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Neutrophil gelatinase-associated lipocalin (NGAL) (25 kDa alpha-2-microglobulin-related subunit of MMP-9) (Lipocalin-2) (Oncogene 24p3) (Siderocalin LCN2) (p25)

 NGAL_HUMAN              Reviewed;         198 AA.
P80188; A6NII8; B4DWV4; B7ZAA2; P30150; Q5SYV9; Q5SYW0; Q6FGL5;
Q92683;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
31-JAN-2018, entry version 184.
RecName: Full=Neutrophil gelatinase-associated lipocalin;
Short=NGAL;
AltName: Full=25 kDa alpha-2-microglobulin-related subunit of MMP-9;
AltName: Full=Lipocalin-2;
AltName: Full=Oncogene 24p3;
AltName: Full=Siderocalin LCN2;
AltName: Full=p25;
Flags: Precursor;
Name=LCN2; Synonyms=HNL, NGAL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8060329; DOI=10.1006/bbrc.1994.2096;
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;
PubMed=9339356; DOI=10.1006/geno.1997.4896;
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] (ISOFORM 2).
TISSUE=Esophagus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-198, AND PARTIAL PROTEIN SEQUENCE.
PubMed=7835423; DOI=10.1016/0014-5793(94)01303-I;
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).
[9]
PROTEIN SEQUENCE OF 21-198, AND PYROGLUTAMATE FORMATION AT GLN-21.
TISSUE=Neutrophil;
PubMed=7683678;
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).
[10]
PROTEIN SEQUENCE OF 51-61; 71-90; 132-136; 152-160 AND 178-192.
TISSUE=Neutrophil;
PubMed=1281792; DOI=10.1016/0014-5793(92)81511-J;
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).
[11]
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).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
TISSUE=Bile;
PubMed=15084671; DOI=10.1074/mcp.M400015-MCP200;
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).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
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).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
TISSUE=Saliva;
PubMed=16740002; DOI=10.1021/pr050492k;
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).
[15]
INDUCTION.
PubMed=19229297; DOI=10.1038/emboj.2009.35;
Sheng Z., Wang S.Z., Green M.R.;
"Transcription and signalling pathways involved in BCR-ABL-mediated
misregulation of 24p3 and 24p3R.";
EMBO J. 28:866-876(2009).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-298.
PubMed=10684642; DOI=10.1021/bi992215v;
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).
[19]
STRUCTURE BY NMR OF 21-198.
PubMed=10339412; DOI=10.1006/jmbi.1999.2755;
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).
[20]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-198 IN COMPLEX WITH
SIDEROPHORE AND IRON, AND SUBUNIT.
PubMed=12453412; DOI=10.1016/S1097-2765(02)00708-6;
Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N.,
Strong R.K.;
"The neutrophil lipocalin NGAL is a bacteriostatic agent that
interferes with siderophore-mediated iron acquisition.";
Mol. Cell 10:1033-1043(2002).
-!- 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}.
-!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer; disulfide-
linked with MMP9. {ECO:0000269|PubMed:12453412}.
-!- INTERACTION:
Q96FA3:PELI1; NbExp=4; IntAct=EBI-11911016, EBI-448369;
O43765:SGTA; NbExp=4; IntAct=EBI-11911016, EBI-347996;
Q86UY0:TXNDC5; NbExp=4; IntAct=EBI-11911016, EBI-2825190;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12453413}.
Note=Upon binding to the SLC22A17 (24p3R) receptor, it is
internalized.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P80188-1; Sequence=Displayed;
Name=2;
IsoId=P80188-2; Sequence=VSP_039780;
-!- 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 lung. Not found in the small
intestine or peripheral blood leukocytes.
{ECO:0000269|PubMed:9339356}.
-!- INDUCTION: Expression is activated by the oncoprotein BCR-ABL;
BCR-ABL misregulates expression via the JAK/STAT pathway and
binding of STAT5A to the promoter. {ECO:0000269|PubMed:19229297}.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAI13824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; X83006; CAA58127.1; -; mRNA.
EMBL; X99133; CAA67574.1; -; Genomic_DNA.
EMBL; AK301694; BAG63166.1; -; mRNA.
EMBL; AK316217; BAH14588.1; -; mRNA.
EMBL; CR542092; CAG46889.1; -; mRNA.
EMBL; AL590708; CAI13823.1; -; Genomic_DNA.
EMBL; AL590708; CAI13824.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471090; EAW87750.1; -; Genomic_DNA.
EMBL; BC033089; AAH33089.1; -; mRNA.
EMBL; S75256; AAD14168.1; -; mRNA.
CCDS; CCDS6892.1; -. [P80188-1]
PIR; JC2339; JC2339.
RefSeq; NP_005555.2; NM_005564.4. [P80188-1]
UniGene; Hs.204238; -.
PDB; 1DFV; X-ray; 2.60 A; A/B=21-197.
PDB; 1L6M; X-ray; 2.40 A; A/B/C=21-198.
PDB; 1NGL; NMR; -; A=21-198.
PDB; 1QQS; X-ray; 2.40 A; A=24-197.
