LUM_BOVIN
ID LUM_BOVIN Reviewed; 342 AA.
AC Q05443; Q3T0T2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Lumican;
DE AltName: Full=Corneal keratan sulfate proteoglycan 37B core protein;
DE AltName: Full=Keratan sulfate proteoglycan;
DE Short=KSPG;
DE Flags: Precursor;
GN Name=LUM; Synonyms=LDC;
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], AND PROTEIN SEQUENCE OF 272-295.
RC TISSUE=Cornea;
RX PubMed=8099356; DOI=10.1016/s0021-9258(19)50281-2;
RA Funderburgh J.L., Funderburgh M.L., Brown S.J., Vergnes J.-P.,
RA Hassell J.R., Mann M.M., Conrad G.W.;
RT "Sequence and structural implications of a bovine corneal keratan sulfate
RT proteoglycan core protein. Protein 37B represents bovine lumican and
RT proteins 37A and 25 are unique.";
RL J. Biol. Chem. 268:11874-11880(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 19-42.
RX PubMed=2139877; DOI=10.1016/s0021-9258(19)39071-4;
RA Funderburgh J.L., Conrad G.W.;
RT "Isoforms of corneal keratan sulfate proteoglycan.";
RL J. Biol. Chem. 265:8297-8303(1990).
RN [4]
RP SULFATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14551184; DOI=10.1074/jbc.m308689200;
RA Onnerfjord P., Heathfield T.F., Heinegaard D.;
RT "Identification of tyrosine sulfation in extracellular leucine-rich repeat
RT proteins using mass spectrometry.";
RL J. Biol. Chem. 279:26-33(2004).
CC -!- SUBUNIT: Binds to laminin.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Cornea and other tissues.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000269|PubMed:14551184}.
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; L11063; AAA30608.1; -; mRNA.
DR EMBL; BC102271; AAI02272.1; -; mRNA.
DR PIR; A46743; A46743.
DR RefSeq; NP_776359.1; NM_173934.1.
DR RefSeq; XP_005206099.1; XM_005206042.2.
DR AlphaFoldDB; Q05443; -.
DR SMR; Q05443; -.
DR STRING; 9913.ENSBTAP00000002279; -.
DR PaxDb; Q05443; -.
DR PeptideAtlas; Q05443; -.
DR PRIDE; Q05443; -.
DR Ensembl; ENSBTAT00000002279; ENSBTAP00000002279; ENSBTAG00000001745.
DR GeneID; 280847; -.
DR KEGG; bta:280847; -.
DR CTD; 4060; -.
DR VEuPathDB; HostDB:ENSBTAG00000001745; -.
DR VGNC; VGNC:31081; LUM.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158177; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; Q05443; -.
DR OMA; DCPINFP; -.
DR OrthoDB; 968788at2759; -.
DR TreeFam; TF334562; -.
DR Reactome; R-BTA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-BTA-2022857; Keratan sulfate degradation.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000001745; Expressed in pigment epithelium of eye and 102 other tissues.
DR GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005583; C:fibrillar collagen trimer; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0030199; P:collagen fibril organization; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 9.
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; Phosphoprotein; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:2139877"
FT CHAIN 19..342
FT /note="Lumican"
FT /id="PRO_0000032732"
FT DOMAIN 32..70
FT /note="LRRNT"
FT REPEAT 71..92
FT /note="LRR 1"
FT REPEAT 95..118
FT /note="LRR 2"
FT REPEAT 121..141
FT /note="LRR 3"
FT REPEAT 142..163
FT /note="LRR 4"
FT REPEAT 164..185
FT /note="LRR 5"
FT REPEAT 189..209
FT /note="LRR 6"
FT REPEAT 210..231
FT /note="LRR 7"
FT REPEAT 234..254
FT /note="LRR 8"
FT REPEAT 259..280
FT /note="LRR 9"
FT REPEAT 281..300
FT /note="LRR 10"
FT REPEAT 309..330
FT /note="LRR 11"
FT MOD_RES 20
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 23
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 34
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51886"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 299..332
FT /evidence="ECO:0000250"
SQ SEQUENCE 342 AA; 38756 MW; 592DEE9A489AEB79 CRC64;
MNLGVFPLLL ALIGGASSTY PDYYEYYDFP QALYGRSSPN CAPECNCPES YPSAMYCDEL
KLKSVPMVPP GIKYLYLRNN QIDHIDDKAF ENVTDLQWLI LDHNLLENSK IKGKVFSKLK
QLKKLHINYN NLTESVGPLP KSLVDLQLTN NKISKLGSFD GLVNLTFIHL QHNQLKEDAV
SAALKGLKSL EYLDLSFNQM TKLPSGLPVS LLTLYLDNNK ISNIPDEYFK RFSALQYLRL
SHNELADSGV PGNSFNVSSL LELDLSYNKL KSIPTVNENL ENYYLEVNEL EKFDVKSFCK
ILGPLSYSKI KHLRLDGNHI TQTSLPPDMY ECLRVANEIT VN
