ID A0A2U3ZZK6_TURTR Unreviewed; 360 AA.
AC A0A2U3ZZK6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-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_004329269.1,
GN ECO:0000313|RefSeq:XP_019774182.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019774182.1};
RN [1] {ECO:0000313|RefSeq:XP_004329269.1, ECO:0000313|RefSeq:XP_019774182.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_004329269.1,
RC ECO:0000313|RefSeq:XP_019774182.1};
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}.
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DR RefSeq; XP_004329269.1; XM_004329221.3.
DR RefSeq; XP_019774182.1; XM_019918623.2.
DR STRING; 9739.ENSTTRP00000001260; -.
DR GeneID; 101328056; -.
DR OrthoDB; 3953748at2759; -.
DR Proteomes; UP000245320; Chromosome 11.
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:UP000245320};
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_5041477805"
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; 40027 MW; 9C0A91428BA0AE80 CRC64;
MKATFIFLLL AQVSWAGPFQ QKGLFDFMLE DEASGIGPDD RFHEVPELEP QVPVCPFRCQ
CHLRVVQCSD LGLEKVPKDL PPDTALLDLQ NNKITEIKDG DFKNLKNLHT LILINNKISK
ISPGAFAPLV KLERLYLSKN QLKELPEKMP KTLQELRVHE NEITKVRKSV LNGLNQLIVV
ELGTNPLKSS GIENGAFQGM KKLSYIRIAD TNITTIPQGL PPSLTELHLD GNKITKVDAA
SLKGLNNLAK LGLGFNSISA VDNDSLANTP HLRELHLNNN KLIKVPGGLA DHKYIQVVYL
HNNNISAIGP NDFCPPGYNT KKASYSGVSL FSNPVQYWEI QPSTFRCVYV RSAIQLGNYK
//
