ID A0A3Q3S5L7_9TELE Unreviewed; 362 AA.
AC A0A3Q3S5L7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Decorin {ECO:0000256|ARBA:ARBA00021503, ECO:0000256|PIRNR:PIRNR002490};
OS Mastacembelus armatus (zig-zag eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000017855.1, ECO:0000313|Proteomes:UP000261640};
RN [1] {ECO:0000313|Ensembl:ENSMAMP00000017855.1}
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; A0A3Q3S5L7; -.
DR STRING; 205130.ENSMAMP00000017855; -.
DR Ensembl; ENSMAMT00000018328.2; ENSMAMP00000017855.1; ENSMAMG00000012078.2.
DR GeneTree; ENSGT00940000158382; -.
DR InParanoid; A0A3Q3S5L7; -.
DR OrthoDB; 3953748at2759; -.
DR Proteomes; UP000261640; 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; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 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:UP000261640};
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..362
FT /note="Decorin"
FT /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT ECO:0000256|RuleBase:RU364097"
FT /id="PRO_5018377456"
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 362 AA; 39996 MW; 74D0537D55D80413 CRC64;
MRSACLSLLL VTACWALPFY QSDFLDIPME DEPGSGVTEA PPDEGFPIMP DGPKCPFRCQ
CHLRVIQCSD LGLKTVPGDI PDDTTLLDLQ NNKITEIKEN DFKNLKGLHA LILVNNKITI
IHPKALSPLT KLQRLYLSKN FLKDMPANMP KSLQELRIHE NEITKIKKAS FQGMANVIVM
ELGSNPLKSA GVEAGAFSDL KRVSYIRIAD TNITEIPKGL PSSLSELHLD GNKITKVTAD
TLKGLKTLAK LGLSYNEISS VENGTLANAP HLRELHLDNN ALTSVPPGLS DHKYIQVVYL
HANKIAAVGT EDFCPPGFNT KKAMYSGISL FSNPVPYWEV QPITFRCVFD RSAIQLGNYR
KK
//
