NGAL_HUMAN
ID NGAL_HUMAN Reviewed; 198 AA.
AC P80188; A6NII8; B4DWV4; B7ZAA2; P30150; Q5SYV9; Q5SYW0; Q6FGL5; Q92683;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Neutrophil gelatinase-associated lipocalin {ECO:0000303|PubMed:9339356};
DE Short=NGAL;
DE AltName: Full=25 kDa alpha-2-microglobulin-related subunit of MMP-9 {ECO:0000303|PubMed:1281792};
DE AltName: Full=Lipocalin-2;
DE AltName: Full=Oncogene 24p3;
DE AltName: Full=Siderocalin {ECO:0000303|PubMed:15642259, ECO:0000303|PubMed:20581821};
DE AltName: Full=p25;
DE Flags: Precursor;
GN Name=LCN2; Synonyms=HNL, NGAL {ECO:0000303|PubMed:8060329};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8060329; DOI=10.1006/bbrc.1994.2096;
RA Bundgaard J.R., Sengelov H., Borregaard N., Kjeldsen L.;
RT "Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin
RT expressed in human neutrophils.";
RL Biochem. Biophys. Res. Commun. 202:1468-1475(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=9339356; DOI=10.1006/geno.1997.4896;
RA Cowland J.B., Borregaard N.;
RT "Molecular characterization and pattern of tissue expression of the gene
RT for neutrophil gelatinase-associated lipocalin from humans.";
RL Genomics 45:17-23(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Esophagus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-198, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7835423; DOI=10.1016/0014-5793(94)01303-i;
RA Bartsch S., Tschesche H.;
RT "Cloning and expression of human neutrophil lipocalin cDNA derived from
RT bone marrow and ovarian cancer cells.";
RL FEBS Lett. 357:255-259(1995).
RN [9]
RP PROTEIN SEQUENCE OF 21-198, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
RP SPECTROMETRY, PYROGLUTAMATE FORMATION AT GLN-21, INTERACTION WITH MMP9,
RP GLYCOSYLATION AT ASN-85, AND TISSUE SPECIFICITY.
RC TISSUE=Neutrophil;
RX PubMed=7683678; DOI=10.1016/s0021-9258(18)82217-7;
RA Kjeldsen L., Johnsen A.H., Sengelov H., Borregaard N.;
RT "Isolation and primary structure of NGAL, a novel protein associated with
RT human neutrophil gelatinase.";
RL J. Biol. Chem. 268:10425-10432(1993).
RN [10]
RP PROTEIN SEQUENCE OF 51-61; 71-90; 132-136; 152-160 AND 178-192, SUBUNIT,
RP AND INTERACTION WITH MMP9.
RC TISSUE=Neutrophil;
RX PubMed=1281792; DOI=10.1016/0014-5793(92)81511-j;
RA Triebel S., Blaeser J., Reinke H., Tschesche H.;
RT "A 25 kDa alpha 2-microglobulin-related protein is a component of the 125
RT kDa form of human gelatinase.";
RL FEBS Lett. 314:386-388(1992).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8298140;
RA Kjeldsen L., Bainton D.F., Sengeloev H., Borregaard N.;
RT "Identification of neutrophil gelatinase-associated lipocalin as a novel
RT matrix protein of specific granules in human neutrophils.";
RL Blood 83:799-807(1994).
RN [12]
RP FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=12453413; DOI=10.1016/s1097-2765(02)00710-4;
RA Yang J., Goetz D., Li J.Y., Wang W., Mori K., Setlik D., Du T.,
RA Erdjument-Bromage H., Tempst P., Strong R., Barasch J.;
RT "An iron delivery pathway mediated by a lipocalin.";
RL Mol. Cell 10:1045-1056(2002).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
RC TISSUE=Bile;
RX PubMed=15084671; DOI=10.1074/mcp.m400015-mcp200;
RA Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J.,
RA Argani P., Goggins M.G., Maitra A., Pandey A.;
RT "A proteomic analysis of human bile.";
RL Mol. Cell. Proteomics 3:715-728(2004).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
RC TISSUE=Saliva;
RX PubMed=16740002; DOI=10.1021/pr050492k;
RA Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT capture and mass spectrometry.";
RL J. Proteome Res. 5:1493-1503(2006).
RN [16]
RP INDUCTION.
