ID A0A2U3Z079_LEPWE Unreviewed; 360 AA.
AC A0A2U3Z079;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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_006749162.1,
GN ECO:0000313|RefSeq:XP_006749163.1};
OS Leptonychotes weddellii (Weddell seal) (Otaria weddellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Phocidae;
OC Leptonychotes.
OX NCBI_TaxID=9713 {ECO:0000313|Proteomes:UP000245341, ECO:0000313|RefSeq:XP_006749163.1};
RN [1] {ECO:0000313|RefSeq:XP_006749162.1, ECO:0000313|RefSeq:XP_006749163.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_006749162.1,
RC ECO:0000313|RefSeq:XP_006749163.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006749162.1; XM_006749099.2.
DR RefSeq; XP_006749163.1; XM_006749100.2.
DR STRING; 9713.A0A2U3Z079; -.
DR GeneID; 102727675; -.
DR KEGG; lww:102727675; -.
DR CTD; 1634; -.
DR OrthoDB; 3953748at2759; -.
DR Proteomes; UP000245341; 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; 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:UP000245341};
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_5041474830"
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; 39962 MW; 61371A2176787760 CRC64;
MKATVIFLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEE HAPVDSDLEP LGPVCPFRCQ
CHLRVVQCSD LGLEKVPKDL PPDTTLLDLQ NNKITEIKDG DFKNLKNLHT LILVNNKISK
ISPAAFTPLL KLQRLYLSKN HLKELPEKMP KTLQELRAHE NEITKVRKSV FNGLNQMIVV
ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLE SNKITKVDAS
SLKGLNNLAK LGLSFNSISA IDNGTLANTP HLRELHLDNN KLIKVPGGLA EHKYIQVVYL
HNNNISAVGS NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK
//
