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P11672 (NGAL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neutrophil gelatinase-associated lipocalin

Short name=NGAL
Alternative name(s):
Lipocalin-2
SV-40-induced 24P3 protein
Siderocalin LCN2
p25
Gene names
Name:Lcn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length200 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Iron-trafficking protein involved in multiple processes such as apoptosis, innate immunity and renal development. Binds iron through association with 2,5-dihydroxybenzoic acid (2,5-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. Involved in innate immunity, possibly by sequestrating iron, leading to limit bacterial growth. Ref.10 Ref.11 Ref.12 Ref.14

Subunit structure

Homodimer; disulfide-linked. Heterodimer; disulfide-linked with MMP9. Ref.15

Subcellular location

Secreted. Note: Upon binding to the SLC22A17 (24p3R) receptor, it is internalized. Ref.7 Ref.10

Tissue specificity

Detected in lung, spleen, uterus, vagina and epididymis. Ref.7

Induction

Upon Toll-like receptor (TLRs) stimuli. By SV-40. Ref.11

Post-translational modification

N-glycosylated. Ref.7 Ref.15

Disruption phenotype

Mice are normal with no visible phenotype. They however show an increased susceptibility to bacterial infections. Neutrophils show significantly less bacteriostatic activity. Ref.11 Ref.13

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processApoptosis
Immunity
Innate immunity
Ion transport
Iron transport
Transport
   Cellular componentSecreted
   DomainSignal
   LigandIron
   PTMDisulfide bond
Glycoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from direct assay Ref.12. Source: MGI

innate immune response

Inferred from mutant phenotype Ref.13. Source: UniProtKB

ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell projection organization

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from direct assay Ref.1. Source: MGI

siderophore transport

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay Ref.12. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioniron ion binding

Inferred from direct assay Ref.12Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

small molecule binding

Inferred from electronic annotation. Source: InterPro

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 By similarity
Chain21 – 200180Neutrophil gelatinase-associated lipocalin
PRO_0000017934

Sites

Binding site1281Catecholate-type ferric siderophore By similarity
Binding site1471Catecholate-type ferric siderophore By similarity
Binding site1561Catecholate-type ferric siderophore By similarity

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid By similarity
Glycosylation811N-linked (GlcNAc...) Potential
Glycosylation851N-linked (GlcNAc...) Ref.15
Disulfide bond98 ↔ 197 Ref.15

Secondary structure

................................ 200
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11672 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: DD9A8D08750E6863

FASTA20022,875
        10         20         30         40         50         60 
MALSVMCLGL ALLGVLQSQA QDSTQNLIPA PSLLTVPLQP DFRSDQFRGR WYVVGLAGNA 

        70         80         90        100        110        120 
VQKKTEGSFT MYSTIYELQE NNSYNVTSIL VRDQDQGCRY WIRTFVPSSR AGQFTLGNMH 

       130        140        150        160        170        180 
RYPQVQSYNV QVATTDYNQF AMVFFRKTSE NKQYFKITLY GRTKELSPEL KERFTRFAKS 

