NGAL_MOUSE
ID NGAL_MOUSE Reviewed; 200 AA.
AC P11672; Q3UE34;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Neutrophil gelatinase-associated lipocalin;
DE Short=NGAL;
DE AltName: Full=Lipocalin-2;
DE AltName: Full=Oncogene 24p3 {ECO:0000303|PubMed:1834059};
DE Short=24p3 {ECO:0000303|PubMed:2542864};
DE AltName: Full=SV-40-induced 24p3 protein {ECO:0000303|PubMed:2542864};
DE AltName: Full=Siderocalin LCN2;
DE AltName: Full=p25;
DE Flags: Precursor;
GN Name=Lcn2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J; TISSUE=Kidney;
RX PubMed=2542864;
RA Hraba-Renevey S., Turler H., Kress M., Salomon C., Weil R.;
RT "SV40-induced expression of mouse gene 24p3 involves a post-transcriptional
RT mechanism.";
RL Oncogene 4:601-608(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8666241; DOI=10.1016/0378-1119(95)00896-9;
RA Garay-Rojas E., Harper M., Hraba-Renevey S., Kress M.;
RT "An apparent autocrine mechanism amplifies the dexamethasone- and retinoic
RT acid-induced expression of mouse lipocalin-encoding gene 24p3.";
RL Gene 170:173-180(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-200, PARTIAL PROTEIN SEQUENCE,
RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8687399; DOI=10.1042/bj3160545;
RA Chu S.T., Huang H.L., Chen J.M., Chen Y.H.;
RT "Demonstration of a glycoprotein derived from the 24p3 gene in mouse
RT uterine luminal fluid.";
RL Biochem. J. 316:545-550(1996).
RN [8]
RP SIMILARITY TO THE LIPOCALIN FAMILY.
RX PubMed=1723819; DOI=10.1016/0968-0004(91)90149-p;
RA Peitsch M.C., Boguski M.S.;
RT "The first lipocalin with enzymatic activity.";
RL Trends Biochem. Sci. 16:363-363(1991).
RN [9]
RP SIMILARITY TO THE LIPOCALIN FAMILY.
RX PubMed=1834059; DOI=10.1016/s0006-291x(05)81256-2;
RA Flower D.R., North A.C.T., Attwood T.K.;
RT "Mouse oncogene protein 24p3 is a member of the lipocalin protein family.";
RL Biochem. Biophys. Res. Commun. 180:69-74(1991).
RN [10]
RP FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
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 [11]
RP FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RX PubMed=15531878; DOI=10.1038/nature03104;
RA Flo T.H., Smith K.D., Sato S., Rodriguez D.J., Holmes M.A., Strong R.K.,
RA Akira S., Aderem A.;
RT "Lipocalin 2 mediates an innate immune response to bacterial infection by
RT sequestrating iron.";
RL Nature 432:917-921(2004).
RN [12]
RP FUNCTION, INTERACTION WITH SLC22A17, IRON-BINDING, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16377569; DOI=10.1016/j.cell.2005.10.027;
RA Devireddy L.R., Gazin C., Zhu X., Green M.R.;
RT "A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis
RT and iron uptake.";
RL Cell 123:1293-1305(2005).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=16446425; DOI=10.1073/pnas.0510847103;
RA Berger T., Togawa A., Duncan G.S., Elia A.J., You-Ten A., Wakeham A.,
RA Fong H.E., Cheung C.C., Mak T.W.;
RT "Lipocalin 2-deficient mice exhibit increased sensitivity to Escherichia
RT coli infection but not to ischemia-reperfusion injury.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:1834-1839(2006).
RN [14]
RP FUNCTION, IRON-BINDING, SIDEROPHORE-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=20550936; DOI=10.1016/j.cell.2010.04.040;
RA Devireddy L.R., Hart D.O., Goetz D.H., Green M.R.;
RT "A mammalian siderophore synthesized by an enzyme with a bacterial homolog
RT involved in enterobactin production.";
RL Cell 141:1006-1017(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16] {ECO:0007744|PDB:3S26}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-200, DISULFIDE BOND, AND
RP GLYCOSYLATION AT ASN-85.
RX PubMed=21911364; DOI=10.1093/nar/gkr706;
RA Bandaranayake A.D., Correnti C., Ryu B.Y., Brault M., Strong R.K.,
RA Rawlings D.J.;
RT "Daedalus: a robust, turnkey platform for rapid production of decigram
RT quantities of active recombinant proteins in human cell lines using novel
RT lentiviral vectors.";
RL Nucleic Acids Res. 39:E143-E143(2011).
CC -!- FUNCTION: Iron-trafficking protein involved in multiple processes such
CC as apoptosis, innate immunity and renal development (PubMed:12453413).
CC Binds iron through association with 2,3-dihydroxybenzoic acid (2,3-
CC DHBA), a siderophore that shares structural similarities with bacterial
CC enterobactin, and delivers or removes iron from the cell, depending on
CC the context. Iron-bound form (holo-24p3) is internalized following
CC binding to the SLC22A17 (24p3R) receptor, leading to release of iron
CC and subsequent increase of intracellular iron concentration. In
CC contrast, association of the iron-free form (apo-24p3) with the
CC SLC22A17 (24p3R) receptor is followed by association with an
CC intracellular siderophore, iron chelation and iron transfer to the
CC extracellular medium, thereby reducing intracellular iron
CC 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. Involved in
CC innate immunity; limits bacterial proliferation by sequestering iron
CC bound to microbial siderophores, such as enterobactin (PubMed:15531878,
CC PubMed:16446425). Can also bind siderophores from M.tuberculosis (By
CC similarity). {ECO:0000250|UniProtKB:P80188,
CC ECO:0000269|PubMed:12453413, ECO:0000269|PubMed:15531878,
CC ECO:0000269|PubMed:16377569, ECO:0000269|PubMed:16446425,
CC ECO:0000269|PubMed:20550936}.