RX PubMed=19229297; DOI=10.1038/emboj.2009.35;
RA Sheng Z., Wang S.Z., Green M.R.;
RT "Transcription and signalling pathways involved in BCR-ABL-mediated
RT misregulation of 24p3 and 24p3R.";
RL EMBO J. 28:866-876(2009).
RN [17]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=27780864; DOI=10.1074/jbc.m116.759183;
RA Shields-Cutler R.R., Crowley J.R., Miller C.D., Stapleton A.E., Cui W.,
RA Henderson J.P.;
RT "Human Metabolome-derived Cofactors Are Required for the Antibacterial
RT Activity of Siderocalin in Urine.";
RL J. Biol. Chem. 291:25901-25910(2016).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-197, GLYCOSYLATION AT ASN-85,
RP AND DISULFIDE BONDS.
RX PubMed=10684642; DOI=10.1021/bi992215v;
RA Goetz D.H., Willie S.T., Armen R.S., Bratt T., Borregaard N., Strong R.K.;
RT "Ligand preference inferred from the structure of neutrophil gelatinase
RT associated lipocalin.";
RL Biochemistry 39:1935-1941(2000).
RN [21]
RP STRUCTURE BY NMR OF 21-198, AND DISULFIDE BONDS.
RX PubMed=10339412; DOI=10.1006/jmbi.1999.2755;
RA Coles M., Diercks T., Muehlenweg B., Bartsch S., Zolzer V., Tschesche H.,
RA Kessler H.;
RT "The solution structure and dynamics of human neutrophil gelatinase-
RT associated lipocalin.";
RL J. Mol. Biol. 289:139-157(1999).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 21-198 IN COMPLEX WITH SIDEROPHORE
RP AND IRON, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=12453412; DOI=10.1016/s1097-2765(02)00708-6;
RA Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N.,
RA Strong R.K.;
RT "The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes
RT with siderophore-mediated iron acquisition.";
RL Mol. Cell 10:1033-1043(2002).
RN [23] {ECO:0007744|PDB:1X71, ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 21-198 IN COMPLEXES WITH
RP CARBOXYMYCOBACTIN S AND CARBOXYMYCOBACTIN T, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=15642259; DOI=10.1016/j.str.2004.10.009;
RA Holmes M.A., Paulsene W., Jide X., Ratledge C., Strong R.K.;
RT "Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending
RT against mycobacterial infections through iron sequestration.";
RL Structure 13:29-41(2005).
RN [24] {ECO:0007744|PDB:3CMP}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ENTEROBACTIN, AND
RP DISULFIDE BONDS.
RA Clifton M.C., Pizzaro J.C., Abergel R., Hoette T., Vigdorovich V.,
RA Raymond K., Strong R.K.;
RT "Structural Studies of Human Siderocalin.";
RL Submitted (MAR-2008) to the PDB data bank.
RN [25] {ECO:0007744|PDB:3FW4, ECO:0007744|PDB:3FW5}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-198, FUNCTION, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF LYS-145 AND LYS-154, AND DISULFIDE BONDS.
RX PubMed=20581821; DOI=10.1038/nchembio.402;
RA Bao G., Clifton M., Hoette T.M., Mori K., Deng S.X., Qiu A., Viltard M.,
RA Williams D., Paragas N., Leete T., Kulkarni R., Li X., Lee B.,
RA Kalandadze A., Ratner A.J., Pizarro J.C., Schmidt-Ott K.M., Landry D.W.,
RA Raymond K.N., Strong R.K., Barasch J.;
RT "Iron traffics in circulation bound to a siderocalin (Ngal)-catechol
RT complex.";
RL Nat. Chem. Biol. 6:602-609(2010).
RN [26] {ECO:0007744|PDB:3PEC, ECO:0007744|PDB:3PED}
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 21-198, FUNCTION, AND DISULFIDE
RP BONDS.
RX PubMed=21978368; DOI=10.1021/cb200331g;
RA Hoette T.M., Clifton M.C., Zawadzka A.M., Holmes M.A., Strong R.K.,
RA Raymond K.N.;
RT "Immune interference in Mycobacterium tuberculosis intracellular iron
RT acquisition through siderocalin recognition of carboxymycobactins.";
RL ACS Chem. Biol. 6:1327-1331(2011).