       190        200 
LGLKDDNIIF SVPTDQCIDN 

« Hide

References

« Hide 'large scale' references
[1]"SV40-induced expression of mouse gene 24p3 involves a post-transcriptional mechanism."
Hraba-Renevey S., Turler H., Kress M., Salomon C., Weil R.
Oncogene 4:601-608(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss.
Tissue: Kidney.
[2]"An apparent autocrine mechanism amplifies the dexamethasone- and retinoic acid-induced expression of mouse lipocalin-encoding gene 24p3."
Garay-Rojas E., Harper M., Hraba-Renevey S., Kress M.
Gene 170:173-180(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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. expand/collapse author list , 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: Bone marrow.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., 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: Brain.
[7]"Demonstration of a glycoprotein derived from the 24p3 gene in mouse uterine luminal fluid."
Chu S.T., Huang H.L., Chen J.M., Chen Y.H.
Biochem. J. 316:545-550(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-200, PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"The first lipocalin with enzymatic activity."
Peitsch M.C., Boguski M.S.
Trends Biochem. Sci. 16:363-363(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO THE LIPOCALIN FAMILY.
[9]"Mouse oncogene protein 24p3 is a member of the lipocalin protein family."
Flower D.R., North A.C.T., Attwood T.K.
Biochem. Biophys. Res. Commun. 180:69-74(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO THE LIPOCALIN FAMILY.
[10]"An iron delivery pathway mediated by a lipocalin."
Yang J., Goetz D., Li J.Y., Wang W., Mori K., Setlik D., Du T., Erdjument-Bromage H., Tempst P., Strong R., Barasch J.
Mol. Cell 10:1045-1056(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, SUBCELLULAR LOCATION.
[11]"Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron."
Flo T.H., Smith K.D., Sato S., Rodriguez D.J., Holmes M.A., Strong R.K., Akira S., Aderem A.
Nature 432:917-921(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, DISRUPTION PHENOTYPE, INDUCTION.
[12]"A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake."
Devireddy L.R., Gazin C., Zhu X., Green M.R.
Cell 123:1293-1305(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SLC22A17, IRON-BINDING.
[13]"Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia coli infection but not to ischemia-reperfusion injury."
Berger T., Togawa A., Duncan G.S., Elia A.J., You-Ten A., Wakeham A., Fong H.E., Cheung C.C., Mak T.W.
Proc. Natl. Acad. Sci. U.S.A. 103:1834-1839(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[14]"A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production."
Devireddy L.R., Hart D.O., Goetz D.H., Green M.R.
Cell 141:1006-1017(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING.
[15]"Daedalus: a robust, turnkey platform for rapid production of decigram quantities of active recombinant proteins in human cell lines using novel lentiviral vectors."
Bandaranayake A.D., Correnti C., Ryu B.Y., Brault M., Strong R.K., Rawlings D.J.
Nucleic Acids Res. 39:E143-E143(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-200, DISULFIDE BOND, GLYCOSYLATION AT ASN-85.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14607 mRNA. Translation: CAA32762.1.
X81627 Genomic DNA. Translation: CAA57283.1.
AK149774 mRNA. Translation: BAE29077.1.
AL808027 Genomic DNA. Translation: CAM15869.1.
CH466542 Genomic DNA. Translation: EDL08545.1.
BC132069 mRNA. Translation: AAI32070.1.
BC132071 mRNA. Translation: AAI32072.1.
S82469 mRNA. No translation available.
CCDSCCDS15913.1.
PIRS07397.
RefSeqNP_032517.1. NM_008491.1.
UniGeneMm.9537.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S26X-ray1.80A21-200[»]
3U9PX-ray2.80C/D21-200[»]
ProteinModelPortalP11672.
SMRP11672. Positions 27-200.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP11672.

Proteomic databases

MaxQBP11672.
PaxDbP11672.
PRIDEP11672.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050785; ENSMUSP00000053962; ENSMUSG00000026822.
GeneID16819.
KEGGmmu:16819.
UCSCuc008jfl.1. mouse.

Organism-specific databases

CTD3934.
MGIMGI:96757. Lcn2.

Phylogenomic databases

eggNOGNOG40148.
GeneTreeENSGT00530000063610.
HOGENOMHOG000231660.
HOVERGENHBG106490.
OMAVPIDQCI.
OrthoDBEOG78M03G.
PhylomeDBP11672.
TreeFamTF336103.

Gene expression databases

BgeeP11672.
CleanExMM_LCN2.
GenevestigatorP11672.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR003087. N_gelatinase.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00179. LIPOCALIN.
PR01275. NGELATINASE.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLCN2. mouse.
NextBio290708.
PROP11672.
SOURCESearch...

Entry information

Entry nameNGAL_MOUSE
AccessionPrimary (citable) accession number: P11672
Secondary accession number(s): Q3UE34
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot