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Neutrophil gelatinase-associated lipocalin (NGAL) (Alpha-2-microglobulin-related protein) (Alpha-2U globulin-related protein) (Lipocalin-2) (Siderocalin LCN2) (p25)

 NGAL_RAT                Reviewed;         198 AA.
P30152; Q5HZF1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 2.
31-JAN-2018, entry version 126.
RecName: Full=Neutrophil gelatinase-associated lipocalin;
Short=NGAL;
AltName: Full=Alpha-2-microglobulin-related protein;
AltName: Full=Alpha-2U globulin-related protein;
AltName: Full=Lipocalin-2;
AltName: Full=Siderocalin LCN2;
AltName: Full=p25;
Flags: Precursor;
Name=Lcn2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2462726; DOI=10.1093/nar/16.23.11368;
Chan Y.-L., Paz V., Wool I.G.;
"The primary structure of rat alpha 2 mu globulin-related protein.";
Nucleic Acids Res. 16:11368-11368(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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).
[3]
STRUCTURE BY NMR OF 21-198, AND DISULFIDE BOND.
PubMed=21538546; DOI=10.1002/prot.23031;
Peng Y., Zhang X., Liu J., Liu Q., Guo C., Zhang Y., Lin D.;
"Solution structure of the protein lipocalin 12 from rat epididymis.";
Proteins 79:2316-2320(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 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer; disulfide-
linked with MMP9 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Upon binding to
the SLC22A17 (24p3R) receptor, it is internalized. {ECO:0000250}.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
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EMBL; X13295; CAA31657.1; -; mRNA.
EMBL; BC089053; AAH89053.1; -; mRNA.
PIR; S01989; S01989.
RefSeq; NP_570097.1; NM_130741.1.
UniGene; Rn.11303; -.
PDB; 2K23; NMR; -; A=21-198.
PDBsum; 2K23; -.
ProteinModelPortal; P30152; -.
SMR; P30152; -.
STRING; 10116.ENSRNOP00000018776; -.
iPTMnet; P30152; -.
PhosphoSitePlus; P30152; -.
PaxDb; P30152; -.
PRIDE; P30152; -.
Ensembl; ENSRNOT00000018776; ENSRNOP00000018776; ENSRNOG00000013973.
GeneID; 170496; -.
KEGG; rno:170496; -.
UCSC; RGD:69408; rat.
CTD; 3934; -.
RGD; 69408; Lcn2.
eggNOG; ENOG410JAXJ; Eukaryota.
eggNOG; ENOG4111A75; LUCA.
GeneTree; ENSGT00530000063610; -.
HOGENOM; HOG000231660; -.
HOVERGEN; HBG106490; -.
InParanoid; P30152; -.
KO; K21129; -.
OMA; VPIDQCI; -.
OrthoDB; EOG091G0R03; -.
PhylomeDB; P30152; -.
TreeFam; TF336103; -.
Reactome; R-RNO-6798695; Neutrophil degranulation.
Reactome; R-RNO-6799990; Metal sequestration by antimicrobial proteins.
Reactome; R-RNO-917937; Iron uptake and transport.
EvolutionaryTrace; P30152; -.
PRO; PR:P30152; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000013973; -.
Genevisible; P30152; RN.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0031669; P:cellular response to nutrient levels; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
GO; GO:0031346; P:positive regulation of cell projection organization; IDA:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IDA:RGD.
GO; GO:0070207; P:protein homotrimerization; IDA:RGD.
GO; GO:0009617; P:response to bacterium; IEP:RGD.
GO; GO:0042493; P:response to drug; IMP:RGD.
GO; GO:0009635; P:response to herbicide; IDA:RGD.
GO; GO:0010046; P:response to mycotoxin; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
GO; GO:0009615; P:response to virus; ISO:RGD.
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; IPR000566; Lipocln_cytosolic_FA-bd_dom.
PANTHER; PTHR11430; PTHR11430; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01275; NGELATINASE.
SUPFAM; SSF50814; SSF50814; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Complete proteome; 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 21 198 Neutrophil gelatinase-associated
lipocalin.
/FTId=PRO_0000017935.
BINDING 126 126 Catecholate-type ferric siderophore.
{ECO:0000250}.
BINDING 145 145 Catecholate-type ferric siderophore.
{ECO:0000250}.
BINDING 154 154 Catecholate-type ferric siderophore.
{ECO:0000250}.
MOD_RES 21 21 Pyrrolidone carboxylic acid.
{ECO:0000250|UniProtKB:P80188}.
CARBOHYD 85 85 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 96 195 {ECO:0000269|PubMed:21538546}.
CONFLICT 18 18 S -> R (in Ref. 1; CAA31657).
{ECO:0000305}.
CONFLICT 58 58 G -> A (in Ref. 1; CAA31657).
{ECO:0000305}.
HELIX 33 35 {ECO:0000244|PDB:2K23}.
HELIX 44 47 {ECO:0000244|PDB:2K23}.
STRAND 49 58 {ECO:0000244|PDB:2K23}.
STRAND 64 66 {ECO:0000244|PDB:2K23}.
STRAND 73 78 {ECO:0000244|PDB:2K23}.
STRAND 84 90 {ECO:0000244|PDB:2K23}.
STRAND 97 105 {ECO:0000244|PDB:2K23}.
STRAND 111 114 {ECO:0000244|PDB:2K23}.
HELIX 117 119 {ECO:0000244|PDB:2K23}.
STRAND 121 132 {ECO:0000244|PDB:2K23}.
STRAND 135 137 {ECO:0000244|PDB:2K23}.
STRAND 139 147 {ECO:0000244|PDB:2K23}.
STRAND 150 162 {ECO:0000244|PDB:2K23}.
HELIX 166 178 {ECO:0000244|PDB:2K23}.
HELIX 183 185 {ECO:0000244|PDB:2K23}.
STRAND 193 195 {ECO:0000244|PDB:2K23}.
SEQUENCE 198 AA; 22476 MW; 7673F036DCA5654E CRC64;
MGLGVLCLAL VLLGVLQSQA QDSTQNLIPA PPLISVPLQP GFWTERFQGR WFVVGLAGNA
VQKERQSRFT MYSTIYELQE DNSYNVTSIL VRGQGCRYWI RTFVPSSRPG QFTLGNIHSY
PQIQSYDVQV ADTDYDQFAM VFFQKTSENK QYFKVTLYGR TKGLSDELKE RFVSFAKSLG
LKDNNIVFSV PTDQCIDN


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