P51884 (LUM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lumican

Alternative name(s):
Keratan sulfate proteoglycan lumican
Short name=KSPG lumican

Gene names

Name:	LUM
Synonyms:	LDC, SLRR2D

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	338 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Binds to laminin By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Cornea and other tissues.
Developmental stage	Present in the extracellular matrix of human articular cartilage at all ages, although its abundance is far greater in the adult. In the adult cartilage lumican exists predominantly in a glycoprotein form lacking keratan sulfate, whereas the juvenile form of the molecule is a proteoglycan.
Post-translational modification	Sulfated on tyrosine residue(s).
Sequence similarities	Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily. Contains 11 LRR (leucine-rich) repeats. Contains 1 LRRNT domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan Pyrrolidone carboxylic acid Sulfation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome cartilage development Inferred from electronic annotation. Source: Compara collagen fibril organization Non-traceable author statement PubMed 10892350. Source: UniProtKB keratan sulfate biosynthetic process Traceable author statement. Source: Reactome keratan sulfate catabolic process Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara response to growth factor stimulus Inferred from electronic annotation. Source: Compara response to organic cyclic compound Inferred from electronic annotation. Source: Compara visual perception Traceable author statement PubMed 10802664. Source: ProtInc
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL fibrillar collagen Inferred from direct assay PubMed 10734230. Source: UniProtKB lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	collagen binding Inferred from direct assay PubMed 10892350. Source: UniProtKB extracellular matrix structural constituent Non-traceable author statement PubMed 10892350. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18
	Chain	19 – 338	320	Lumican		PRO_0000032733
Regions
	Domain	28 – 66	39	LRRNT
	Repeat	67 – 88	22	LRR 1
	Repeat	91 – 114	24	LRR 2
	Repeat	117 – 137	21	LRR 3
	Repeat	138 – 159	22	LRR 4
	Repeat	160 – 181	22	LRR 5
	Repeat	185 – 205	21	LRR 6
	Repeat	206 – 227	22	LRR 7
	Repeat	230 – 253	24	LRR 8
	Repeat	255 – 276	22	LRR 9
	Repeat	277 – 296	20	LRR 10
	Repeat	305 – 326	22	LRR 11
	Compositional bias	37 – 53	17	Cys-rich
Amino acid modifications
	Modified residue	19	1	Pyrrolidone carboxylic acid
	Modified residue	20	1	Sulfotyrosine By similarity
	Modified residue	21	1	Sulfotyrosine By similarity
	Modified residue	23	1	Sulfotyrosine By similarity
	Modified residue	30	1	Sulfotyrosine By similarity
	Glycosylation	88	1	N-linked (GlcNAc...) (keratan sulfate) Ref.8 Ref.9 Ref.10
	Glycosylation	127	1	N-linked (GlcNAc...) (keratan sulfate) Potential
	Glycosylation	160	1	N-linked (GlcNAc...) (keratan sulfate) Ref.8 Ref.9 Ref.10
	Glycosylation	252	1	N-linked (GlcNAc...) (keratan sulfate) Potential
	Disulfide bond	295 ↔ 328		By similarity
Natural variations
	Natural variant	199	1	L → P Found in patients with amyotrophic lateral sclerosis. Ref.11		VAR_065763
Experimental info
	Sequence conflict	27	1	L → P in AAA85268. Ref.1
	Sequence conflict	101	1	L → V in AAA85268. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51884 [UniParc]. Last modified January 23, 2002. Version 2. Checksum: 905D2EBD370CC59D	FASTA	338	38,429
