LUM_HUMAN
ID LUM_HUMAN Reviewed; 338 AA.
AC P51884; B2R6R5; Q96QM7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Lumican;
DE AltName: Full=Keratan sulfate proteoglycan lumican;
DE Short=KSPG lumican;
DE Flags: Precursor;
GN Name=LUM; Synonyms=LDC, SLRR2D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cartilage, Intestine, and Placenta;
RX PubMed=7665616; DOI=10.1074/jbc.270.37.21942;
RA Grover J., Chen X.-N., Korenberg J.R., Roughley P.J.;
RT "The human lumican gene. Organization, chromosomal location, and expression
RT in articular cartilage.";
RL J. Biol. Chem. 270:21942-21949(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Cornea;
RX PubMed=7558030; DOI=10.1006/geno.1995.1080;
RA Chakravarti S., Stallings R.L., Sundar-Raj N., Cornuet P.K., Hassell J.R.;
RT "Primary structure of human lumican (keratan sulfate proteoglycan) and
RT localization of the gene (LUM) to chromosome 12q21.3-q22.";
RL Genomics 27:481-488(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and 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 [7]
RP SULFATION, PYROGLUTAMATE FORMATION AT GLN-19, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=14551184; DOI=10.1074/jbc.m308689200;
RA Onnerfjord P., Heathfield T.F., Heinegaard D.;
RT "Identification of tyrosine sulfation in extracellular leucine-rich repeat
RT proteins using mass spectrometry.";
RL J. Biol. Chem. 279:26-33(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88 AND ASN-160.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 AND
RP ASN-252.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 AND
RP ASN-252.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP VARIANT PRO-199.
RX PubMed=21220648; DOI=10.1001/archneurol.2010.351;
RA Daoud H., Valdmanis P.N., Gros-Louis F., Belzil V., Spiegelman D.,
RA Henrion E., Diallo O., Desjarlais A., Gauthier J., Camu W., Dion P.A.,
RA Rouleau G.A.;
RT "Resequencing of 29 candidate genes in patients with familial and sporadic
RT amyotrophic lateral sclerosis.";
RL Arch. Neurol. 68:587-593(2011).
CC -!- SUBUNIT: Binds to laminin. {ECO:0000250}.
CC -!- INTERACTION:
CC P51884; Q92993: KAT5; NbExp=3; IntAct=EBI-725780, EBI-399080;
CC P51884; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-725780, EBI-11742507;
CC P51884; P50281: MMP14; NbExp=2; IntAct=EBI-725780, EBI-992788;
CC P51884; P17252: PRKCA; NbExp=3; IntAct=EBI-725780, EBI-1383528;
CC P51884; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-725780, EBI-9090795;
CC P51884; P61981: YWHAG; NbExp=3; IntAct=EBI-725780, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Cornea and other tissues.
CC -!- DEVELOPMENTAL STAGE: Present in the extracellular matrix of human
CC articular cartilage at all ages, although its abundance is far greater
CC in the adult. In the adult cartilage lumican exists predominantly in a
CC glycoprotein form lacking keratan sulfate, whereas the juvenile form of
CC the molecule is a proteoglycan.
CC -!- PTM: Sulfated on tyrosine residue(s). {ECO:0000269|PubMed:14551184}.
CC -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC family. SLRP class II subfamily. {ECO:0000305}.
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DR EMBL; U18728; AAA85268.1; -; mRNA.
DR EMBL; U21128; AAA91639.1; -; mRNA.
DR EMBL; BT006707; AAP35353.1; -; mRNA.
DR EMBL; AK312682; BAG35562.1; -; mRNA.
DR EMBL; CH471054; EAW97449.1; -; Genomic_DNA.
DR EMBL; BC007038; AAH07038.1; -; mRNA.
DR EMBL; BC035997; AAH35997.1; -; mRNA.
DR CCDS; CCDS9038.1; -.
DR RefSeq; NP_002336.1; NM_002345.3.
DR AlphaFoldDB; P51884; -.
DR SMR; P51884; -.
DR BioGRID; 110238; 23.
DR IntAct; P51884; 14.
DR MINT; P51884; -.
DR STRING; 9606.ENSP00000266718; -.
DR DrugBank; DB09130; Copper.
DR GlyConnect; 1470; 87 N-Linked glycans (4 sites).
DR GlyGen; P51884; 7 sites, 97 N-linked glycans (4 sites), 2 O-linked glycans (3 sites).
DR iPTMnet; P51884; -.
