ID Q66J59_XENLA Unreviewed; 364 AA.
AC Q66J59;
DT 11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
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.L {ECO:0000313|RefSeq:NP_001087658.1,
GN ECO:0000313|RefSeq:XP_018106571.1, ECO:0000313|RefSeq:XP_041441107.1,
GN ECO:0000313|Xenbase:XB-GENE-864959};
GN Synonyms=cscd {ECO:0000313|RefSeq:NP_001087658.1,
GN ECO:0000313|RefSeq:XP_018106571.1}, dcn
GN {ECO:0000313|RefSeq:NP_001087658.1, ECO:0000313|RefSeq:XP_018106571.1,
GN ECO:0000313|RefSeq:XP_041441107.1,
GN ECO:0000313|Xenbase:XB-GENE-864959}, dspg2
GN {ECO:0000313|RefSeq:NP_001087658.1, ECO:0000313|RefSeq:XP_018106571.1,
GN ECO:0000313|RefSeq:XP_041441107.1}, MGC81824
GN {ECO:0000313|EMBL:AAH81050.1}, pg40
GN {ECO:0000313|RefSeq:NP_001087658.1,
GN ECO:0000313|RefSeq:XP_018106571.1}, pgii
GN {ECO:0000313|RefSeq:NP_001087658.1,
GN ECO:0000313|RefSeq:XP_018106571.1}, pgs2
GN {ECO:0000313|RefSeq:NP_001087658.1,
GN ECO:0000313|RefSeq:XP_018106571.1}, slrr1b
GN {ECO:0000313|RefSeq:NP_001087658.1, ECO:0000313|RefSeq:XP_018106571.1,
GN ECO:0000313|RefSeq:XP_041441107.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH81050.1};
RN [1] {ECO:0000313|RefSeq:NP_001087658.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH81050.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000313|EMBL:AAH81050.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:XP_018106571.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018106571.1,
RC ECO:0000313|RefSeq:XP_041441107.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018106571.1,
RC ECO:0000313|RefSeq:XP_041441107.1};
RG RefSeq;
RL Submitted (APR-2022) 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.
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 EMBL; BC081050; AAH81050.1; -; mRNA.
DR RefSeq; NP_001087658.1; NM_001094189.1.
DR RefSeq; XP_018106571.1; XM_018251082.2.
DR RefSeq; XP_041441107.1; XM_041585173.1.
DR STRING; 8355.Q66J59; -.
DR PaxDb; 8355-Q66J59; -.
DR DNASU; 447482; -.
DR GeneID; 447482; -.
DR KEGG; xla:447482; -.
DR AGR; Xenbase:XB-GENE-864959; -.
DR CTD; 447482; -.
DR Xenbase; XB-GENE-864959; dcn.L.
DR OMA; IITRCHS; -.
DR OrthoDB; 3953748at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 447482; Expressed in lung and 18 other cell types or tissues.
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; SM00365; LRR_SD22; 5.
DR SMART; SM00369; LRR_TYP; 7.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 3.
PE 2: Evidence at transcript level;
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:UP000186698};
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..364
FT /note="Decorin"
FT /evidence="ECO:0000256|PIRNR:PIRNR002490,
FT ECO:0000256|RuleBase:RU364097"
FT /id="PRO_5033206966"
FT DOMAIN 58..90
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DISULFID 59..65
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 63..72
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
FT DISULFID 318..351
FT /evidence="ECO:0000256|PIRSR:PIRSR002490-1"
SQ SEQUENCE 364 AA; 40208 MW; 71C83DDAF724E158 CRC64;
MKATIILFVL LPLCISKPFH QRGLFDFMLE DDASGDGSSL WPEPSLPTDG PTGPIGPICP
FRCQCHLRVV QCSDIGLEQV PKDIPSDTTL LDLQNNKITE IKDGDFKNLK NLHALILVNN
KIKSISPSAF ASLTKLERLY LSKNNLKDLP ANMPKSLQEL RVHENSITKL KKSVFDGLNN
MIVVELGTNP IESSGVEKGA FQGMKKLSYL RIADTNMTNI PKGLPSSLTE LHLDGNKIAK
IDSDSLNGLN NLAKLGLSYN KIITIENGTV SGVPHLRELH LDHNALTQVP AGLGEHKYIQ
VVYLHNNKIA AVSTNDFCPL GYNTKKASYT GISLFSNPVQ YWEIQPATFR CVYERSAIQI
GNYK
//
