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Neutrophil gelatinase-associated lipocalin (NGAL) (Lipocalin-2) (SV-40-induced 24P3 protein) (Siderocalin LCN2) (p25)

 NGAL_MOUSE              Reviewed;         200 AA.
P11672; Q3UE34;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
25-OCT-2017, entry version 143.
RecName: Full=Neutrophil gelatinase-associated lipocalin;
Short=NGAL;
AltName: Full=Lipocalin-2;
AltName: Full=SV-40-induced 24P3 protein;
AltName: Full=Siderocalin LCN2;
AltName: Full=p25;
Flags: Precursor;
Name=Lcn2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=SWR/J; TISSUE=Kidney;
PubMed=2542864;
Hraba-Renevey S., Turler H., Kress M., Salomon C., Weil R.;
"SV40-induced expression of mouse gene 24p3 involves a post-
transcriptional mechanism.";
Oncogene 4:601-608(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8666241; DOI=10.1016/0378-1119(95)00896-9;
Garay-Rojas E., Harper M., Hraba-Renevey S., Kress M.;
"An apparent autocrine mechanism amplifies the dexamethasone- and
retinoic acid-induced expression of mouse lipocalin-encoding gene
24p3.";
Gene 170:173-180(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-200, PARTIAL PROTEIN SEQUENCE,
GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8687399; DOI=10.1042/bj3160545;
Chu S.T., Huang H.L., Chen J.M., Chen Y.H.;
"Demonstration of a glycoprotein derived from the 24p3 gene in mouse
uterine luminal fluid.";
Biochem. J. 316:545-550(1996).
[8]
SIMILARITY TO THE LIPOCALIN FAMILY.
PubMed=1723819; DOI=10.1016/0968-0004(91)90149-P;
Peitsch M.C., Boguski M.S.;
"The first lipocalin with enzymatic activity.";
Trends Biochem. Sci. 16:363-363(1991).
[9]
SIMILARITY TO THE LIPOCALIN FAMILY.
PubMed=1834059; DOI=10.1016/S0006-291X(05)81256-2;
Flower D.R., North A.C.T., Attwood T.K.;
"Mouse oncogene protein 24p3 is a member of the lipocalin protein
family.";
Biochem. Biophys. Res. Commun. 180:69-74(1991).
[10]
FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, AND SUBCELLULAR LOCATION.
PubMed=12453413; DOI=10.1016/S1097-2765(02)00710-4;
Yang J., Goetz D., Li J.Y., Wang W., Mori K., Setlik D., Du T.,
Erdjument-Bromage H., Tempst P., Strong R., Barasch J.;
"An iron delivery pathway mediated by a lipocalin.";
Mol. Cell 10:1045-1056(2002).
[11]
FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, DISRUPTION PHENOTYPE, AND
INDUCTION.
PubMed=15531878; DOI=10.1038/nature03104;
Flo T.H., Smith K.D., Sato S., Rodriguez D.J., Holmes M.A.,
Strong R.K., Akira S., Aderem A.;
"Lipocalin 2 mediates an innate immune response to bacterial infection
by sequestrating iron.";
Nature 432:917-921(2004).
[12]
FUNCTION, INTERACTION WITH SLC22A17, AND IRON-BINDING.
PubMed=16377569; DOI=10.1016/j.cell.2005.10.027;
Devireddy L.R., Gazin C., Zhu X., Green M.R.;
"A cell-surface receptor for lipocalin 24p3 selectively mediates
apoptosis and iron uptake.";
Cell 123:1293-1305(2005).
[13]
DISRUPTION PHENOTYPE.
PubMed=16446425; DOI=10.1073/pnas.0510847103;
Berger T., Togawa A., Duncan G.S., Elia A.J., You-Ten A., Wakeham A.,
Fong H.E., Cheung C.C., Mak T.W.;
"Lipocalin 2-deficient mice exhibit increased sensitivity to
Escherichia coli infection but not to ischemia-reperfusion injury.";
Proc. Natl. Acad. Sci. U.S.A. 103:1834-1839(2006).
[14]
FUNCTION, IRON-BINDING, AND SIDEROPHORE-BINDING.
PubMed=20550936; DOI=10.1016/j.cell.2010.04.040;
Devireddy L.R., Hart D.O., Goetz D.H., Green M.R.;
"A mammalian siderophore synthesized by an enzyme with a bacterial
homolog involved in enterobactin production.";
Cell 141:1006-1017(2010).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-200, DISULFIDE BOND, AND
GLYCOSYLATION AT ASN-85.
PubMed=21911364; DOI=10.1093/nar/gkr706;
Bandaranayake A.D., Correnti C., Ryu B.Y., Brault M., Strong R.K.,
Rawlings D.J.;
"Daedalus: a robust, turnkey platform for rapid production of decigram
quantities of active recombinant proteins in human cell lines using
novel lentiviral vectors.";
Nucleic Acids Res. 39:E143-E143(2011).
-!- 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.
{ECO:0000269|PubMed:12453413, ECO:0000269|PubMed:15531878,
ECO:0000269|PubMed:16377569, ECO:0000269|PubMed:20550936}.
-!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer; disulfide-
linked with MMP9. {ECO:0000269|PubMed:21911364}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12453413,
ECO:0000269|PubMed:8687399}. Note=Upon binding to the SLC22A17
(24p3R) receptor, it is internalized.
-!- TISSUE SPECIFICITY: Detected in lung, spleen, uterus, vagina and
epididymis. {ECO:0000269|PubMed:8687399}.