DR PhosphoSitePlus; P51884; -.
DR BioMuta; LUM; -.
DR DMDM; 20141464; -.
DR EPD; P51884; -.
DR jPOST; P51884; -.
DR MassIVE; P51884; -.
DR MaxQB; P51884; -.
DR PaxDb; P51884; -.
DR PeptideAtlas; P51884; -.
DR PRIDE; P51884; -.
DR ProteomicsDB; 56448; -.
DR TopDownProteomics; P51884; -.
DR ABCD; P51884; 7 sequenced antibodies.
DR Antibodypedia; 867; 392 antibodies from 34 providers.
DR DNASU; 4060; -.
DR Ensembl; ENST00000266718.5; ENSP00000266718.4; ENSG00000139329.5.
DR GeneID; 4060; -.
DR KEGG; hsa:4060; -.
DR MANE-Select; ENST00000266718.5; ENSP00000266718.4; NM_002345.4; NP_002336.1.
DR UCSC; uc001tbm.4; human.
DR CTD; 4060; -.
DR DisGeNET; 4060; -.
DR GeneCards; LUM; -.
DR HGNC; HGNC:6724; LUM.
DR HPA; ENSG00000139329; Tissue enhanced (gallbladder, placenta).
DR MIM; 600616; gene.
DR neXtProt; NX_P51884; -.
DR OpenTargets; ENSG00000139329; -.
DR PharmGKB; PA30486; -.
DR VEuPathDB; HostDB:ENSG00000139329; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158177; -.
DR HOGENOM; CLU_000288_186_4_1; -.
DR InParanoid; P51884; -.
DR OMA; DCPINFP; -.
DR OrthoDB; 968788at2759; -.
DR PhylomeDB; P51884; -.
DR TreeFam; TF334562; -.
DR PathwayCommons; P51884; -.
DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-HSA-2022857; Keratan sulfate degradation.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-3656225; Defective CHST6 causes MCDC1.
DR Reactome; R-HSA-3656243; Defective ST3GAL3 causes MCT12 and EIEE15.
DR Reactome; R-HSA-3656244; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d).
DR SignaLink; P51884; -.
DR BioGRID-ORCS; 4060; 11 hits in 1066 CRISPR screens.
DR ChiTaRS; LUM; human.
DR GeneWiki; LUM; -.
DR GenomeRNAi; 4060; -.
DR Pharos; P51884; Tbio.
DR PRO; PR:P51884; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P51884; protein.
DR Bgee; ENSG00000139329; Expressed in gall bladder and 181 other tissues.
DR ExpressionAtlas; P51884; baseline and differential.
DR Genevisible; P51884; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:ProtInc.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005583; C:fibrillar collagen trimer; IDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB.
DR GO; GO:0030021; F:extracellular matrix structural constituent conferring compression resistance; ISS:BHF-UCL.
DR GO; GO:0030199; P:collagen fibril organization; NAS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR Gene3D; 3.80.10.10; -; 3.
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; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 8.
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_0000032733"
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..253
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:14551184"
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:0000250|UniProtKB:P51886"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
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:0000269|PubMed:14760718,
FT ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 295..328
FT /evidence="ECO:0000250"
FT VARIANT 199
FT /note="L -> P (found in patients with amyotrophic lateral
FT sclerosis; dbSNP:rs147975710)"
FT /evidence="ECO:0000269|PubMed:21220648"
FT /id="VAR_065763"
FT CONFLICT 27
FT /note="L -> P (in Ref. 1; AAA85268)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="L -> V (in Ref. 1; AAA85268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 38429 MW; 905D2EBD370CC59D CRC64;
MSLSAFTLFL ALIGGTSGQY YDYDFPLSIY GQSSPNCAPE CNCPESYPSA MYCDELKLKS
VPMVPPGIKY LYLRNNQIDH IDEKAFENVT DLQWLILDHN LLENSKIKGR VFSKLKQLKK
LHINHNNLTE SVGPLPKSLE DLQLTHNKIT KLGSFEGLVN LTFIHLQHNR LKEDAVSAAF
KGLKSLEYLD LSFNQIARLP SGLPVSLLTL YLDNNKISNI PDEYFKRFNA LQYLRLSHNE
LADSGIPGNS FNVSSLVELD LSYNKLKNIP TVNENLENYY LEVNQLEKFD IKSFCKILGP
LSYSKIKHLR LDGNRISETS LPPDMYECLR VANEVTLN
