Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P11672

- NGAL_MOUSE

UniProt

P11672 - NGAL_MOUSE

Protein

Neutrophil gelatinase-associated lipocalin

Gene

Lcn2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei128 – 1281Catecholate-type ferric siderophoreBy similarity
    Binding sitei147 – 1471Catecholate-type ferric siderophoreBy similarity
    Binding sitei156 – 1561Catecholate-type ferric siderophoreBy similarity

    GO - Molecular functioni

    1. iron ion binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. small molecule binding Source: InterPro
    4. transporter activity Source: InterPro

    GO - Biological processi

    1. cellular response to hydrogen peroxide Source: Ensembl
    2. cellular response to interleukin-1 Source: Ensembl
    3. cellular response to lipopolysaccharide Source: Ensembl
    4. cellular response to nutrient levels Source: Ensembl
    5. cellular response to tumor necrosis factor Source: Ensembl
    6. extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
    7. innate immune response Source: UniProtKB
    8. ion transport Source: UniProtKB-KW
    9. positive regulation of cell projection organization Source: Ensembl
    10. positive regulation of gene expression Source: Ensembl
    11. protein homotrimerization Source: Ensembl
    12. response to drug Source: Ensembl
    13. response to herbicide Source: Ensembl
    14. response to virus Source: MGI
    15. siderophore transport Source: UniProtKB

    Keywords - Biological processi

    Apoptosis, Immunity, Innate immunity, Ion transport, Iron transport, Transport

    Keywords - Ligandi

    Iron

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neutrophil gelatinase-associated lipocalin
    Short name:
    NGAL
    Alternative name(s):
    Lipocalin-2
    SV-40-induced 24P3 protein
    Siderocalin LCN2
    p25
    Gene namesi
    Name:Lcn2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:96757. Lcn2.

    Subcellular locationi

    Secreted 2 Publications
    Note: Upon binding to the SLC22A17 (24p3R) receptor, it is internalized.

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Mice are normal with no visible phenotype. They however show an increased susceptibility to bacterial infections. Neutrophils show significantly less bacteriostatic activity.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020By similarityAdd
    BLAST
    Chaini21 – 200180Neutrophil gelatinase-associated lipocalinPRO_0000017934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei21 – 211Pyrrolidone carboxylic acidBy similarity
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi85 – 851N-linked (GlcNAc...)2 Publications
    Disulfide bondi98 ↔ 1971 Publication

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP11672.
    PaxDbiP11672.
    PRIDEiP11672.

    PTM databases

    PhosphoSiteiP11672.

    Expressioni

    Tissue specificityi

    Detected in lung, spleen, uterus, vagina and epididymis.1 Publication

    Inductioni

    Upon Toll-like receptor (TLRs) stimuli. By SV-40.1 Publication

    Gene expression databases

    BgeeiP11672.
    CleanExiMM_LCN2.
    GenevestigatoriP11672.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Heterodimer; disulfide-linked with MMP9.1 Publication

    Structurei

    Secondary structure

    1
    200
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni33 – 353
    Turni44 – 474
    Beta strandi49 – 5810
    Turni63 – 653
    Beta strandi73 – 786
    Beta strandi84 – 918
    Beta strandi98 – 10710
    Beta strandi113 – 1175
    Helixi119 – 1213
    Beta strandi125 – 13511
    Beta strandi137 – 14913
    Beta strandi152 – 16413
    Helixi168 – 18013
    Helixi185 – 1873
    Beta strandi188 – 1925
    Beta strandi195 – 1973

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3S26X-ray1.80A21-200[»]
    3U9PX-ray2.80C/D21-200[»]
    ProteinModelPortaliP11672.
    SMRiP11672. Positions 27-200.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG40148.
    GeneTreeiENSGT00530000063610.
    HOGENOMiHOG000231660.
    HOVERGENiHBG106490.
    OMAiVPIDQCI.
    OrthoDBiEOG78M03G.
    PhylomeDBiP11672.
    TreeFamiTF336103.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR003087. N_gelatinase.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00179. LIPOCALIN.
    PR01275. NGELATINASE.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00213. LIPOCALIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P11672-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALSVMCLGL ALLGVLQSQA QDSTQNLIPA PSLLTVPLQP DFRSDQFRGR    50
    WYVVGLAGNA VQKKTEGSFT MYSTIYELQE NNSYNVTSIL VRDQDQGCRY 100
    WIRTFVPSSR AGQFTLGNMH RYPQVQSYNV QVATTDYNQF AMVFFRKTSE 150
    NKQYFKITLY GRTKELSPEL KERFTRFAKS LGLKDDNIIF SVPTDQCIDN 200
    Length:200
    Mass (Da):22,875
    Last modified:October 1, 1989 - v1
    Checksum:iDD9A8D08750E6863
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS15913.1.
    PIRiS07397.
    RefSeqiNP_032517.1. NM_008491.1.
    UniGeneiMm.9537.

    Genome annotation databases

    EnsembliENSMUST00000050785; ENSMUSP00000053962; ENSMUSG00000026822.
    GeneIDi16819.
    KEGGimmu:16819.
    UCSCiuc008jfl.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS15913.1.
    PIRi S07397.
    RefSeqi NP_032517.1. NM_008491.1.
    UniGenei Mm.9537.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3S26 X-ray 1.80 A 21-200 [» ]
    3U9P X-ray 2.80 C/D 21-200 [» ]
    ProteinModelPortali P11672.
    SMRi P11672. Positions 27-200.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P11672.

    Proteomic databases

    MaxQBi P11672.
    PaxDbi P11672.
    PRIDEi P11672.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000050785 ; ENSMUSP00000053962 ; ENSMUSG00000026822 .
    GeneIDi 16819.
    KEGGi mmu:16819.
    UCSCi uc008jfl.1. mouse.

    Organism-specific databases

    CTDi 3934.
    MGIi MGI:96757. Lcn2.

    Phylogenomic databases

    eggNOGi NOG40148.
    GeneTreei ENSGT00530000063610.
    HOGENOMi HOG000231660.
    HOVERGENi HBG106490.
    OMAi VPIDQCI.
    OrthoDBi EOG78M03G.
    PhylomeDBi P11672.
    TreeFami TF336103.

    Miscellaneous databases

    ChiTaRSi LCN2. mouse.
    NextBioi 290708.
    PROi P11672.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11672.
    CleanExi MM_LCN2.
    Genevestigatori P11672.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR003087. N_gelatinase.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00179. LIPOCALIN.
    PR01275. NGELATINASE.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiNGAL_MOUSE
    AccessioniPrimary (citable) accession number: P11672
    Secondary accession number(s): Q3UE34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3