PDB; 1X71; X-ray; 2.10 A; A/B/C=21-198.
PDB; 1X89; X-ray; 2.10 A; A/B/C=21-198.
PDB; 1X8U; X-ray; 2.20 A; A/B/C=21-198.
PDB; 3BY0; X-ray; 2.57 A; A/B/C=1-198.
PDB; 3CBC; X-ray; 2.17 A; A/B/C=1-198.
PDB; 3CMP; X-ray; 2.80 A; A/B/C=1-198.
PDB; 3DSZ; X-ray; 2.00 A; A/B=21-198.
PDB; 3DTQ; X-ray; 2.50 A; A/B/C=21-198.
PDB; 3FW4; X-ray; 2.30 A; A/B/C=21-198.
PDB; 3FW5; X-ray; 2.30 A; A/B/C=21-198.
PDB; 3HWD; X-ray; 2.95 A; A/B/C=1-198.
PDB; 3HWE; X-ray; 2.80 A; A/B/C=1-198.
PDB; 3HWF; X-ray; 3.20 A; A/B/C=1-198.
PDB; 3HWG; X-ray; 2.19 A; A/B/C=1-198.
PDB; 3I0A; X-ray; 2.60 A; A/B/C=1-198.
PDB; 3K3L; X-ray; 2.62 A; A/B/C=21-198.
PDB; 3PEC; X-ray; 2.19 A; A/B/C=21-198.
PDB; 3PED; X-ray; 2.30 A; A/B/C=21-198.
PDB; 3T1D; X-ray; 2.30 A; A/B/C=1-198.
PDB; 3TF6; X-ray; 2.35 A; A/B/C=21-198.
PDB; 3TZS; X-ray; 2.45 A; A/B/C=21-198.
PDB; 3U03; X-ray; 2.40 A; A/C=1-198.
PDB; 3U0D; X-ray; 2.51 A; A/B/C/D=1-198.
PDB; 4GH7; X-ray; 2.60 A; A/C=21-198.
PDB; 4IAW; X-ray; 2.40 A; A/B/C=21-198.
PDB; 4IAX; X-ray; 1.90 A; A=21-198.
PDB; 4K19; X-ray; 2.74 A; A/B/C=21-198.
PDB; 4MVI; X-ray; 1.70 A; A=21-198.
PDB; 4MVK; X-ray; 1.50 A; A=21-198.
PDB; 4MVL; X-ray; 2.30 A; A/B/C/D=21-198.
PDB; 4QAE; X-ray; 2.10 A; A/B/C/D/E/F=21-198.
PDB; 4ZFX; X-ray; 2.55 A; A/B/C=21-198.
PDB; 4ZHC; X-ray; 2.04 A; A/B/C=21-198.
PDB; 4ZHD; X-ray; 2.05 A; A/B/C=21-198.
PDB; 4ZHF; X-ray; 2.45 A; A/B/C/D/E/F=21-198.
PDB; 4ZHG; X-ray; 2.05 A; A/B/C/D/E/F=21-198.
PDB; 4ZHH; X-ray; 2.04 A; A/B/C/D/E/F=21-198.
PDB; 5JR8; X-ray; 2.65 A; A/B=21-198.
PDB; 5KHP; X-ray; 2.65 A; A/B/C=21-198.
PDB; 5KIC; X-ray; 2.70 A; A/B/C=21-198.
PDB; 5KID; X-ray; 2.15 A; A/B/C=21-198.
PDB; 5MHH; X-ray; 2.00 A; A=21-198.
PDBsum; 1DFV; -.
PDBsum; 1L6M; -.
PDBsum; 1NGL; -.
PDBsum; 1QQS; -.
PDBsum; 1X71; -.
PDBsum; 1X89; -.
PDBsum; 1X8U; -.
PDBsum; 3BY0; -.
PDBsum; 3CBC; -.
PDBsum; 3CMP; -.
PDBsum; 3DSZ; -.
PDBsum; 3DTQ; -.
PDBsum; 3FW4; -.
PDBsum; 3FW5; -.
PDBsum; 3HWD; -.
PDBsum; 3HWE; -.
PDBsum; 3HWF; -.
PDBsum; 3HWG; -.
PDBsum; 3I0A; -.
PDBsum; 3K3L; -.
PDBsum; 3PEC; -.
PDBsum; 3PED; -.
PDBsum; 3T1D; -.
PDBsum; 3TF6; -.
PDBsum; 3TZS; -.
PDBsum; 3U03; -.
PDBsum; 3U0D; -.
PDBsum; 4GH7; -.
PDBsum; 4IAW; -.
PDBsum; 4IAX; -.
PDBsum; 4K19; -.
PDBsum; 4MVI; -.
PDBsum; 4MVK; -.
PDBsum; 4MVL; -.
PDBsum; 4QAE; -.
PDBsum; 4ZFX; -.
PDBsum; 4ZHC; -.
PDBsum; 4ZHD; -.
PDBsum; 4ZHF; -.
PDBsum; 4ZHG; -.