-!- INDUCTION: Upon Toll-like receptor (TLRs) stimuli. By SV-40.
{ECO:0000269|PubMed:15531878}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:21911364,
ECO:0000269|PubMed:8687399}.
-!- DISRUPTION PHENOTYPE: Mice are normal with no visible phenotype.
They however show an increased susceptibility to bacterial
infections. Neutrophils show significantly less bacteriostatic
activity. {ECO:0000269|PubMed:15531878,
ECO:0000269|PubMed:16446425}.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
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EMBL; X14607; CAA32762.1; -; mRNA.
EMBL; X81627; CAA57283.1; -; Genomic_DNA.
EMBL; AK149774; BAE29077.1; -; mRNA.
EMBL; AL808027; CAM15869.1; -; Genomic_DNA.
EMBL; CH466542; EDL08545.1; -; Genomic_DNA.
EMBL; BC132069; AAI32070.1; -; mRNA.
EMBL; BC132071; AAI32072.1; -; mRNA.
EMBL; S82469; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS15913.1; -.
PIR; S07397; S07397.
RefSeq; NP_032517.1; NM_008491.1.
UniGene; Mm.9537; -.
PDB; 3S26; X-ray; 1.80 A; A=21-200.
PDB; 3U9P; X-ray; 2.80 A; C/D=21-200.
PDBsum; 3S26; -.
PDBsum; 3U9P; -.
ProteinModelPortal; P11672; -.
SMR; P11672; -.
STRING; 10090.ENSMUSP00000053962; -.
iPTMnet; P11672; -.
PhosphoSitePlus; P11672; -.
MaxQB; P11672; -.
PaxDb; P11672; -.
PeptideAtlas; P11672; -.
PRIDE; P11672; -.
Ensembl; ENSMUST00000050785; ENSMUSP00000053962; ENSMUSG00000026822.
GeneID; 16819; -.
KEGG; mmu:16819; -.
UCSC; uc008jfl.1; mouse.
CTD; 3934; -.
MGI; MGI:96757; Lcn2.
eggNOG; ENOG410JAXJ; Eukaryota.
eggNOG; ENOG4111A75; LUCA.
GeneTree; ENSGT00530000063610; -.
HOGENOM; HOG000231660; -.
HOVERGEN; HBG106490; -.
InParanoid; P11672; -.
KO; K21129; -.
PhylomeDB; P11672; -.
TreeFam; TF336103; -.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-6799990; Metal sequestration by antimicrobial proteins.
Reactome; R-MMU-917937; Iron uptake and transport.
ChiTaRS; Lcn2; mouse.
PRO; PR:P11672; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000026822; -.
CleanEx; MM_LCN2; -.
ExpressionAtlas; P11672; baseline and differential.
Genevisible; P11672; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0070207; P:protein homotrimerization; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009635; P:response to herbicide; IEA:Ensembl.
GO; GO:0010046; P:response to mycotoxin; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IDA:MGI.
GO; GO:0015891; P:siderophore transport; IDA:UniProtKB.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR003087; LCN2/LCN12.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00179; LIPOCALIN.
PRINTS; PR01275; NGELATINASE.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Immunity; Innate immunity;
Ion transport; Iron; Iron transport; Pyrrolidone carboxylic acid;
Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 200 Neutrophil gelatinase-associated
lipocalin.
/FTId=PRO_0000017934.
BINDING 128 128 Catecholate-type ferric siderophore.
{ECO:0000250}.
BINDING 147 147 Catecholate-type ferric siderophore.
{ECO:0000250}.
BINDING 156 156 Catecholate-type ferric siderophore.
{ECO:0000250}.
MOD_RES 21 21 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P80188}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21911364}.
DISULFID 98 197 {ECO:0000269|PubMed:21911364}.
TURN 33 35 {ECO:0000244|PDB:3S26}.
TURN 44 47 {ECO:0000244|PDB:3S26}.
STRAND 49 58 {ECO:0000244|PDB:3S26}.
TURN 63 65 {ECO:0000244|PDB:3U9P}.
STRAND 73 78 {ECO:0000244|PDB:3S26}.
STRAND 84 91 {ECO:0000244|PDB:3S26}.
STRAND 98 107 {ECO:0000244|PDB:3S26}.
STRAND 113 117 {ECO:0000244|PDB:3S26}.
HELIX 119 121 {ECO:0000244|PDB:3S26}.
STRAND 125 135 {ECO:0000244|PDB:3S26}.
STRAND 137 149 {ECO:0000244|PDB:3S26}.
STRAND 152 164 {ECO:0000244|PDB:3S26}.
HELIX 168 180 {ECO:0000244|PDB:3S26}.
HELIX 185 187 {ECO:0000244|PDB:3S26}.
STRAND 188 192 {ECO:0000244|PDB:3S26}.
STRAND 195 197 {ECO:0000244|PDB:3S26}.
SEQUENCE 200 AA; 22875 MW; DD9A8D08750E6863 CRC64;
MALSVMCLGL ALLGVLQSQA QDSTQNLIPA PSLLTVPLQP DFRSDQFRGR WYVVGLAGNA
VQKKTEGSFT MYSTIYELQE NNSYNVTSIL VRDQDQGCRY WIRTFVPSSR AGQFTLGNMH
RYPQVQSYNV QVATTDYNQF AMVFFRKTSE NKQYFKITLY GRTKELSPEL KERFTRFAKS
LGLKDDNIIF SVPTDQCIDN


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