ID A4IIC2_XENTR Unreviewed; 364 AA.
AC A4IIC2;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 123.
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|EMBL:AAI35959.1,
GN ECO:0000313|Ensembl:ENSXETP00000059085,
GN ECO:0000313|RefSeq:NP_001093704.1, ECO:0000313|RefSeq:XP_031753378.1,
GN ECO:0000313|Xenbase:XB-GENE-485545};
GN Synonyms=cscd {ECO:0000313|RefSeq:NP_001093704.1,
GN ECO:0000313|RefSeq:XP_031753378.1}, dspg2
GN {ECO:0000313|RefSeq:NP_001093704.1,
GN ECO:0000313|RefSeq:XP_031753378.1}, pg40
GN {ECO:0000313|RefSeq:NP_001093704.1,
GN ECO:0000313|RefSeq:XP_031753378.1}, pgii
GN {ECO:0000313|RefSeq:NP_001093704.1,
GN ECO:0000313|RefSeq:XP_031753378.1}, pgs2
GN {ECO:0000313|RefSeq:NP_001093704.1,
GN ECO:0000313|RefSeq:XP_031753378.1}, slrr1b
GN {ECO:0000313|RefSeq:NP_001093704.1,
GN ECO:0000313|RefSeq:XP_031753378.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAI35959.1};
RN [1] {ECO:0000313|RefSeq:NP_001093704.1}
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:AAI35959.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole embryo {ECO:0000313|EMBL:AAI35959.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSXETP00000059085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000059085};
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [4] {ECO:0000313|Ensembl:ENSXETP00000059085}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAY-2020) to UniProtKB.
RN [5] {ECO:0000313|RefSeq:NP_001093704.1, ECO:0000313|RefSeq:XP_031753378.1}
RP IDENTIFICATION.
RC STRAIN=Nigerian {ECO:0000313|RefSeq:XP_031753378.1};
RC TISSUE=Liver and blood {ECO:0000313|RefSeq:XP_031753378.1};
RG RefSeq;
RL Submitted (NOV-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.
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; BC135958; AAI35959.1; -; mRNA.
DR RefSeq; NP_001093704.1; NM_001100234.1.
DR RefSeq; XP_012813830.1; XM_012958376.2.
DR RefSeq; XP_012813831.1; XM_012958377.2.
DR RefSeq; XP_031753378.1; XM_031897518.1.
DR STRING; 8364.ENSXETP00000047568; -.
DR PaxDb; 8364-ENSXETP00000047254; -.
DR DNASU; 100101716; -.
DR Ensembl; ENSXETT00000063928; ENSXETP00000059085; ENSXETG00000021847.
DR GeneID; 100101716; -.
DR KEGG; xtr:100101716; -.
DR AGR; Xenbase:XB-GENE-485545; -.
DR CTD; 1634; -.
DR Xenbase; XB-GENE-485545; dcn.
DR HOGENOM; CLU_000288_186_0_1; -.
DR OMA; PFHQKGL; -.
DR OrthoDB; 3953748at2759; -.
DR Reactome; R-XTR-1474228; Degradation of the extracellular matrix.
DR Reactome; R-XTR-1971475; A tetrasaccharide linker sequence is required for GAG synthesis.
DR Reactome; R-XTR-2022870; Chondroitin sulfate biosynthesis.
DR Reactome; R-XTR-2022923; Dermatan sulfate biosynthesis.
DR Reactome; R-XTR-2024101; CS/DS degradation.
DR Reactome; R-XTR-3000178; ECM proteoglycans.
DR Proteomes; UP000008143; Chromosome 3.
DR Bgee; ENSXETG00000021847; Expressed in skeletal muscle tissue and 15 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; SM00369; LRR_TYP; 8.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 2.
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:UP000008143};
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_5033207245"
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; 40165 MW; 75F8399E97C2C97B CRC64;
MKATIILFVL LPLCISKPFH QRGLFDFMLE DDASGDGSSL WPEPSLPTDG PTGPIGPICP
FRCQCHLRVV QCSDIGLEQV PKDIPSDTTL LDLQNNKITE IKEGDFKNLK NLHALILVNN
KIKSISPSAF ASLTKLERLY LSKNNLKDLP ANMPKSLQEL RVHENSITKL KKSVFDGLNN
MIVVELGTNP IESSGVEKGA FQGMKKLSYL RIADTNITSI PKGLPASLTE LHLDGNKIAK
VDSDSLNGLN NLAKLGLSYN NIITLENGTV TGVPHLRELH LDHNSLTQVP AGLGEHKYIQ
VVYLHNNKIS AVSTNDFCPL GYNTKKASYS GISLFSNPVQ YWEIQPATFR CVYERSAIQI
GNYK
//
