ID A0A2K5IBC2_COLAP Unreviewed; 359 AA.
AC A0A2K5IBC2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|RuleBase:RU364097};
DE AltName: Full=Bone proteoglycan II {ECO:0000256|RuleBase:RU364097};
OS Colobus angolensis palliatus (Peters' Angolan colobus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000013925.1, ECO:0000313|Proteomes:UP000233080};
RN [1] {ECO:0000313|Ensembl:ENSCANP00000013925.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. 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_011789045.1; XM_011933655.1.
DR AlphaFoldDB; A0A2K5IBC2; -.
DR STRING; 336983.ENSCANP00000013925; -.
DR Ensembl; ENSCANT00000036845.1; ENSCANP00000013925.1; ENSCANG00000030393.1.
DR GeneID; 105505716; -.
DR CTD; 1634; -.
DR OMA; PFHQKGL; -.
DR OrthoDB; 3953748at2759; -.
DR Proteomes; UP000233080; 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; 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|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:UP000233080};
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..359
FT /note="Decorin"
FT /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT ECO:0000256|RuleBase:RU364097"
FT /id="PRO_5014210169"
FT DOMAIN 53..85
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DISULFID 54..60
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 58..67
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 313..346
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ SEQUENCE 359 AA; 39859 MW; AC72B6849BF6D5E2 CRC64;
MKVTIILLLL AQVSWAGPFQ QRGLFDFMLE DEASGIGPEL PDDRDFEPPL GPVCPFRCQC
HLRVVQCSDL GLDKVPKDLP PDTTLLDLQN NKITEIKDGD FKNLKNLHAL ILVNNKISKI
SPGAFTPLVK LERLYLSKNQ LKELPEKMPK TLQELRAHEN EITKVRKTTF NGLNQMIVIE
LGTNPLKSAG IENGAFQGMK KLSYIRIADT NITSIPQGLP PSLTELHLDG NKISRVDAAS
LKGLNNLAKL GLSFNSISTV DNGSLANMPH LRELHLDNNK LTRVPGGLAE HKYIQVVYLH
NNNISVVGSS DFCPPGHNTK KASYSGVSLF SNPVQYWEIQ PSTFRCVYVR SAIQLGNYK
//