CC -!- FUNCTION: Iron-trafficking protein involved in multiple processes such
CC as apoptosis, innate immunity and renal development (PubMed:12453413,
CC PubMed:27780864, PubMed:20581821). Binds iron through association with
CC 2,3-dihydroxybenzoic acid (2,3-DHBA), a siderophore that shares
CC structural similarities with bacterial enterobactin, and delivers or
CC removes iron from the cell, depending on the context. Iron-bound form
CC (holo-24p3) is internalized following binding to the SLC22A17 (24p3R)
CC receptor, leading to release of iron and subsequent increase of
CC intracellular iron concentration. In contrast, association of the iron-
CC free form (apo-24p3) with the SLC22A17 (24p3R) receptor is followed by
CC association with an intracellular siderophore, iron chelation and iron
CC transfer to the extracellular medium, thereby reducing intracellular
CC iron concentration. Involved in apoptosis due to interleukin-3 (IL3)
CC deprivation: iron-loaded form increases intracellular iron
CC concentration without promoting apoptosis, while iron-free form
CC decreases intracellular iron levels, inducing expression of the
CC proapoptotic protein BCL2L11/BIM, resulting in apoptosis (By
CC similarity). Involved in innate immunity; limits bacterial
CC proliferation by sequestering iron bound to microbial siderophores,
CC such as enterobactin (PubMed:27780864). Can also bind siderophores from
CC M.tuberculosis (PubMed:15642259, PubMed:21978368).
CC {ECO:0000250|UniProtKB:P11672, ECO:0000269|PubMed:12453413,
CC ECO:0000269|PubMed:15642259, ECO:0000269|PubMed:20581821,
CC ECO:0000269|PubMed:21978368, ECO:0000269|PubMed:27780864}.
CC -!- SUBUNIT: Monomer (PubMed:7683678, PubMed:1281792). Homodimer;
CC disulfide-linked (PubMed:7683678). Heterodimer; disulfide-linked with
CC MMP9 (PubMed:7683678). {ECO:0000269|PubMed:12453412,
CC ECO:0000269|PubMed:1281792, ECO:0000269|PubMed:7683678}.
CC -!- INTERACTION:
CC P80188; P49419-2: ALDH7A1; NbExp=3; IntAct=EBI-11911016, EBI-11107920;
CC P80188; Q9NXW9: ALKBH4; NbExp=3; IntAct=EBI-11911016, EBI-8637516;
CC P80188; Q8WXI3: ASB10; NbExp=3; IntAct=EBI-11911016, EBI-3923154;
CC P80188; Q12797-6: ASPH; NbExp=3; IntAct=EBI-11911016, EBI-12092171;
CC P80188; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-11911016, EBI-745073;
CC P80188; Q96LC9: BMF; NbExp=3; IntAct=EBI-11911016, EBI-3919268;
CC P80188; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-11911016, EBI-12155483;
CC P80188; P49069: CAMLG; NbExp=3; IntAct=EBI-11911016, EBI-1748958;
CC P80188; P24863: CCNC; NbExp=3; IntAct=EBI-11911016, EBI-395261;
CC P80188; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-11911016, EBI-741528;
CC P80188; Q9H6B4: CLMP; NbExp=3; IntAct=EBI-11911016, EBI-4314260;
CC P80188; O14595: CTDSP2; NbExp=3; IntAct=EBI-11911016, EBI-2802973;
CC P80188; Q08426: EHHADH; NbExp=3; IntAct=EBI-11911016, EBI-2339219;
CC P80188; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-11911016, EBI-12013806;
CC P80188; B3EWG5: FAM25C; NbExp=3; IntAct=EBI-11911016, EBI-14240149;
CC P80188; Q7Z4H3: HDDC2; NbExp=3; IntAct=EBI-11911016, EBI-6163836;
CC P80188; Q6ISS4: LAIR2; NbExp=3; IntAct=EBI-11911016, EBI-10250491;
CC P80188; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-11911016, EBI-9394625;
CC P80188; P80188: LCN2; NbExp=4; IntAct=EBI-11911016, EBI-11911016;
CC P80188; Q9UIQ6-2: LNPEP; NbExp=3; IntAct=EBI-11911016, EBI-12133176;
CC P80188; Q9Y6Y9: LY96; NbExp=3; IntAct=EBI-11911016, EBI-1539247;
CC P80188; Q96JG8: MAGED4; NbExp=3; IntAct=EBI-11911016, EBI-721864;
CC P80188; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-11911016, EBI-10699187;
CC P80188; Q969H8: MYDGF; NbExp=3; IntAct=EBI-11911016, EBI-718622;
