KERA_BOVIN
ID KERA_BOVIN Reviewed; 352 AA.
AC O62702; Q0VC34; Q28032;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Keratocan;
DE Short=KTN;
DE AltName: Full=Corneal keratan sulfate proteoglycan 37A core protein;
DE AltName: Full=Keratan sulfate proteoglycan keratocan;
DE Short=KSPG keratocan;
DE Flags: Precursor;
GN Name=KERA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cornea;
RX PubMed=8621655; DOI=10.1074/jbc.271.16.9759;
RA Corpuz L.M., Funderburgh J.L., Funderburgh M.L., Bottomley G.S.,
RA Prakash S., Conrad G.W.;
RT "Molecular cloning and tissue distribution of keratocan. Bovine corneal
RT keratan sulfate proteoglycan 37A.";
RL J. Biol. Chem. 271:9759-9763(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Cornea;
RX PubMed=9751803; DOI=10.1016/s0378-1119(98)00390-4;
RA Tasheva E.S., Funderburgh J.L., Corpuz L.M., Conrad G.W.;
RT "Cloning, characterization and tissue-specific expression of the gene
RT encoding bovine keratocan, a corneal keratan sulfate proteoglycan.";
RL Gene 218:63-68(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION.
RC TISSUE=Cornea;
RX PubMed=1907274; DOI=10.1016/s0021-9258(18)98671-0;
RA Funderburgh J.L., Funderburgh M.L., Mann M.M., Conrad G.W.;
RT "Unique glycosylation of three keratan sulfate proteoglycan isoforms.";
RL J. Biol. Chem. 266:14226-14231(1991).
CC -!- FUNCTION: May be important in developing and maintaining corneal
CC transparency and for the structure of the stromal matrix.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Abundant in cornea and sclera but also found in
CC other tissues. {ECO:0000269|PubMed:9751803}.
CC -!- PTM: Binds three long, highly sulfated keratan sulfate chains in the
CC cornea but short, non-sulfated poly(N-acetyllactosamine) chains in
CC other tissues.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; U48360; AAC48568.1; -; mRNA.
DR EMBL; AF036962; AAC69272.1; -; Genomic_DNA.
DR EMBL; BC120375; AAI20376.1; -; mRNA.
DR RefSeq; NP_776335.1; NM_173910.1.
DR RefSeq; XP_010803060.1; XM_010804758.2.
DR RefSeq; XP_015326371.1; XM_015470885.1.
DR AlphaFoldDB; O62702; -.
DR SMR; O62702; -.
DR STRING; 9913.ENSBTAP00000019066; -.
DR PaxDb; O62702; -.
DR GeneID; 280785; -.
DR KEGG; bta:280785; -.
DR CTD; 11081; -.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; O62702; -.
DR OrthoDB; 826997at2759; -.
DR TreeFam; TF334562; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 9.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Proteoglycan; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..352
FT /note="Keratocan"
FT /id="PRO_0000032747"
FT DOMAIN 33..71
FT /note="LRRNT"
FT REPEAT 72..93
FT /note="LRR 1"
FT REPEAT 96..117
FT /note="LRR 2"
FT REPEAT 122..142
FT /note="LRR 3"
FT REPEAT 143..164
FT /note="LRR 4"
FT REPEAT 167..180
FT /note="LRR 5"
FT REPEAT 193..214
FT /note="LRR 6"
FT REPEAT 215..235
FT /note="LRR 7"
FT REPEAT 238..258
FT /note="LRR 8"
FT REPEAT 263..282
FT /note="LRR 9"
FT REPEAT 283..304
FT /note="LRR 10"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..48
FT /evidence="ECO:0000250|UniProtKB:P21793"
FT DISULFID 46..58
FT /evidence="ECO:0000250|UniProtKB:P21793"
FT DISULFID 303..343
FT /evidence="ECO:0000250|UniProtKB:P21793"
FT CONFLICT 189
FT /note="K -> R (in Ref. 2; AAC69272)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="V -> L (in Ref. 3; AAI20376)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="H -> Y (in Ref. 3; AAI20376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 40406 MW; C16E4072CF4A85F0 CRC64;
MASTICFILW VVFVTDTVWT RSVRQVYEAS DPEDWTMHDF DCPRECFCPP SFPTALYCEN
RGLKEIPAIP SRIWYLYLEN NLIETIPEKP FENATQLRWI NLNKNKITNY GIEKGALSQL
KKLLFLFLED NELEEVPSPL PRSLEQLQLA RNKVSRIPQG TFSNLENLTL LDLQHNKLLD
NAFQRDTFKG LKNLMQLNMA KNALRNMPPR LPANTMQVFL DNNSIEGIPE NYFNVIPKVA
FLRLNHNKLS DAGLPSSGFN VSSILDLQLS HNQLTKVPKI SAHLQHLHLD HNKIRNVNVS
VICPSTPTTL PVEDSFSYGP HLRYLRLDGN EIKPPIPMDL MTCFRLLQAV II
