KERA_CHICK
ID KERA_CHICK Reviewed; 353 AA.
AC O42235;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Keratocan;
DE Short=KTN;
DE AltName: Full=Keratan sulfate proteoglycan keratocan;
DE Flags: Precursor;
GN Name=KERA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 74-92; 212-220 AND 250-267,
RP AND GLYCOSYLATION AT ASN-94; ASN-223 AND ASN-261.
RC TISSUE=Cornea;
RX PubMed=9545293; DOI=10.1074/jbc.273.16.9615;
RA Dunlevy J.R., Neame P.J., Vergnes J.-P., Hassell J.R.;
RT "Identification of the N-linked oligosaccharide sites in chick corneal
RT lumican and keratocan that receive keratan sulfate.";
RL J. Biol. Chem. 273:9615-9621(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10712821; DOI=10.1006/exer.1999.0789;
RA Dunlevy J.R., Beales M.P., Berryhill B.L., Cornuet P.K., Hassell J.R.;
RT "Expression of the keratan sulfate proteoglycans lumican, keratocan and
RT osteoglycin/mimecan during chick corneal development.";
RL Exp. Eye Res. 70:349-362(2000).
CC -!- FUNCTION: Plays an important role in generating and maintaining a
CC transparent matrix within the corneal stroma.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
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; AF022890; AAC15506.1; -; mRNA.
DR RefSeq; NP_989507.1; NM_204176.1.
DR RefSeq; XP_015139177.1; XM_015283691.1.
DR RefSeq; XP_015139185.1; XM_015283699.1.
DR RefSeq; XP_015139192.1; XM_015283706.1.
DR AlphaFoldDB; O42235; -.
DR SMR; O42235; -.
DR STRING; 9031.ENSGALP00000018369; -.
DR iPTMnet; O42235; -.
DR PaxDb; O42235; -.
DR Ensembl; ENSGALT00000018391; ENSGALP00000018369; ENSGALG00000011270.
DR Ensembl; ENSGALT00000061247; ENSGALP00000043919; ENSGALG00000011270.
DR Ensembl; ENSGALT00000085113; ENSGALP00000064476; ENSGALG00000011270.
DR GeneID; 373995; -.
DR KEGG; gga:373995; -.
DR CTD; 11081; -.
DR VEuPathDB; HostDB:geneid_373995; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158968; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; O42235; -.
DR OMA; MECFCPP; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O42235; -.
DR TreeFam; TF334562; -.
DR Reactome; R-GGA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-GGA-2022857; Keratan sulfate degradation.
DR PRO; PR:O42235; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000011270; Expressed in cerebellum.
DR ExpressionAtlas; O42235; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..353
FT /note="Keratocan"
FT /id="PRO_0000032750"
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..262
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:0000269|PubMed:9545293"
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:0000269|PubMed:9545293"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:9545293"
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; 40266 MW; CBF42601FDF33ED6 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 SDDGIPPNGF NVSSILDLQL SHNQLTKIPP INAHLEHLHL DHNRIKSVNG
TQICPVSIAV AEDYGLYGNI PRLRYLRLDG NEIQPPIPLD IMICFQLLQA VVI