CC P80188; Q969S2: NEIL2; NbExp=3; IntAct=EBI-11911016, EBI-10281234;
CC P80188; Q17RF5: ODAPH; NbExp=3; IntAct=EBI-11911016, EBI-10239029;
CC P80188; P07237: P4HB; NbExp=3; IntAct=EBI-11911016, EBI-395883;
CC P80188; P13667: PDIA4; NbExp=3; IntAct=EBI-11911016, EBI-1054653;
CC P80188; Q96FA3: PELI1; NbExp=3; IntAct=EBI-11911016, EBI-448369;
CC P80188; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-11911016, EBI-79165;
CC P80188; Q13526: PIN1; NbExp=3; IntAct=EBI-11911016, EBI-714158;
CC P80188; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-11911016, EBI-10320765;
CC P80188; Q12837: POU4F2; NbExp=3; IntAct=EBI-11911016, EBI-17236143;
CC P80188; P54646: PRKAA2; NbExp=3; IntAct=EBI-11911016, EBI-1383852;
CC P80188; Q86Y79: PTRH1; NbExp=3; IntAct=EBI-11911016, EBI-2602515;
CC P80188; O60895: RAMP2; NbExp=3; IntAct=EBI-11911016, EBI-9009040;
CC P80188; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-11911016, EBI-748391;
CC P80188; P60059: SEC61G; NbExp=3; IntAct=EBI-11911016, EBI-4402709;
CC P80188; O43765: SGTA; NbExp=5; IntAct=EBI-11911016, EBI-347996;
CC P80188; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-11911016, EBI-744081;
CC P80188; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-11911016, EBI-12018146;
CC P80188; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-11911016, EBI-11119202;
CC P80188; P20396: TRH; NbExp=3; IntAct=EBI-11911016, EBI-12813975;
CC P80188; O43715: TRIAP1; NbExp=3; IntAct=EBI-11911016, EBI-2820212;
CC P80188; Q13049: TRIM32; NbExp=3; IntAct=EBI-11911016, EBI-742790;
CC P80188; Q99816: TSG101; NbExp=3; IntAct=EBI-11911016, EBI-346882;
CC P80188; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-11911016, EBI-9090990;
CC P80188; Q99757: TXN2; NbExp=3; IntAct=EBI-11911016, EBI-2932492;
CC P80188; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-11911016, EBI-7353612;
CC P80188; Q969M7: UBE2F; NbExp=3; IntAct=EBI-11911016, EBI-1056876;
CC P80188; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-11911016, EBI-741480;
CC P80188; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-11911016, EBI-947187;
CC P80188; P15692-12: VEGFA; NbExp=3; IntAct=EBI-11911016, EBI-6622053;
CC P80188; Q14119: VEZF1; NbExp=3; IntAct=EBI-11911016, EBI-11980193;
CC P80188; Q9Y6T4: WUGSC:H_DJ0726N20.gs.b; NbExp=3; IntAct=EBI-11911016, EBI-12369705;
CC P80188; Q9H0D6: XRN2; NbExp=3; IntAct=EBI-11911016, EBI-372110;
CC P80188; O96006: ZBED1; NbExp=3; IntAct=EBI-11911016, EBI-740037;
CC P80188; A0A1U9X8X8; NbExp=3; IntAct=EBI-11911016, EBI-17234977;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12453413,
CC ECO:0000269|PubMed:27780864, ECO:0000269|PubMed:7683678}. Cytoplasmic
CC granule lumen {ECO:0000269|PubMed:8298140}. Cytoplasmic vesicle lumen
CC {ECO:0000269|PubMed:12453413}. Note=Upon binding to the SLC22A17
CC (24p3R) receptor, it is internalized (By similarity). Releases the
CC bound iron in the acidic lumen of cytoplasmic vesicles
CC (PubMed:12453413, PubMed:20581821). {ECO:0000250|UniProtKB:P11672,
CC ECO:0000269|PubMed:12453413, ECO:0000269|PubMed:20581821}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P80188-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P80188-2; Sequence=VSP_039780;
CC -!- TISSUE SPECIFICITY: Detected in neutrophils (at protein level)
CC (PubMed:7683678, PubMed:8298140). Expressed in bone marrow and in
CC tissues that are prone to exposure to microorganism. High expression is
CC found in bone marrow as well as in uterus, prostate, salivary gland,
CC stomach, appendix, colon, trachea and lung. Not found in the small
CC intestine or peripheral blood leukocytes. {ECO:0000269|PubMed:7683678,
CC ECO:0000269|PubMed:8298140, ECO:0000269|PubMed:9339356}.
