P80188A6NII8B4DWV4B7ZAA2P30150Q5SYV9Q5SYW0Q6FGL5Q92683NGAL_HUMANNeutrophil gelatinase-associated lipocalinNGAL25 kDa alpha-2-microglobulin-related subunit of MMP-9Lipocalin-2Oncogene 24p3Siderocalinp25LCN2HNLNGALHomo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoMolecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)Molecular characterization and pattern of tissue expression of the gene for neutrophil gelatinase-associated lipocalin from humans.NUCLEOTIDE SEQUENCE [GENOMIC DNA]TISSUE SPECIFICITYComplete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)DNA sequence and analysis of human chromosome 9.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)Cloning and expression of human neutrophil lipocalin cDNA derived from bone marrow and ovarian cancer cells.NUCLEOTIDE SEQUENCE [MRNA] OF 21-198PARTIAL PROTEIN SEQUENCEIsolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase.PROTEIN SEQUENCE OF 21-198SUBCELLULAR LOCATIONIDENTIFICATION BY MASS SPECTROMETRYPYROGLUTAMATE FORMATION AT GLN-21INTERACTION WITH MMP9GLYCOSYLATION AT ASN-85TISSUE SPECIFICITYA 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase.PROTEIN SEQUENCE OF 51-61; 71-90; 132-136; 152-160 AND 178-192SUBUNITINTERACTION WITH MMP9Identification of neutrophil gelatinase-associated lipocalin as a novel matrix protein of specific granules in human neutrophils.SUBCELLULAR LOCATIONTISSUE SPECIFICITYAn iron delivery pathway mediated by a lipocalin.FUNCTIONIRON-BINDINGSIDEROPHORE-BINDINGSUBCELLULAR LOCATIONA proteomic analysis of human bile.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85Transcription and signalling pathways involved in BCR-ABL-mediated misregulation of 24p3 and 24p3R.INDUCTIONGlycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85Human Metabolome-derived Cofactors Are Required for the Antibacterial Activity of Siderocalin in Urine.FUNCTIONSUBCELLULAR LOCATIONInitial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Insulin receptor signaling regulates renal collecting duct and intercalated cell antibacterial defenses.TISSUE SPECIFICITYINDUCTIONLigand preference inferred from the structure of neutrophil gelatinase associated lipocalin.X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-197GLYCOSYLATION AT ASN-85DISULFIDE BONDSThe solution structure and dynamics of human neutrophil gelatinase-associated lipocalin.STRUCTURE BY NMR OF 21-198DISULFIDE BONDSThe neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition.X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-198 IN COMPLEX WITH SIDEROPHORE AND IRONSUBUNITDISULFIDE BONDSiderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration.X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 21-198 IN COMPLEXES WITH CARBOXYMYCOBACTIN S AND CARBOXYMYCOBACTIN TFUNCTIONDISULFIDE BONDSStructural Studies of Human Siderocalin.X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ENTEROBACTINDISULFIDE BONDSIron traffics in circulation bound to a siderocalin (Ngal)-catechol complex.X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-198FUNCTIONSUBCELLULAR LOCATIONMUTAGENESIS OF LYS-145 AND LYS-154DISULFIDE BONDSImmune interference in Mycobacterium tuberculosis intracellular iron acquisition through siderocalin recognition of carboxymycobactins.X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 21-198FUNCTIONDISULFIDE BONDSIron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development (PubMed:12453413, PubMed:27780864, PubMed:20581821). Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares structural similarities with bacterial enterobactin, and delivers or removes iron from the cell, depending on the context. Iron-bound form (holo-24p3) is internalized following binding to the SLC22A17 (24p3R) receptor, leading to release of iron and subsequent increase of intracellular iron concentration. In contrast, association of the iron-free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by association with an intracellular siderophore, iron chelation and iron transfer to the extracellular medium, thereby reducing intracellular iron concentration. Involved in apoptosis due to interleukin-3 (IL3) deprivation: iron-loaded form increases intracellular iron concentration without promoting apoptosis, while iron-free form decreases intracellular iron levels, inducing expression of the proapoptotic protein BCL2L11/BIM, resulting in apoptosis (By similarity). Involved in innate immunity; limits bacterial proliferation by sequestering iron bound to microbial siderophores, such as enterobactin (PubMed:27780864). Can also bind siderophores from M.tuberculosis (PubMed:15642259, PubMed:21978368).Monomer (PubMed:7683678, PubMed:1281792). Homodimer; disulfide-linked (PubMed:7683678). Heterodimer; disulfide-linked with MMP9 (PubMed:7683678).P80188P49419-2false3P80188Q9NXW9false3P80188Q8WXI3false3P80188Q12797-6false3P80188Q9BXY8false3P80188Q96LC9false3P80188P49069false3P80188P24863false3P80188Q9UKJ5false3P80188Q9H1P6false3P80188Q9H6B4false3P80188O14595false3P80188Q08426false3P80188Q6NZ36-4false3P80188B3EWG5false3P80188Q7Z4H3false3P80188Q6ISS4false3P80188Q5TA76false3P80188P80188false4P80188Q9UIQ6-2false3P80188Q9Y6Y9false3P80188Q96JG8false3P80188Q8IXL7-2false3P80188Q969H8false3P80188Q969S2false3P80188Q17RF5false3P80188P07237false3P80188P13667false3P80188Q96FA3false3P80188Q9NRD5false3P80188Q13526false3P80188Q9UGP5-2false3P80188Q12837false3P80188P54646false3P80188Q86Y79false3P80188O60895false3P80188Q9BWG6false3P80188P60059false3P80188O43765false5P80188Q96EQ0false3P80188Q8IYX1false3P80188Q9UL33-2false3P80188P20396false3P80188O43715false3P80188Q13049false3P80188Q99816false3P80188Q5W5X9-3false3P80188Q99757false3P80188P57075-2false3P80188Q969M7false3P80188Q9UMX0false3P80188Q9UHD9false5P80188P15692-12false3P80188Q14119false3P80188Q9Y6T4false3P80188Q9H0D6false3P80188O96006false3P80188A0A1U9X8X8false3SecretedCytoplasmic granule lumenCytoplasmic vesicle lumenUpon binding to the SLC22A17 (24p3R) receptor, it is internalized (By similarity). Releases the bound iron in the acidic lumen of cytoplasmic vesicles (PubMed:12453413, PubMed:20581821).P80188-11P80188-22Detected in neutrophils (at protein level) (PubMed:7683678, PubMed:8298140). Expressed in bone marrow and in tissues that are prone to exposure to microorganism (PubMed:9339356). High expression is found in bone marrow as well as in uterus, prostate, salivary gland, stomach, appendix, colon, trachea and lung (PubMed:9339356). Expressed in the medullary tubules of the kidney (PubMed:30418175). Not found in the small intestine or peripheral blood leukocytes (PubMed:9339356).Expression is activated by the oncoprotein BCR-ABL; BCR-ABL misregulates expression via the JAK/STAT pathway and binding of STAT5A to the promoter (PubMed:19229297). Induced by insulin (PubMed:30418175).Belongs to the calycin superfamily. Lipocalin family.3D-structureAlternative splicingApoptosisCytoplasmic vesicleDirect protein sequencingDisulfide bondGlycoproteinImmunityInnate immunityIon transportIronIron transportPyrrolidone carboxylic acidReference proteomeSecretedSignalTransporta carboxymycobactinenterobactina carboxymycobactina carboxymycobactinenterobactina carboxymycobactinDQCIDGGNGQSGKAKAGRLSKNIVSYMPLGLLWLGLALLGALHAQAQDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKEDKSYNVTSVLFRKKKCDYWIRTFVPGCQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAMVFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
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