CC -!- SUBUNIT: Monomer. Homodimer; disulfide-linked. Heterodimer; disulfide-
CC linked with MMP9. {ECO:0000250|UniProtKB:P80188}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12453413,
CC ECO:0000269|PubMed:20550936, ECO:0000269|PubMed:8687399}. Cytoplasmic
CC granule lumen {ECO:0000250|UniProtKB:P80188}. Cytoplasmic vesicle lumen
CC {ECO:0000250|UniProtKB:P80188}. Note=Upon binding to the SLC22A17
CC (24p3R) receptor, it is internalized (PubMed:16377569). Releases the
CC bound iron in the acidic lumen of cytoplasmic vesicles (By similarity).
CC {ECO:0000250|UniProtKB:P80188, ECO:0000269|PubMed:16377569}.
CC -!- TISSUE SPECIFICITY: Detected in lung, spleen, uterus, vagina and
CC epididymis. {ECO:0000269|PubMed:8687399}.
CC -!- INDUCTION: Upon Toll-like receptor (TLRs) stimuli. By SV-40.
CC {ECO:0000269|PubMed:15531878}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:21911364,
CC ECO:0000269|PubMed:8687399}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal with no visible phenotype. They
CC however show an increased susceptibility to bacterial infections.
CC Neutrophils show significantly less bacteriostatic activity.
CC {ECO:0000269|PubMed:15531878, ECO:0000269|PubMed:16446425}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X14607; CAA32762.1; -; mRNA.
DR EMBL; X81627; CAA57283.1; -; Genomic_DNA.
DR EMBL; AK149774; BAE29077.1; -; mRNA.
DR EMBL; AL808027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08545.1; -; Genomic_DNA.
DR EMBL; BC132069; AAI32070.1; -; mRNA.
DR EMBL; BC132071; AAI32072.1; -; mRNA.
DR EMBL; S82469; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15913.1; -.
DR PIR; S07397; S07397.
DR RefSeq; NP_032517.1; NM_008491.1.
DR PDB; 3S26; X-ray; 1.80 A; A=21-200.
DR PDB; 3U9P; X-ray; 2.80 A; C/D=21-200.
DR PDBsum; 3S26; -.
DR PDBsum; 3U9P; -.
DR AlphaFoldDB; P11672; -.
DR SMR; P11672; -.
DR BioGRID; 201121; 3.
DR IntAct; P11672; 1.
DR STRING; 10090.ENSMUSP00000053962; -.
DR GlyGen; P11672; 2 sites.
DR iPTMnet; P11672; -.
DR PhosphoSitePlus; P11672; -.
DR EPD; P11672; -.
DR MaxQB; P11672; -.
DR PaxDb; P11672; -.
DR PeptideAtlas; P11672; -.
DR PRIDE; P11672; -.
DR ProteomicsDB; 287504; -.
DR ABCD; P11672; 1 sequenced antibody.
DR Antibodypedia; 1059; 1716 antibodies from 47 providers.
DR DNASU; 16819; -.
DR Ensembl; ENSMUST00000050785; ENSMUSP00000053962; ENSMUSG00000026822.
DR GeneID; 16819; -.
DR KEGG; mmu:16819; -.
DR UCSC; uc008jfl.1; mouse.
DR CTD; 3934; -.
DR MGI; MGI:96757; Lcn2.
DR VEuPathDB; HostDB:ENSMUSG00000026822; -.
DR eggNOG; ENOG502T7VZ; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_2_0_1; -.
DR InParanoid; P11672; -.
DR OMA; IDKCIDD; -.
DR OrthoDB; 1341030at2759; -.
DR PhylomeDB; P11672; -.
DR TreeFam; TF336103; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6799990; Metal sequestration by antimicrobial proteins.
DR Reactome; R-MMU-917937; Iron uptake and transport.
DR BioGRID-ORCS; 16819; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Lcn2; mouse.
DR PRO; PR:P11672; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P11672; protein.
DR Bgee; ENSMUSG00000026822; Expressed in granulocyte and 119 other tissues.
DR ExpressionAtlas; P11672; baseline and differential.
DR Genevisible; P11672; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0060205; C:cytoplasmic vesicle lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:1903981; F:enterobactin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:1905956; P:positive regulation of endothelial tube morphogenesis; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:1904440; P:positive regulation of iron ion import across plasma membrane; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0009635; P:response to herbicide; ISO:MGI.
DR GO; GO:0009615; P:response to virus; IDA:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0097577; P:sequestering of iron ion; ISS:UniProtKB.
DR GO; GO:0007614; P:short-term memory; ISO:MGI.
DR GO; GO:0015891; P:siderophore transport; IDA: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; Apoptosis; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Innate immunity; Ion transport;
KW Iron; Iron transport; Pyrrolidone carboxylic acid; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..200
FT /note="Neutrophil gelatinase-associated lipocalin"
FT /id="PRO_0000017934"
FT BINDING 72..74
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT BINDING 128
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT BINDING 147
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT BINDING 156
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT BINDING 156
FT /ligand="enterobactin"
FT /ligand_id="ChEBI:CHEBI:77805"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT BINDING 160
FT /ligand="a carboxymycobactin"
FT /ligand_id="ChEBI:CHEBI:178051"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P80188"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21911364"
FT DISULFID 98..197
FT /evidence="ECO:0000269|PubMed:21911364"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3S26"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:3S26"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3U9P"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:3S26"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 137..149
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 152..164
FT /evidence="ECO:0007829|PDB:3S26"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:3S26"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:3S26"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3S26"
SQ 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
