KERA_MOUSE
ID KERA_MOUSE Reviewed; 351 AA.
AC O35367;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Keratocan;
DE Short=KTN;
DE AltName: Full=Keratan sulfate proteoglycan keratocan;
DE Flags: Precursor;
GN Name=Kera; Synonyms=Ktcn;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AKR/J X C57L/J; TISSUE=Eye;
RX PubMed=9530631; DOI=10.1007/s003359900757;
RA Dunlevy J.R., Chakravarti S., Gyalzen P., Vergnes J.-P., Hassell J.R.;
RT "Cloning and chromosomal localization of mouse keratocan, a corneal keratan
RT sulfate proteoglycan.";
RL Mamm. Genome 9:316-319(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Cornea;
RX PubMed=9712886; DOI=10.1074/jbc.273.35.22584;
RA Liu C.-Y., Shiraishi A., Kao C.W.-C., Converse R.L., Funderburgh J.L.,
RA Corpuz L.M., Conrad G.W., Kao W.W.-Y.;
RT "The cloning of mouse keratocan cDNA and genomic DNA and the
RT characterization of its expression during eye development.";
RL J. Biol. Chem. 273:22584-22588(1998).
CC -!- FUNCTION: May be important in developing and maintaining corneal
CC transparency and for the structure of the stromal matrix.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Selectively expressed in cornea of adult where it
CC is detected in keratocytes but not in scleral cells. In embryo, first
CC detected in periocular mesenchymal cells migrating toward developing
CC cornea on 13.5 dpc; expression gradually restricted to corneal stromal
CC cells on 14.5 to 18.5 dpc. Detected in scleral cells of 15.5 dpc but
CC not in 18.5 dpc embryos.
CC -!- PTM: Binds keratan sulfate chains.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; AF022256; AAC15505.1; -; mRNA.
DR EMBL; AF057301; AAC61257.1; -; Genomic_DNA.
DR CCDS; CCDS36044.1; -.
DR RefSeq; NP_032464.1; NM_008438.3.
DR RefSeq; XP_006513336.1; XM_006513273.3.
DR AlphaFoldDB; O35367; -.
DR SMR; O35367; -.
DR STRING; 10090.ENSMUSP00000100923; -.
DR GlyGen; O35367; 4 sites.
DR iPTMnet; O35367; -.
DR PhosphoSitePlus; O35367; -.
DR MaxQB; O35367; -.
DR PaxDb; O35367; -.
DR PRIDE; O35367; -.
DR ProteomicsDB; 263595; -.
DR Antibodypedia; 30000; 143 antibodies from 24 providers.
DR DNASU; 16545; -.
DR Ensembl; ENSMUST00000105286; ENSMUSP00000100923; ENSMUSG00000019932.
DR GeneID; 16545; -.
DR KEGG; mmu:16545; -.
DR UCSC; uc007gxa.1; mouse.
DR CTD; 11081; -.
DR MGI; MGI:1202398; Kera.
DR VEuPathDB; HostDB:ENSMUSG00000019932; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158968; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; O35367; -.
DR OMA; MECFCPP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O35367; -.
DR TreeFam; TF334562; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR BioGRID-ORCS; 16545; 1 hit in 72 CRISPR screens.
DR PRO; PR:O35367; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O35367; protein.
DR Bgee; ENSMUSG00000019932; Expressed in cornea and 91 other tissues.
DR ExpressionAtlas; O35367; baseline and differential.
DR Genevisible; O35367; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0061303; P:cornea development in camera-type eye; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 2.
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; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 6.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..351
FT /note="Keratocan"
FT /id="PRO_0000032749"
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..181
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...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..342
FT /evidence="ECO:0000250|UniProtKB:P21793"
SQ SEQUENCE 351 AA; 40404 MW; B0632B387864B98D CRC64;
MATPNCLILW VLLIADTVWT QSVRQAYEIQ DPEDWDVHDD FYCPRECFCP PSFPTALYCE
NRGLTEIPPI PSRIWYLYLE NNLIESIPEK PFENATQLRW INLNKNKITN YGIEKGALSQ
LKKLLFLFLE DNELEEVPSP LPRSLEQLQL ARNKVSRIPQ GTFSNLENLT LLDLQHNKLL
DNAFQRDTFK GLKNLMQLNM AKNALRNMPP RLPANTMQLF LDNNSIEGIP ENYFNVIPKV
AFLRLNHNKL SDAGLPSRGF DVSSILDLQL SYNQLTNFPR INANLQHLHL DHNKIKNVNM
SVICPTTLRA EQDAFIHGPQ LSYLRLDGNE IKPPIPIDLV ACFKLLQAFI I
