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P51885

- LUM_MOUSE

UniProt

P51885 - LUM_MOUSE

Protein

Lumican

Gene

Lum

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (20 Jun 2002)
      Previous versions | rss
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    Functioni

    GO - Biological processi

    1. cartilage development Source: Ensembl
    2. collagen fibril organization Source: InterPro
    3. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    4. response to growth factor Source: Ensembl
    5. response to organic cyclic compound Source: Ensembl
    6. visual perception Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_198578. Keratan sulfate biosynthesis.
    REACT_198960. Keratan sulfate degradation.
    REACT_216309. Integrin cell surface interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lumican
    Alternative name(s):
    Keratan sulfate proteoglycan lumican
    Short name:
    KSPG lumican
    Gene namesi
    Name:Lum
    Synonyms:Lcn, Ldc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:109347. Lum.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: Ensembl
    2. fibrillar collagen trimer Source: Ensembl
    3. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Add
    BLAST
    Chaini19 – 338320LumicanPRO_0000032734Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
    Modified residuei20 – 201Sulfotyrosine1 Publication
    Modified residuei21 – 211Sulfotyrosine1 Publication
    Modified residuei23 – 231Sulfotyrosine1 Publication
    Modified residuei30 – 301Sulfotyrosine1 Publication
    Glycosylationi88 – 881N-linked (GlcNAc...) (keratan sulfate)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...) (keratan sulfate)Sequence Analysis
    Glycosylationi160 – 1601N-linked (GlcNAc...) (keratan sulfate)Sequence Analysis
    Glycosylationi252 – 2521N-linked (GlcNAc...) (keratan sulfate)Sequence Analysis
    Disulfide bondi295 ↔ 328By similarity

    Post-translational modificationi

    Cys-37, Cys-41, Cys-43 and Cys-53 are involved in disulfide bonds.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan, Pyrrolidone carboxylic acid, Sulfation

    Proteomic databases

    MaxQBiP51885.
    PaxDbiP51885.
    PRIDEiP51885.

    PTM databases

    PhosphoSiteiP51885.

    Expressioni

    Tissue specificityi

    Cornea and other tissues.

    Gene expression databases

    BgeeiP51885.
    CleanExiMM_LUM.
    GenevestigatoriP51885.

    Interactioni

    Subunit structurei

    Binds to laminin.By similarity

    Protein-protein interaction databases

    IntActiP51885. 1 interaction.
    MINTiMINT-4100731.

    Structurei

    3D structure databases

    ProteinModelPortaliP51885.
    SMRiP51885. Positions 43-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 6639LRRNTAdd
    BLAST
    Repeati67 – 8822LRR 1Add
    BLAST
    Repeati91 – 11424LRR 2Add
    BLAST
    Repeati117 – 13721LRR 3Add
    BLAST
    Repeati138 – 15922LRR 4Add
    BLAST
    Repeati160 – 18122LRR 5Add
    BLAST
    Repeati185 – 20521LRR 6Add
    BLAST
    Repeati206 – 22722LRR 7Add
    BLAST
    Repeati230 – 25021LRR 8Add
    BLAST
    Repeati255 – 27622LRR 9Add
    BLAST
    Repeati277 – 29620LRR 10Add
    BLAST
    Repeati305 – 32622LRR 11Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi37 – 5317Cys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 11 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    GeneTreeiENSGT00600000084286.
    HOGENOMiHOG000234447.
    HOVERGENiHBG108061.
    InParanoidiP51885.
    KOiK08122.
    OMAiKKLHINY.
    OrthoDBiEOG75F4DF.
    PhylomeDBiP51885.
    TreeFamiTF334562.