PDBsum; 4ZHH; -.
PDBsum; 5JR8; -.
PDBsum; 5KHP; -.
PDBsum; 5KIC; -.
PDBsum; 5KID; -.
PDBsum; 5MHH; -.
ProteinModelPortal; P80188; -.
SMR; P80188; -.
BioGrid; 110126; 25.
DIP; DIP-29952N; -.
IntAct; P80188; 67.
STRING; 9606.ENSP00000277480; -.
BindingDB; P80188; -.
DrugBank; DB01926; Carboxymycobactin S.
DrugBank; DB04043; Carboxymycobactin T.
DrugBank; DB01631; Methyl Nonanoate (Ester).
iPTMnet; P80188; -.
PhosphoSitePlus; P80188; -.
BioMuta; LCN2; -.
DMDM; 1171700; -.
MaxQB; P80188; -.
PaxDb; P80188; -.
PeptideAtlas; P80188; -.
PRIDE; P80188; -.
DNASU; 3934; -.
Ensembl; ENST00000277480; ENSP00000277480; ENSG00000148346. [P80188-1]
Ensembl; ENST00000373017; ENSP00000362108; ENSG00000148346. [P80188-1]
GeneID; 3934; -.
KEGG; hsa:3934; -.
UCSC; uc004bto.1; human. [P80188-1]
CTD; 3934; -.
DisGeNET; 3934; -.
EuPathDB; HostDB:ENSG00000148346.11; -.
GeneCards; LCN2; -.
HGNC; HGNC:6526; LCN2.
HPA; CAB016549; -.
HPA; CAB016550; -.
HPA; HPA002695; -.
MIM; 600181; gene.
neXtProt; NX_P80188; -.
OpenTargets; ENSG00000148346; -.
PharmGKB; PA30309; -.
eggNOG; ENOG410JAXJ; Eukaryota.
eggNOG; ENOG4111A75; LUCA.
GeneTree; ENSGT00530000063610; -.
HOVERGEN; HBG106490; -.
InParanoid; P80188; -.
KO; K21129; -.
PhylomeDB; P80188; -.
TreeFam; TF336103; -.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
Reactome; R-HSA-917937; Iron uptake and transport.
SIGNOR; P80188; -.
ChiTaRS; LCN2; human.
EvolutionaryTrace; P80188; -.
GeneWiki; LCN2; -.
GenomeRNAi; 3934; -.
PRO; PR:P80188; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148346; -.
CleanEx; HS_LCN2; -.
ExpressionAtlas; P80188; baseline and differential.
Genevisible; P80188; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0015891; P:siderophore transport; ISS: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.
PANTHER; PTHR11430; PTHR11430; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01275; NGELATINASE.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; 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:0000269|PubMed:7683678}.
CHAIN 21 198 Neutrophil gelatinase-associated
lipocalin.
/FTId=PRO_0000017933.
BINDING 126 126 Catecholate-type ferric siderophore.
BINDING 145 145 Catecholate-type ferric siderophore.
BINDING 154 154 Catecholate-type ferric siderophore.
MOD_RES 21 21 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:7683678}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15084671,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:16740002,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:7683678}.
DISULFID 96 195
VAR_SEQ 193 198 DQCIDG -> GNGQSG (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039780.
CONFLICT 9 9 G -> R (in Ref. 3; BAG63166).
{ECO:0000305}.
CONFLICT 13 13 L -> S (in Ref. 4; CAG46889).
{ECO:0000305}.
CONFLICT 82 82 K -> N (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 155 155 I -> V (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 178 178 S -> Y (in Ref. 2; CAA67574).
{ECO:0000305}.
HELIX 33 35 {ECO:0000244|PDB:4MVK}.
HELIX 44 47 {ECO:0000244|PDB:4MVK}.
STRAND 49 60 {ECO:0000244|PDB:4MVK}.
STRAND 64 66 {ECO:0000244|PDB:4MVK}.
STRAND 73 78 {ECO:0000244|PDB:4MVK}.
TURN 80 82 {ECO:0000244|PDB:1NGL}.
STRAND 84 91 {ECO:0000244|PDB:4MVK}.
STRAND 93 105 {ECO:0000244|PDB:4MVK}.
STRAND 111 114 {ECO:0000244|PDB:4MVK}.
STRAND 116 118 {ECO:0000244|PDB:4MVK}.
STRAND 119 121 {ECO:0000244|PDB:4MVL}.
STRAND 124 133 {ECO:0000244|PDB:4MVK}.
STRAND 135 147 {ECO:0000244|PDB:4MVK}.
STRAND 150 162 {ECO:0000244|PDB:4MVK}.
HELIX 166 178 {ECO:0000244|PDB:4MVK}.
HELIX 183 185 {ECO:0000244|PDB:4MVK}.
TURN 194 196 {ECO:0000244|PDB:4MVK}.
SEQUENCE 198 AA; 22588 MW; CD761805723FEF1E CRC64;
MPLGLLWLGL ALLGALHAQA QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA
ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY
PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG
LPENHIVFPV PIDQCIDG


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