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UniProtKB/Swiss-Prot entry P80188


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NGAL_HUMAN
Primary accession number P80188
Secondary accession numbers P30150 Q92683
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on November 1, 1995 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 94)
Name and origin of the protein
Protein name Neutrophil gelatinase-associated lipocalin [Precursor]
Synonyms NGAL
p25
25 kDa alpha-2-microglobulin-related subunit of MMP-9
Lipocalin-2
Oncogene 24p3
Gene name
Name: LCN2
Synonyms: HNL, NGAL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/bbrc.1994.2096; PubMed=8060329 [NCBI, ExPASy, EBI, Israel, Japan]
Bundgaard J.R., Sengelov H., Borregaard N., Kjeldsen L.;
"Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils.";
Biochem. Biophys. Res. Commun. 202:1468-1475(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Bone marrow;
DOI=10.1006/geno.1997.4896; PubMed=9339356 [NCBI, ExPASy, EBI, Israel, Japan]
Cowland J.B., Borregaard N.;
"Molecular characterization and pattern of tissue expression of the gene for neutrophil gelatinase-associated lipocalin from humans.";
Genomics 45:17-23(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-198, AND PARTIAL PROTEIN SEQUENCE.
DOI=10.1016/0014-5793(94)01303-I; PubMed=7835423 [NCBI, ExPASy, EBI, Israel, Japan]
Bartsch S., Tschesche H.;
"Cloning and expression of human neutrophil lipocalin cDNA derived from bone marrow and ovarian cancer cells.";
FEBS Lett. 357:255-259(1995).
[5]
PROTEIN SEQUENCE OF 21-198.
TISSUE=Neutrophil;
PubMed=7683678 [NCBI, ExPASy, EBI, Israel, Japan]
Kjeldsen L., Johnsen A.H., Sengelov H., Borregaard N.;
"Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase.";
J. Biol. Chem. 268:10425-10432(1993).
[6]
PROTEIN SEQUENCE OF 51-61; 71-90; 132-136; 152-160 AND 178-192.
TISSUE=Neutrophil;
DOI=10.1016/0014-5793(92)81511-J; PubMed=1281792 [NCBI, ExPASy, EBI, Israel, Japan]
Triebel S., Blaeser J., Reinke H., Tschesche H.;
"A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase.";
FEBS Lett. 314:386-388(1992).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, AND MASS SPECTROMETRY.
TISSUE=Bile;
DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan]
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, AND MASS SPECTROMETRY.
TISSUE=Saliva;
DOI=10.1021/pr050492k; PubMed=16740002 [NCBI, ExPASy, EBI, Israel, Japan]
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.";
J. Proteome Res. 5:1493-1503(2006).
[10]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-298.
DOI=10.1021/bi992215v; PubMed=10684642 [NCBI, ExPASy, EBI, Israel, Japan]
Goetz D.H., Willie S.T., Armen R.S., Bratt T., Borregaard N., Strong R.K.;
"Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin.";
Biochemistry 39:1935-1941(2000).
[11]
STRUCTURE BY NMR OF 21-198.
DOI=10.1006/jmbi.1999.2755; PubMed=10339412 [NCBI, ExPASy, EBI, Israel, Japan]
Coles M., Diercks T., Muehlenweg B., Bartsch S., Zolzer V., Tschesche H., Kessler H.;
"The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin.";
J. Mol. Biol. 289:139-157(1999).
Comments
  • FUNCTION: Transport of small lipophilic substances (Potential).
  • SUBUNIT: Forms a covalently linked, disulfide-bridged heterodimer with the 92 kDa type V collagenase (MMP-9).
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed in bone marrow and in tissues that are prone to exposure to microorganism. High expression is found in bone marrow as well as in uterus, prostate, salivary gland, stomach, appendix, colon, trachea and lungs. Not found in the small intestine or peripheral blood leukocytes.
  • SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X83006; CAA58127.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X99133; CAA67574.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033089; AAH33089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S75256; AAD14168.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC2339; JC2339.
RefSeq NP_005555.2; -.
UniGene Hs.204238
3D structure databases
PDB
1DFV; X-ray; 2.60 A; A/B=21-197.[ExPASy / RCSB / EBI]
1L6M; X-ray; 2.40 A; A/B/C=21-198.[ExPASy / RCSB / EBI]
1NGL; NMR; -; A=21-198.[ExPASy / RCSB / EBI]
1QQS; X-ray; 2.40 A; A=24-197.[ExPASy / RCSB / EBI]
1X71; X-ray; 2.10 A; A/B/C=21-198.[ExPASy / RCSB / EBI]
1X89; X-ray; 2.10 A; A/B/C=21-198.[ExPASy / RCSB / EBI]
1X8U; X-ray; 2.20 A; A/B/C=21-198.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DFV; -.
1L6M; -.
1NGL; -.
1QQS; -.
1X71; -.
1X89; -.
1X8U; -.
ModBase P80188.
Organism-specific databases
H-InvDB HIX0008419; -.
HGNC HGNC:6526; LCN2.
GenAtlas LCN2.
HPA CAB016549; -.
CAB016550; -.
HPA002695; -.
MIM 600181; gene. [NCBI / EBI]
PharmGKB PA26547; -.
GeneCards P80188.
Gene expression databases
ArrayExpress P80188; -.
CleanEx HS_LCN2; -.
GermOnline ENSG00000148346; Homo sapiens.
Family and domain databases
InterPro IPR012674; Calycin.
IPR002345; Lipocalin.
IPR000566; Lipocln_cytFABP.
IPR003087; N_gelatinase.
Graphical view of domain structure.
Gene3D G3DSA:2.40.128.20; Calycin; 1.
Pfam PF00061; Lipocalin; 1.
Pfam graphical view of domain structure.
PRINTS PR00179; LIPOCALIN.
PR01275; NGELATINASE.
PROSITE PS00213; LIPOCALIN; 1.
BLOCKS P80188.
Genome annotation databases
Ensembl ENSG00000148346; Homo sapiens. [Contig view]
GeneID 3934; -.
KEGG hsa:3934; -.
Phylogenomic databases
HOVERGEN P80188; -.
Other
SOURCE LCN2; Homo sapiens.
ProtoNet P80188.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Glycoprotein; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   198  178     Neutrophil gelatinase-associated lipocalin. PRO_0000017933
MOD_RES   21    21        Pyrrolidone carboxylic acid. 
CARBOHYD   85    85        N-linked (GlcNAc...). 
DISULFID   96   195         
CONFLICT   82    82        K -> N (in Ref. 6; AA sequence). 
CONFLICT   155   155        I -> V (in Ref. 6; AA sequence). 
CONFLICT   178   178        S -> Y (in Ref. 2; CAA67574). 
HELIX   33    35  3      
TURN   44    47  4      
STRAND   49    58  10      
STRAND   65    67  3      
STRAND   73    78  6      
STRAND   84    92  9      
STRAND   95   105  11      
STRAND   111   114  4      
HELIX   117   119  3      
STRAND   123   133  11      
STRAND   135   147  13      
STRAND   150   162  13      
HELIX   166   177  12      
TURN   178   180  3      
HELIX   183   185  3      
TURN   194   196  3      
Sequence information
Length: 198 AA [This is the length of the unprocessed precursor] Molecular weight: 22588 Da [This is the MW of the unprocessed precursor] CRC64: CD761805723FEF1E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPLGLLWLGL ALLGALHAQA QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA 

        70         80         90        100        110        120 
ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY 

       130        140        150        160        170        180 
PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG 

       190 
LPENHIVFPV PIDQCIDG 

P80188 in FASTA format

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