CC -!- INDUCTION: Expression is activated by the oncoprotein BCR-ABL; BCR-ABL
CC misregulates expression via the JAK/STAT pathway and binding of STAT5A
CC to the promoter. {ECO:0000269|PubMed:19229297}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X83006; CAA58127.1; -; mRNA.
DR EMBL; X99133; CAA67574.1; -; Genomic_DNA.
DR EMBL; AK301694; BAG63166.1; -; mRNA.
DR EMBL; AK316217; BAH14588.1; -; mRNA.
DR EMBL; CR542092; CAG46889.1; -; mRNA.
DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87750.1; -; Genomic_DNA.
DR EMBL; BC033089; AAH33089.1; -; mRNA.
DR EMBL; S75256; AAD14168.1; -; mRNA.
DR CCDS; CCDS6892.1; -. [P80188-1]
DR PIR; JC2339; JC2339.
DR RefSeq; NP_005555.2; NM_005564.4. [P80188-1]
DR PDB; 1DFV; X-ray; 2.60 A; A/B=21-197.
DR PDB; 1L6M; X-ray; 2.40 A; A/B/C=21-198.
DR PDB; 1NGL; NMR; -; A=21-198.
DR PDB; 1QQS; X-ray; 2.40 A; A=24-197.
DR PDB; 1X71; X-ray; 2.10 A; A/B/C=21-198.
DR PDB; 1X89; X-ray; 2.10 A; A/B/C=21-198.
DR PDB; 1X8U; X-ray; 2.20 A; A/B/C=21-198.
DR PDB; 3BY0; X-ray; 2.57 A; A/B/C=1-198.
DR PDB; 3CBC; X-ray; 2.17 A; A/B/C=1-198.
DR PDB; 3CMP; X-ray; 2.80 A; A/B/C=1-198.
DR PDB; 3DSZ; X-ray; 2.00 A; A/B=21-198.
DR PDB; 3DTQ; X-ray; 2.50 A; A/B/C=21-198.
DR PDB; 3FW4; X-ray; 2.30 A; A/B/C=21-198.
DR PDB; 3FW5; X-ray; 2.30 A; A/B/C=21-198.
DR PDB; 3HWD; X-ray; 2.95 A; A/B/C=1-198.
DR PDB; 3HWE; X-ray; 2.80 A; A/B/C=1-198.
DR PDB; 3HWF; X-ray; 3.20 A; A/B/C=1-198.
DR PDB; 3HWG; X-ray; 2.19 A; A/B/C=1-198.
DR PDB; 3I0A; X-ray; 2.60 A; A/B/C=1-198.
DR PDB; 3K3L; X-ray; 2.62 A; A/B/C=21-198.
DR PDB; 3PEC; X-ray; 2.19 A; A/B/C=21-198.
DR PDB; 3PED; X-ray; 2.30 A; A/B/C=21-198.
DR PDB; 3T1D; X-ray; 2.30 A; A/B/C=1-198.
DR PDB; 3TF6; X-ray; 2.35 A; A/B/C=21-198.
DR PDB; 3TZS; X-ray; 2.45 A; A/B/C=21-198.
DR PDB; 3U0D; X-ray; 2.51 A; A/B/C/D=1-198.
DR PDB; 4GH7; X-ray; 2.60 A; A/C=21-198.
DR PDB; 4IAW; X-ray; 2.40 A; A/B/C=21-198.
DR PDB; 4IAX; X-ray; 1.90 A; A=21-198.
DR PDB; 4K19; X-ray; 2.74 A; A/B/C=21-198.
DR PDB; 4MVI; X-ray; 1.70 A; A=21-198.
