ID   KERA_COTJA              Reviewed;         353 AA.
AC   Q9DE66;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Keratocan;
DE            Short=KTN;
DE   AltName: Full=Keratan sulfate proteoglycan keratocan;
DE   Flags: Precursor;
GN   Name=KERA;
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, and Sclera;
RX   PubMed=11102758; DOI=10.1016/s0945-053x(00)00116-5;
RA   Corpuz L.M., Dunlevy J.R., Hassell J.R., Conrad A.H., Conrad G.W.;
RT   "Molecular cloning and relative tissue expression of keratocan and mimecan
RT   in embryonic quail cornea.";
RL   Matrix Biol. 19:693-698(2000).
CC   -!- FUNCTION: Plays an important role in generating and maintaining a
CC       transparent matrix within the corneal stroma. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Cornea.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; AF128223; AAG48156.1; -; mRNA.
DR   RefSeq; NP_001310134.1; NM_001323205.1.
DR   RefSeq; XP_015713487.1; XM_015858001.1.
DR   AlphaFoldDB; Q9DE66; -.
DR   SMR; Q9DE66; -.
DR   Ensembl; ENSCJPT00005008302; ENSCJPP00005005059; ENSCJPG00005004896.
DR   Ensembl; ENSCJPT00005008303; ENSCJPP00005005060; ENSCJPG00005004896.
DR   GeneID; 107311475; -.
DR   KEGG; cjo:107311475; -.
DR   CTD; 11081; -.
DR   GeneTree; ENSGT00940000158968; -.
DR   Proteomes; UP000694412; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0061303; P:cornea development in camera-type eye; IEA:Ensembl.
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   Pfam; PF13516; LRR_6; 2.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00369; LRR_TYP; 5.
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; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..353
FT                   /note="Keratocan"
FT                   /id="PRO_0000032751"
FT   DOMAIN          34..72
FT                   /note="LRRNT"
FT   REPEAT          73..94
FT                   /note="LRR 1"
FT   REPEAT          97..118
FT                   /note="LRR 2"
FT   REPEAT          123..143
FT                   /note="LRR 3"
FT   REPEAT          144..165
FT                   /note="LRR 4"
FT   REPEAT          168..188
FT                   /note="LRR 5"
FT   REPEAT          194..214
FT                   /note="LRR 6"
FT   REPEAT          215..236
FT                   /note="LRR 7"
FT   REPEAT          239..259
FT                   /note="LRR 8"
FT   REPEAT          264..283
FT                   /note="LRR 9"
FT   REPEAT          284..305
FT                   /note="LRR 10"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        43..49
FT                   /evidence="ECO:0000250|UniProtKB:P21793"
FT   DISULFID        47..59
FT                   /evidence="ECO:0000250|UniProtKB:P21793"
FT   DISULFID        304..344
FT                   /evidence="ECO:0000250|UniProtKB:P21793"
SQ   SEQUENCE   353 AA;  40280 MW;  DEE07614FC598F7D CRC64;
     MMTLKVCPSL LLLFLVHSVW TRTVRQVYNE LDPEHWSHYT FECPQECFCP PSFPNALYCD
     NKGLKEIPAI PARIWYLYLQ NNLIETISEK PFVNATHLRW INLNKNKITN NGIESGVLSK
     LKRLLYLFLE DNELEEVPAP LPVGLEQLRL ARNKISRIPE GVFSNLENLT MLDLHQNNLL
     DSALQSDTFQ GLNSLMQLNI AKNSLKKMPL SIPANTLQLF LDNNSIEVIP ENYFSAIPKV
     TFLRLNYNKL SDEGIPPNGF NVSSILDLQL SHNQLTKIPP INAHLEHLHL DHNRIKSVNG
     TQICPVSIAV AEDYGLYGNI PRLRYLRLDG NEIQPPIPLD IMICFQLLQA VVI