original site: A0A340WQB2_LIPVE 
ID   A0A340WQB2_LIPVE        Unreviewed;       360 AA.
AC   A0A340WQB2;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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|RefSeq:XP_007449165.1,
GN   ECO:0000313|RefSeq:XP_007449166.1, ECO:0000313|RefSeq:XP_007449167.1};
OS   Lipotes vexillifer (Yangtze river dolphin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Lipotidae; Lipotes.
OX   NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007449165.1};
RN   [1] {ECO:0000313|RefSeq:XP_007449165.1, ECO:0000313|RefSeq:XP_007449166.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May affect the rate of fibrils formation.
CC       {ECO:0000256|ARBA:ARBA00004025, 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   RefSeq; XP_007449165.1; XM_007449103.1.
DR   RefSeq; XP_007449166.1; XM_007449104.1.
DR   RefSeq; XP_007449167.1; XM_007449105.1.
DR   STRING; 118797.A0A340WQB2; -.
DR   GeneID; 103076411; -.
DR   KEGG; lve:103076411; -.
DR   CTD; 1634; -.
DR   OrthoDB; 3953748at2759; -.
DR   Proteomes; UP000265300; 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   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; 9.
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:UP000265300};
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..360
FT                   /note="Decorin"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT                   ECO:0000256|RuleBase:RU364097"
FT                   /id="PRO_5041477883"
FT   DOMAIN          54..86
FT                   /note="LRRNT"
FT                   /evidence="ECO:0000259|SMART:SM00013"
FT   DISULFID        55..61
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT   DISULFID        59..68
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT   DISULFID        314..347
FT                   /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ   SEQUENCE   360 AA;  39985 MW;  ACBD74624726AF1A CRC64;
     MKATFIFLLL AQVSWAGPFQ QKGLFDFMLE DEASGIGPDN RFHEVPELEP QVPVCPFRCQ
     CHLRVVQCSD LGLDKVPKDL PPDTALLDLQ NNKITEIKDG DFKNLKNLHT LILINNKISK
     ISPGAFAPLV KLERLYLSKN QLKELPEKMP KTLQELRVHE NEITKVRKSV LNGLNQLIVV
     ELGTNPLKSS GIESGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKVDAA
     SLKGLNNLAK LGLGFNSISA VDNDSLANTP HLRELHLNNN KLIKVPGGLA DHKYIQVVYL
     HNNNISAIGP NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK
//
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