DR PDB; 4MVK; X-ray; 1.50 A; A=21-198.
DR PDB; 4MVL; X-ray; 2.30 A; A/B/C/D=21-198.
DR PDB; 4QAE; X-ray; 2.10 A; A/B/C/D/E/F=21-198.
DR PDB; 4ZFX; X-ray; 2.55 A; A/B/C=21-198.
DR PDB; 4ZHC; X-ray; 2.04 A; A/B/C=21-198.
DR PDB; 4ZHD; X-ray; 2.05 A; A/B/C=21-198.
DR PDB; 4ZHF; X-ray; 2.45 A; A/B/C/D/E/F=21-198.
DR PDB; 4ZHG; X-ray; 2.05 A; A/B/C/D/E/F=21-198.
DR PDB; 4ZHH; X-ray; 2.04 A; A/B/C/D/E/F=21-198.
DR PDB; 5JR8; X-ray; 2.65 A; A/B=21-198.
DR PDB; 5KHP; X-ray; 2.65 A; A/B/C=21-198.
DR PDB; 5KIC; X-ray; 2.70 A; A/B/C=21-198.
DR PDB; 5KID; X-ray; 2.15 A; A/B/C=21-198.
DR PDB; 5MHH; X-ray; 2.00 A; A=21-198.
DR PDB; 5N47; X-ray; 3.00 A; A/C/E=21-198.
DR PDB; 5N48; X-ray; 1.60 A; A/C=21-198.
DR PDB; 5NKN; X-ray; 2.20 A; A=25-198.
DR PDB; 6GQZ; X-ray; 1.40 A; A/B=25-198.
DR PDB; 6GR0; X-ray; 2.50 A; A/B/C=25-198.
DR PDB; 6O5D; X-ray; 2.40 A; A/B/C=25-198.
DR PDB; 6QMU; X-ray; 1.98 A; A/B=21-198.
DR PDB; 6S8V; X-ray; 1.80 A; A/C=21-198.
DR PDB; 6SUA; X-ray; 2.75 A; A/C=21-198.
DR PDB; 6Z2C; X-ray; 1.80 A; A/B/C=21-198.
DR PDB; 6Z6Z; X-ray; 1.78 A; A=21-198.
DR PDBsum; 1DFV; -.
DR PDBsum; 1L6M; -.
DR PDBsum; 1NGL; -.
DR PDBsum; 1QQS; -.
DR PDBsum; 1X71; -.
DR PDBsum; 1X89; -.
DR PDBsum; 1X8U; -.
DR PDBsum; 3BY0; -.
DR PDBsum; 3CBC; -.
DR PDBsum; 3CMP; -.
DR PDBsum; 3DSZ; -.
DR PDBsum; 3DTQ; -.
DR PDBsum; 3FW4; -.
DR PDBsum; 3FW5; -.
DR PDBsum; 3HWD; -.
DR PDBsum; 3HWE; -.
DR PDBsum; 3HWF; -.
DR PDBsum; 3HWG; -.
DR PDBsum; 3I0A; -.
DR PDBsum; 3K3L; -.
DR PDBsum; 3PEC; -.
DR PDBsum; 3PED; -.
DR PDBsum; 3T1D; -.
DR PDBsum; 3TF6; -.
DR PDBsum; 3TZS; -.
DR PDBsum; 3U0D; -.
DR PDBsum; 4GH7; -.
DR PDBsum; 4IAW; -.
DR PDBsum; 4IAX; -.
DR PDBsum; 4K19; -.
DR PDBsum; 4MVI; -.
DR PDBsum; 4MVK; -.
DR PDBsum; 4MVL; -.
DR PDBsum; 4QAE; -.
DR PDBsum; 4ZFX; -.
DR PDBsum; 4ZHC; -.
DR PDBsum; 4ZHD; -.
DR PDBsum; 4ZHF; -.
DR PDBsum; 4ZHG; -.
DR PDBsum; 4ZHH; -.
DR PDBsum; 5JR8; -.
DR PDBsum; 5KHP; -.
DR PDBsum; 5KIC; -.
DR PDBsum; 5KID; -.
DR PDBsum; 5MHH; -.
DR PDBsum; 5N47; -.
DR PDBsum; 5N48; -.
DR PDBsum; 5NKN; -.
DR PDBsum; 6GQZ; -.
