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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
 
 
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