ID   LUM_COTJA               Reviewed;         343 AA.
AC   Q9DE67;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Lumican;
DE   AltName: Full=Keratan sulfate proteoglycan lumican;
DE            Short=KSPG lumican;
DE   Flags: Precursor;
GN   Name=LUM; Synonyms=LDC;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cornea;
RX   PubMed=11102759; DOI=10.1016/s0945-053x(00)00117-7;
RA   Corpuz L.M., Dunlevy J.R., Hassell J.R., Conrad A.H., Conrad G.W.;
RT   "Molecular cloning and relative tissue expression of decorin and lumican in
RT   embryonic quail cornea.";
RL   Matrix Biol. 19:699-704(2000).
CC   -!- SUBUNIT: Binds to laminin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- PTM: Binds keratan sulfate chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; AF125251; AAG48155.1; -; mRNA.
DR   RefSeq; NP_001310144.1; NM_001323215.1.
DR   AlphaFoldDB; Q9DE67; -.
DR   SMR; Q9DE67; -.
DR   Ensembl; ENSCJPT00005008308; ENSCJPP00005005065; ENSCJPG00005004898.
DR   GeneID; 107311489; -.
DR   KEGG; cjo:107311489; -.
DR   CTD; 4060; -.
DR   GeneTree; ENSGT00940000158177; -.
DR   OrthoDB; 968788at2759; -.
DR   Proteomes; UP000694412; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005583; C:fibrillar collagen trimer; IEA:Ensembl.
DR   GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR   GO; GO:0030199; P:collagen fibril organization; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IEA:Ensembl.
DR   GO; GO:0007601; P:visual perception; IEA:InterPro.
DR   Gene3D; 3.80.10.10; -; 3.
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; IPR027219; Lumican.
DR   PANTHER; PTHR45712:SF6; PTHR45712:SF6; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 10.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Proteoglycan; Pyrrolidone carboxylic acid; Reference proteome; Repeat;
KW   Secreted; Signal; Sulfation.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..343
FT                   /note="Lumican"
FT                   /id="PRO_0000032737"
FT   DOMAIN          31..69
FT                   /note="LRRNT"
FT   REPEAT          70..91
FT                   /note="LRR 1"
FT   REPEAT          94..117
FT                   /note="LRR 2"
FT   REPEAT          120..140
FT                   /note="LRR 3"
FT   REPEAT          141..162
FT                   /note="LRR 4"
FT   REPEAT          165..186
FT                   /note="LRR 5"
FT   REPEAT          190..211
FT                   /note="LRR 6"
FT   REPEAT          212..232
FT                   /note="LRR 7"
FT   REPEAT          235..255
FT                   /note="LRR 8"
FT   REPEAT          260..281
FT                   /note="LRR 9"
FT   REPEAT          282..301
FT                   /note="LRR 10"
FT   REPEAT          310..330
FT                   /note="LRR 11"
FT   MOD_RES         19
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         20
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         22
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        130
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        320
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        300..333
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   343 AA;  38642 MW;  A95199C7F32B7C4C CRC64;
     MTLNSLPIFL VLISGIFCQY DYGPADDYGY DPFGPSTAVC APECNCPLSY PTAMYCDNLK
     LKTIPIVPSG IKYLYLRNNM IESIEENTFD NVTDLQWLIL DHNHLENSKI KGRVFSKLKN
     LKKLHINYNN LTEAVGPLPK TLDDLQLSHN KITKVNPGAL EGLVNLTVIH LQNNQLKADS
     ISGAFKGLNS LLYLDLSFNQ LTKLPTGLPH SLLMLYFDNN QISNIPDEYF QGFKTLQYLR
     LSHNKLTDSG IPGNVFNITS LVELDLSFNQ LKSIPTVSEN LENFYLQVNK INKFPLSSFC
     KVVGPLTYSK ITHLRLDGNN LTRADLPQEM YNCLRVAAEI SLE