DR PDBsum; 6GR0; -.
DR PDBsum; 6O5D; -.
DR PDBsum; 6QMU; -.
DR PDBsum; 6S8V; -.
DR PDBsum; 6SUA; -.
DR PDBsum; 6Z2C; -.
DR PDBsum; 6Z6Z; -.
DR AlphaFoldDB; P80188; -.
DR BMRB; P80188; -.
DR SMR; P80188; -.
DR BioGRID; 110126; 198.
DR DIP; DIP-29952N; -.
DR IntAct; P80188; 82.
DR MINT; P80188; -.
DR STRING; 9606.ENSP00000362108; -.
DR BindingDB; P80188; -.
DR DrugBank; DB02710; 2,3,-Dihydroxybenzoylserine.
DR DrugBank; DB01672; 2,3-Dihydroxy-Benzoic Acid.
DR DrugBank; DB01926; Carboxymycobactin S.
DR DrugBank; DB04043; Carboxymycobactin T.
DR DrugBank; DB01631; Methyl nonanoate.
DR DrugBank; DB04476; Trencam-3,2-Hopo.
DR MoonDB; P80188; Predicted.
DR GlyConnect; 1565; 6 N-Linked glycans (1 site).
DR GlyGen; P80188; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; P80188; -.
DR PhosphoSitePlus; P80188; -.
DR BioMuta; LCN2; -.
DR DMDM; 1171700; -.
DR CPTAC; CPTAC-681; -.
DR EPD; P80188; -.
DR jPOST; P80188; -.
DR MassIVE; P80188; -.
DR MaxQB; P80188; -.
DR PaxDb; P80188; -.
DR PeptideAtlas; P80188; -.
DR PRIDE; P80188; -.
DR ProteomicsDB; 57669; -. [P80188-1]
DR ProteomicsDB; 57670; -. [P80188-2]
DR ABCD; P80188; 2 sequenced antibodies.
DR Antibodypedia; 1059; 1716 antibodies from 47 providers.
DR DNASU; 3934; -.
DR Ensembl; ENST00000277480.7; ENSP00000277480.2; ENSG00000148346.12. [P80188-1]
DR Ensembl; ENST00000373017.5; ENSP00000362108.1; ENSG00000148346.12. [P80188-1]
DR GeneID; 3934; -.
DR KEGG; hsa:3934; -.
DR MANE-Select; ENST00000277480.7; ENSP00000277480.2; NM_005564.5; NP_005555.2.
DR UCSC; uc004bto.1; human. [P80188-1]
DR CTD; 3934; -.
DR DisGeNET; 3934; -.
DR GeneCards; LCN2; -.
DR HGNC; HGNC:6526; LCN2.
DR HPA; ENSG00000148346; Tissue enhanced (bone marrow, gallbladder, salivary gland).
DR MIM; 600181; gene.
DR neXtProt; NX_P80188; -.
DR OpenTargets; ENSG00000148346; -.
DR PharmGKB; PA30309; -.
DR VEuPathDB; HostDB:ENSG00000148346; -.
DR eggNOG; ENOG502T7VZ; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR InParanoid; P80188; -.
DR OMA; IDKCIDD; -.
DR OrthoDB; 1341030at2759; -.
DR PhylomeDB; P80188; -.
DR TreeFam; TF336103; -.
DR PathwayCommons; P80188; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6799990; Metal sequestration by antimicrobial proteins.
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR SignaLink; P80188; -.
DR SIGNOR; P80188; -.
DR BioGRID-ORCS; 3934; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; LCN2; human.
DR EvolutionaryTrace; P80188; -.
DR GeneWiki; LCN2; -.
DR GenomeRNAi; 3934; -.
DR Pharos; P80188; Tbio.
DR PRO; PR:P80188; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P80188; protein.
DR Bgee; ENSG00000148346; Expressed in palpebral conjunctiva and 145 other tissues.
DR ExpressionAtlas; P80188; baseline and differential.
DR Genevisible; P80188; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1903981; F:enterobactin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0097577; P:sequestering of iron ion; IDA:UniProtKB.
