LUM_RAT
ID LUM_RAT Reviewed; 338 AA.
AC P51886;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Lumican;
DE AltName: Full=Keratan sulfate proteoglycan lumican;
DE Short=KSPG lumican;
DE Flags: Precursor;
GN Name=Lum; Synonyms=Lcn, Ldc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Eye;
RA Krull N.B.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBUNIT: Binds to laminin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; X84039; CAA58858.1; -; mRNA.
DR EMBL; BC061878; AAH61878.1; -; mRNA.
DR PIR; S52284; S52284.
DR RefSeq; NP_112312.1; NM_031050.1.
DR AlphaFoldDB; P51886; -.
DR SMR; P51886; -.
DR BioGRID; 249579; 1.
DR STRING; 10116.ENSRNOP00000006109; -.
DR GlyGen; P51886; 4 sites.
DR iPTMnet; P51886; -.
DR PhosphoSitePlus; P51886; -.
DR PaxDb; P51886; -.
DR PRIDE; P51886; -.
DR Ensembl; ENSRNOT00000006109; ENSRNOP00000006109; ENSRNOG00000004610.
DR GeneID; 81682; -.
DR KEGG; rno:81682; -.
DR UCSC; RGD:620984; rat.
DR CTD; 4060; -.
DR RGD; 620984; Lum.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158177; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P51886; -.
DR OMA; DCPINFP; -.
DR OrthoDB; 968788at2759; -.
DR PhylomeDB; P51886; -.
DR TreeFam; TF334562; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-2022857; Keratan sulfate degradation.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR PRO; PR:P51886; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000004610; Expressed in esophagus and 19 other tissues.
DR Genevisible; P51886; RN.
DR GO; GO:0031012; C:extracellular matrix; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005583; C:fibrillar collagen trimer; ISO:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; IEP:RGD.
DR GO; GO:0030199; P:collagen fibril organization; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; ISO:RGD.
DR GO; GO:0070848; P:response to growth factor; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0007601; P:visual perception; IEA:InterPro.
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 InterPro; IPR027219; Lumican.
DR PANTHER; PTHR45712:SF6; PTHR45712:SF6; 1.
DR Pfam; PF13855; LRR_8; 3.
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 Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW Phosphoprotein; Proteoglycan; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation.
FT SIGNAL 1..18
FT /evidence="ECO:0000250"
FT CHAIN 19..338
FT /note="Lumican"
FT /id="PRO_0000032735"
FT DOMAIN 28..66
FT /note="LRRNT"
FT REPEAT 67..88
FT /note="LRR 1"
FT REPEAT 91..114
FT /note="LRR 2"
FT REPEAT 117..137
FT /note="LRR 3"
FT REPEAT 138..159
FT /note="LRR 4"
FT REPEAT 160..181
FT /note="LRR 5"
FT REPEAT 185..205
FT /note="LRR 6"
FT REPEAT 206..227
FT /note="LRR 7"
FT REPEAT 230..250
FT /note="LRR 8"
FT REPEAT 255..276
FT /note="LRR 9"
FT REPEAT 277..296
FT /note="LRR 10"
FT REPEAT 305..326
FT /note="LRR 11"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P51884"
FT MOD_RES 20
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 21
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 23
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 30
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 295..328
FT /evidence="ECO:0000250"
SQ SEQUENCE 338 AA; 38279 MW; 13442BAECC905585 CRC64;
MNVCTFTLVL ALVGSVSGQY YDYDAPLFMY GELSPNCAPE CNCPHSYPTA MYCDDLKLKS
VPMVPPGIKY LYLRNNQIDH IDEKAFENVT DLQWLILDHN LLENSKIKGK VFSKLKQLKK
LHINYNNLTE SVGPLPKSLQ DLQLANNKIS KLGSFDGLVN LTFIYLQHNQ LKEEAVSASL
KGLKSLEYLD LSFNQMSKLP AGLPTSLLTL YLDNNKITNI PDEYFNRFTG LQYLRLSHNE
LADSGVPGNS FNISSLLELD LSYNKLKSIP TVNENLENYY LEVNKLEKFD VKSFCKILGP
LSYSKIKHLR LDGNPLTQSS LPPDMYECLR VANEITVN
