LUM_MOUSE
ID LUM_MOUSE Reviewed; 338 AA.
AC P51885; Q3TP25; Q99JZ3; Q9CXK0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 184.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cornea;
RX PubMed=7558724;
RA Funderburgh J.L., Funderburgh M.L., Hevelone N.D., Stech M.E.,
RA Justice M.J., Liu C.-Y., Kao W.W.-Y., Conrad G.W.;
RT "Sequence, molecular properties, and chromosomal mapping of mouse
RT lumican.";
RL Invest. Ophthalmol. Vis. Sci. 36:2296-2303(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Ying S., Shiraishi A., Kao C.W.-C., Converse R.L., Funderburgh J.L.,
RA Swiergiel J., Roth M.R., Kao W.W.-Y.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryonic head, and Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 [5]
RP PROTEIN SEQUENCE OF 29-52, SULFATION AT TYR-20; TYR-21; TYR-23 AND TYR-30,
RP PYROGLUTAMATE FORMATION AT GLN-19, DISULFIDE BONDS, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17558413; DOI=10.1038/nmeth1056;
RA Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.;
RT "Determination of the sites of tyrosine O-sulfation in peptides and
RT proteins.";
RL Nat. Methods 4:583-588(2007).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127 AND ASN-160.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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: Cys-37, Cys-41, Cys-43 and Cys-53 are involved in disulfide bonds.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; S79461; AAB35361.1; -; mRNA.
DR EMBL; AF013262; AAB87767.1; -; Genomic_DNA.
DR EMBL; AK014312; BAB29264.1; -; mRNA.
DR EMBL; AK075737; BAC35919.1; -; mRNA.
DR EMBL; AK164774; BAE37912.1; -; mRNA.
DR EMBL; BC005550; AAH05550.1; -; mRNA.
DR CCDS; CCDS24142.1; -.
DR RefSeq; NP_032550.2; NM_008524.2.
DR AlphaFoldDB; P51885; -.
DR SMR; P51885; -.
DR BioGRID; 201228; 3.
DR STRING; 10090.ENSMUSP00000040877; -.
DR GlyGen; P51885; 4 sites.
DR PhosphoSitePlus; P51885; -.
DR CPTAC; non-CPTAC-3358; -.
DR jPOST; P51885; -.
DR MaxQB; P51885; -.
DR PaxDb; P51885; -.
DR PeptideAtlas; P51885; -.
DR PRIDE; P51885; -.
DR ProteomicsDB; 290192; -.
DR Antibodypedia; 867; 392 antibodies from 34 providers.
DR DNASU; 17022; -.
DR Ensembl; ENSMUST00000038160; ENSMUSP00000040877; ENSMUSG00000036446.
DR GeneID; 17022; -.
DR KEGG; mmu:17022; -.
DR UCSC; uc007gwz.2; mouse.
DR CTD; 4060; -.
DR MGI; MGI:109347; Lum.
DR VEuPathDB; HostDB:ENSMUSG00000036446; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158177; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P51885; -.
DR OMA; DCPINFP; -.
DR OrthoDB; 968788at2759; -.
DR PhylomeDB; P51885; -.
DR TreeFam; TF334562; -.
DR Reactome; R-MMU-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR BioGRID-ORCS; 17022; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Lum; mouse.
DR PRO; PR:P51885; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P51885; protein.
DR Bgee; ENSMUSG00000036446; Expressed in vault of skull and 199 other tissues.
DR Genevisible; P51885; MM.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005583; C:fibrillar collagen trimer; ISO:MGI.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IMP:CACAO.
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 Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Leucine-rich repeat; Phosphoprotein; Proteoglycan;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..18
FT CHAIN 19..338
FT /note="Lumican"
FT /id="PRO_0000032734"
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:0000269|PubMed:17558413"
FT MOD_RES 20
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:17558413"
FT MOD_RES 21
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:17558413"
FT MOD_RES 23
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:17558413"
FT MOD_RES 30
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:17558413"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51886"
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"
FT CONFLICT 57
FT /note="K -> M (in Ref. 3; BAB29264)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="G -> E (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38265 MW; FF1E050C89779140 CRC64;
MNVCAFSLAL ALVGSVSGQY YDYDIPLFMY GQISPNCAPE CNCPHSYPTA MYCDDLKLKS
VPMVPPGIKY LYLRNNQIDH IDEKAFENVT DLQWLILDHN LLENSKIKGK VFSKLKQLKK
LHINYNNLTE SVGPLPKSLQ DLQLTNNKIS KLGSFDGLVN LTFIYLQHNQ LKEDAVSASL
KGLKSLEYLD LSFNQMSKLP AGLPTSLLTL YLDNNKISNI PDEYFKRFTG LQYLRLSHNE
LADSGVPGNS FNISSLLELD LSYNKLKSIP TVNENLENYY LEVNELEKFD VKSFCKILGP
LSYSKIKHLR LDGNPLTQSS LPPDMYECLR VANEITVN
