LUM_CHICK
ID LUM_CHICK Reviewed; 343 AA.
AC P51890;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Lumican;
DE AltName: Full=Keratan sulfate proteoglycan lumican;
DE Short=KSPG lumican;
DE Flags: Precursor;
GN Name=LUM; Synonyms=LDC;
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].
RX PubMed=1370446; DOI=10.1016/s0021-9258(18)48500-6;
RA Blochberger T.C., Vergnes J.-P., Hempel J., Hassell J.R.;
RT "cDNA to chick lumican (corneal keratan sulfate proteoglycan) reveals
RT homology to the small interstitial proteoglycan gene family and expression
RT in muscle and intestine.";
RL J. Biol. Chem. 267:347-352(1992).
RN [2]
RP PROTEIN SEQUENCE OF 79-85; 155-167 AND 246-256, AND GLYCOSYLATION AT
RP ASN-91; ASN-165 AND ASN-257.
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).
CC -!- SUBUNIT: Binds to laminin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Cornea and other tissues.
CC -!- PTM: Binds keratan sulfate chains.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M80584; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A41748; A41748.
DR RefSeq; NP_001263286.1; NM_001276357.1.
DR AlphaFoldDB; P51890; -.
DR SMR; P51890; -.
DR STRING; 9031.ENSGALP00000018370; -.
DR iPTMnet; P51890; -.
DR PaxDb; P51890; -.
DR Ensembl; ENSGALT00000018392; ENSGALP00000018370; ENSGALG00000011271.
DR GeneID; 417891; -.
DR KEGG; gga:417891; -.
DR CTD; 4060; -.
DR VEuPathDB; HostDB:geneid_417891; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158177; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P51890; -.
DR OMA; DCPINFP; -.
DR OrthoDB; 968788at2759; -.
DR PhylomeDB; P51890; -.
DR TreeFam; TF334562; -.
DR Reactome; R-GGA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-GGA-2022857; Keratan sulfate degradation.
DR PRO; PR:P51890; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000011271; Expressed in colon and 10 other tissues.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IEA:InterPro.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Proteoglycan;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..343
FT /note="Lumican"
FT /id="PRO_0000032736"
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:0000269|PubMed:9545293"
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:0000269|PubMed:9545293"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:9545293"
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; 0A3A68D6F4F63B8A CRC64;
MTLNSLPIFL VLISGIFCQY DYGPADDYGY DPFGPSTAVC APECNCPLSY PTAMYCDNLK
LKTIPIVPSG IKYLYLRNNM IEAIEENTFD NVTDLQWLIL DHNHLENSKI KGRVFSKLKN
LKKLHINYNN LTEAVGPLPK TLDDLQLSHN KITKVNPGAL EGLVNLTVIH LQNNQLKTDS
ISGAFKGLNS LLYLDLSFNQ LTKLPTGLPH SLLMLYFDNN QISNIPDEYF QGFKTLQYLR
LSHNKLTDSG IPGNVFNITS LVELDLSFNQ LKSIPTVSEN LENFYLQVNK INKFPLSSFC
KVVGPLTYSK ITHLRLDGNN LTRADLPQEM YNCLRVAADI SLE