DR GO; GO:0015891; P:siderophore transport; ISS:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR003087; LCN2/LCN12.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01275; NGELATINASE.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Ion transport; Iron; Iron transport;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:7683678"
FT CHAIN 21..198
FT /note="Neutrophil gelatinase-associated lipocalin"
FT /id="PRO_0000017933"
FT BINDING 72..74
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U"
FT BINDING 126
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0007744|PDB:3CMP"
FT BINDING 145
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000269|PubMed:15642259,
FT ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U"
FT BINDING 154
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000269|PubMed:15642259,
FT ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U"
FT BINDING 154
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0007744|PDB:3CMP"
FT BINDING 158
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000269|PubMed:15642259,
FT ECO:0007744|PDB:1X89, ECO:0007744|PDB:1X8U"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:7683678"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10684642,
FT ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:16740002, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:7683678, ECO:0007744|PDB:1DFV,
FT ECO:0007744|PDB:1QQS"
FT DISULFID 96..195
FT /evidence="ECO:0000269|PubMed:10339412,
FT ECO:0000269|PubMed:10684642, ECO:0000269|PubMed:12453412,
FT ECO:0007744|PDB:1DFV, ECO:0007744|PDB:1L6M,
FT ECO:0007744|PDB:1NGL, ECO:0007744|PDB:1QQS,
FT ECO:0007744|PDB:1X71, ECO:0007744|PDB:1X89,
FT ECO:0007744|PDB:1X8U, ECO:0007744|PDB:3BY0,
FT ECO:0007744|PDB:3CBC, ECO:0007744|PDB:3CMP,
FT ECO:0007744|PDB:3DSZ, ECO:0007744|PDB:3DTQ,
FT ECO:0007744|PDB:3FW4, ECO:0007744|PDB:3FW5,
FT ECO:0007744|PDB:3HWD, ECO:0007744|PDB:3HWE,
FT ECO:0007744|PDB:3HWF, ECO:0007744|PDB:3HWG,
FT ECO:0007744|PDB:3I0A, ECO:0007744|PDB:3K3L,
FT ECO:0007744|PDB:3PEC, ECO:0007744|PDB:3PED,
FT ECO:0007744|PDB:3T1D, ECO:0007744|PDB:3TF6,
FT ECO:0007744|PDB:3TZS, ECO:0007744|PDB:3U0D,
FT ECO:0007744|PDB:4GH7, ECO:0007744|PDB:4IAW,
FT ECO:0007744|PDB:4IAX, ECO:0007744|PDB:4K19,
FT ECO:0007744|PDB:4MVI, ECO:0007744|PDB:4MVK,
FT ECO:0007744|PDB:4MVL, ECO:0007744|PDB:4QAE,
FT ECO:0007744|PDB:4ZFX, ECO:0007744|PDB:4ZHC,
FT ECO:0007744|PDB:4ZHD, ECO:0007744|PDB:4ZHF,
FT ECO:0007744|PDB:4ZHG, ECO:0007744|PDB:4ZHH,
FT ECO:0007744|PDB:5JR8, ECO:0007744|PDB:5KHP,
FT ECO:0007744|PDB:5KIC, ECO:0007744|PDB:5KID,
FT ECO:0007744|PDB:5MHH, ECO:0007744|PDB:5N47,
FT ECO:0007744|PDB:5N48, ECO:0007744|PDB:5NKN,
FT ECO:0007744|PDB:6O5D"
FT VAR_SEQ 193..198
FT /note="DQCIDG -> GNGQSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039780"
FT MUTAGEN 145
FT /note="K->A: Strongly reduced affinity for catecholate-type
FT ferric siderophores; when associated with A-154."
FT /evidence="ECO:0000269|PubMed:20581821"
FT MUTAGEN 154
FT /note="K->A: Strongly reduced affinity for catecholate-type
FT ferric siderophores; when associated with A-145."
FT /evidence="ECO:0000269|PubMed:20581821"
FT CONFLICT 9
FT /note="G -> R (in Ref. 3; BAG63166)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="L -> S (in Ref. 4; CAG46889)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="K -> N (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="I -> V (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="S -> Y (in Ref. 2; CAA67574)"
FT /evidence="ECO:0000305"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6GQZ"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:4MVK"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6Z2C"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6GQZ"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1NGL"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:6GQZ"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 135..147
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 150..162
FT /evidence="ECO:0007829|PDB:6GQZ"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:6GQZ"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6GQZ"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6GQZ"
SQ 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
