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P51885

- LUM_MOUSE

UniProt

P51885 - LUM_MOUSE

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Protein
Lumican
Gene
Lum, Lcn, Ldc
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818
Add
BLAST
Chaini19 – 338320Lumican
PRO_0000032734Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

Contains 1 LRRNT domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571K → M in BAB29264. 1 Publication
Sequence conflicti109 – 1091G → E1 Publication
Sequence conflicti109 – 1091G → E1 Publication
Sequence conflicti293 – 2931S → T1 Publication
Sequence conflicti293 – 2931S → T1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

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