    Family and domain databases

    InterProiIPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR027219. Lumican.
    [Graphical view]
    PANTHERiPTHR24371:SF54. PTHR24371:SF54. 1 hit.
    PfamiPF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 10 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P51885-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVCAFSLAL ALVGSVSGQY YDYDIPLFMY GQISPNCAPE CNCPHSYPTA    50
    MYCDDLKLKS VPMVPPGIKY LYLRNNQIDH IDEKAFENVT DLQWLILDHN 100
    LLENSKIKGK VFSKLKQLKK LHINYNNLTE SVGPLPKSLQ DLQLTNNKIS 150
    KLGSFDGLVN LTFIYLQHNQ LKEDAVSASL KGLKSLEYLD LSFNQMSKLP 200
    AGLPTSLLTL YLDNNKISNI PDEYFKRFTG LQYLRLSHNE LADSGVPGNS 250
    FNISSLLELD LSYNKLKSIP TVNENLENYY LEVNELEKFD VKSFCKILGP 300
    LSYSKIKHLR LDGNPLTQSS LPPDMYECLR VANEITVN 338
    Length:338
    Mass (Da):38,265
    Last modified:June 20, 2002 - v2
    Checksum:iFF1E050C89779140
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571K → M in BAB29264. (PubMed:16141072)Curated
    Sequence conflicti109 – 1091G → E(PubMed:7558724)Curated
    Sequence conflicti109 – 1091G → E1 PublicationCurated
    Sequence conflicti293 – 2931S → T(PubMed:7558724)Curated
    Sequence conflicti293 – 2931S → T1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S79461 mRNA. Translation: AAB35361.1.
    AF013262 Genomic DNA. Translation: AAB87767.1.
    AK014312 mRNA. Translation: BAB29264.1.
    AK075737 mRNA. Translation: BAC35919.1.
    AK164774 mRNA. Translation: BAE37912.1.
    BC005550 mRNA. Translation: AAH05550.1.
    CCDSiCCDS24142.1.
    RefSeqiNP_032550.2. NM_008524.2.
    UniGeneiMm.18888.

    Genome annotation databases

    EnsembliENSMUST00000038160; ENSMUSP00000040877; ENSMUSG00000036446.
    GeneIDi17022.
    KEGGimmu:17022.
    UCSCiuc007gwz.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S79461 mRNA. Translation: AAB35361.1 .
    AF013262 Genomic DNA. Translation: AAB87767.1 .
    AK014312 mRNA. Translation: BAB29264.1 .
    AK075737 mRNA. Translation: BAC35919.1 .
    AK164774 mRNA. Translation: BAE37912.1 .
    BC005550 mRNA. Translation: AAH05550.1 .
    CCDSi CCDS24142.1.
    RefSeqi NP_032550.2. NM_008524.2.
    UniGenei Mm.18888.

    3D structure databases

    ProteinModelPortali P51885.
    SMRi P51885. Positions 43-329.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P51885. 1 interaction.
    MINTi MINT-4100731.

    PTM databases

    PhosphoSitei P51885.

    Proteomic databases

    MaxQBi P51885.
    PaxDbi P51885.
    PRIDEi P51885.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000038160 ; ENSMUSP00000040877 ; ENSMUSG00000036446 .
    GeneIDi 17022.
    KEGGi mmu:17022.
    UCSCi uc007gwz.2. mouse.

    Organism-specific databases

    CTDi 4060.
    MGIi MGI:109347. Lum.

    Phylogenomic databases

    eggNOGi COG4886.
    GeneTreei ENSGT00600000084286.
    HOGENOMi HOG000234447.
    HOVERGENi HBG108061.
    InParanoidi P51885.
    KOi K08122.
    OMAi KKLHINY.
    OrthoDBi EOG75F4DF.
    PhylomeDBi P51885.
    TreeFami TF334562.

    Enzyme and pathway databases

    Reactomei REACT_198578. Keratan sulfate biosynthesis.
    REACT_198960. Keratan sulfate degradation.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    NextBioi 291134.
    PROi P51885.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51885.
    CleanExi MM_LUM.
    Genevestigatori P51885.

    Family and domain databases

    InterProi IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR027219. Lumican.
    [Graphical view ]
    PANTHERi PTHR24371:SF54. PTHR24371:SF54. 1 hit.
    Pfami PF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 10 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence, molecular properties, and chromosomal mapping of mouse lumican."
      Funderburgh J.L., Funderburgh M.L., Hevelone N.D., Stech M.E., Justice M.J., Liu C.-Y., Kao W.W.-Y., Conrad G.W.
      Invest. Ophthalmol. Vis. Sci. 36:2296-2303(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Cornea.
    2. Ying S., Shiraishi A., Kao C.W.-C., Converse R.L., Funderburgh J.L., Swiergiel J., Roth M.R., Kao W.W.-Y.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cerebellum, Embryonic head and Mammary gland.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Mammary gland.
    5. "Determination of the sites of tyrosine O-sulfation in peptides and proteins."
      Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.
      Nat. Methods 4:583-588(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-52, SULFATION AT TYR-20; TYR-21; TYR-23 AND TYR-30, PYROGLUTAMATE FORMATION AT GLN-19, DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127.
      Strain: C57BL/6.
      Tissue: Plasma.
    7. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
      Bernhard O.K., Kapp E.A., Simpson R.J.
      J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-127 AND ASN-160.
      Strain: C57BL/6.
      Tissue: Plasma.

    Entry informationi

    Entry nameiLUM_MOUSE
    AccessioniPrimary (citable) accession number: P51885
    Secondary accession number(s): Q3TP25, Q99JZ3, Q9CXK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: June 20, 2002
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3