	10 20 30 40 50 60 MSLSAFTLFL ALIGGTSGQY YDYDFPLSIY GQSSPNCAPE CNCPESYPSA MYCDELKLKS 70 80 90 100 110 120 VPMVPPGIKY LYLRNNQIDH IDEKAFENVT DLQWLILDHN LLENSKIKGR VFSKLKQLKK 130 140 150 160 170 180 LHINHNNLTE SVGPLPKSLE DLQLTHNKIT KLGSFEGLVN LTFIHLQHNR LKEDAVSAAF 190 200 210 220 230 240 KGLKSLEYLD LSFNQIARLP SGLPVSLLTL YLDNNKISNI PDEYFKRFNA LQYLRLSHNE 250 260 270 280 290 300 LADSGIPGNS FNVSSLVELD LSYNKLKNIP TVNENLENYY LEVNQLEKFD IKSFCKILGP 310 320 330 LSYSKIKHLR LDGNRISETS LPPDMYECLR VANEVTLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The human lumican gene. Organization, chromosomal location, and expression in articular cartilage." Grover J., Chen X.-N., Korenberg J.R., Roughley P.J. J. Biol. Chem. 270:21942-21949(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cartilage, Intestine and Placenta.
[2]	"Primary structure of human lumican (keratan sulfate proteoglycan) and localization of the gene (LUM) to chromosome 12q21.3-q22." Chakravarti S., Stallings R.L., Sundar-Raj N., Cornuet P.K., Hassell J.R. Genomics 27:481-488(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Cornea.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Lung and Prostate.
[7]	"Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry." Onnerfjord P., Heathfield T.F., Heinegaard D. J. Biol. Chem. 279:26-33(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION, PYROGLUTAMATE FORMATION AT GLN-19, MASS SPECTROMETRY.
[8]	"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry." Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R. Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88 AND ASN-160, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 AND ASN-252, MASS SPECTROMETRY. Tissue: Plasma.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 AND ASN-252, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Resequencing of 29 candidate genes in patients with familial and sporadic amyotrophic lateral sclerosis." Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D., Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A., Rouleau G.A. Arch. Neurol. 68:587-593(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PRO-199.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18728 mRNA. Translation: AAA85268.1. U21128 mRNA. Translation: AAA91639.1. BT006707 mRNA. Translation: AAP35353.1. AK312682 mRNA. Translation: BAG35562.1. CH471054 Genomic DNA. Translation: EAW97449.1. BC007038 mRNA. Translation: AAH07038.1. BC035997 mRNA. Translation: AAH35997.1.
IPI	IPI00020986.
RefSeq	NP_002336.1. NM_002345.3.
UniGene	Hs.406475.
3D structure databases
ProteinModelPortal	P51884.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51884. 2 interactions.
MINT	MINT-1422554.
STRING	9606.ENSP00000266718.
PTM databases
PhosphoSite	P51884.
Polymorphism databases
DMDM	20141464.
Proteomic databases
PaxDb	P51884.
PeptideAtlas	P51884.
PRIDE	P51884.
Protocols and materials databases
DNASU	4060.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266718; ENSP00000266718; ENSG00000139329.
GeneID	4060.
KEGG	hsa:4060.
UCSC	uc001tbm.3. human.
Organism-specific databases
CTD	4060.
GeneCards	GC12M091430.
HGNC	HGNC:6724. LUM.
HPA	CAB022193. HPA001522.
MIM	600616. gene.
neXtProt	NX_P51884.
PharmGKB	PA30486.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000234447.
HOVERGEN	HBG108061.
InParanoid	P51884.
KO	K08122.
OMA	LHINYNN.
OrthoDB	EOG4CZBGK.
PhylomeDB	P51884.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
Bgee	P51884.
CleanEx	HS_LUM.
Genevestigator	P51884.
GermOnline	ENSG00000139329. Homo sapiens.
Family and domain databases
InterPro	IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR000372. LRR-contain_N. IPR027219. Lumican. [Graphical view]
PANTHER	PTHR24371:SF1. PTHR24371:SF1. 1 hit.
Pfam	PF01462. LRRNT. 1 hit. [Graphical view]
SMART	SM00369. LRR_TYP. 1 hit. SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 10 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LUM. human.
GenomeRNAi	4060.
NextBio	15912.
PMAP-CutDB	P51884.
SOURCE	Search...

Entry information

Entry name

LUM_HUMAN

Accession

Primary (citable) accession number: P51884
Secondary accession number(s): B2R6R5, Q96QM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2002
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.