Neutrophil gelatinase-associated lipocalin precursor

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P30152 (NGAL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Neutrophil gelatinase-associated lipocalin
Short name=NGAL

Alternative name(s):
Alpha-2-microglobulin-related protein
Alpha-2U globulin-related protein
Lipocalin-2
p25

Gene names

Name:

Lcn2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	198 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Homodimer; disulfide-linked. Heterodimer; disulfide-linked with MMP9 By similarity.
Subcellular location	Secreted By similarity. Note: Upon binding to the SLC22A17 (24p3R) receptor, it is internalized By similarity.
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Biological process	Apoptosis Immunity Innate immunity Ion transport Iron transport Transport
Cellular component	Secreted
Domain	Signal
Ligand	Iron
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to hydrogen peroxide Inferred from direct assay. Source: RGD cellular response to interleukin-1 Inferred from expression pattern. Source: RGD cellular response to lipopolysaccharide Inferred from expression pattern. Source: RGD cellular response to nutrient levels Inferred from expression pattern. Source: RGD cellular response to tumor necrosis factor Inferred from expression pattern. Source: RGD innate immune response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell projection organization Inferred from direct assay. Source: RGD positive regulation of gene expression Inferred from direct assay. Source: RGD protein homotrimerization Inferred from direct assay. Source: RGD regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from mutant phenotype. Source: RGD response to herbicide Inferred from direct assay. Source: RGD siderophore transport Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay. Source: RGD extracellular space Inferred from direct assay. Source: RGD
Molecular function	iron ion binding Inferred from sequence or structural similarity. Source: UniProtKB protease binding Inferred from physical interaction. Source: RGD protein homodimerization activity Inferred from direct assay. Source: RGD transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

By similarity

Chain

21 – 198

178

Neutrophil gelatinase-associated lipocalin

PRO_0000017935

Sites

Binding site

126

Catecholate-type ferric siderophore By similarity

Binding site

145

Catecholate-type ferric siderophore By similarity

Binding site

154

Catecholate-type ferric siderophore By similarity

Amino acid modifications

Modified residue

Pyrrolidone carboxylic acid By similarity

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

96 ↔ 195

By similarity

Experimental info

Sequence conflict

S → R in CAA31657. Ref.1

Sequence conflict

G → A in CAA31657. Ref.1

Secondary structure

198

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P30152 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 7673F036DCA5654E
Show »

FASTA

198

22,476

        10         20         30         40         50         60 
MGLGVLCLAL VLLGVLQSQA QDSTQNLIPA PPLISVPLQP GFWTERFQGR WFVVGLAGNA 

        70         80         90        100        110        120 
VQKERQSRFT MYSTIYELQE DNSYNVTSIL VRGQGCRYWI RTFVPSSRPG QFTLGNIHSY 

       130        140        150        160        170        180 
PQIQSYDVQV ADTDYDQFAM VFFQKTSENK QYFKVTLYGR TKGLSDELKE RFVSFAKSLG 

       190 
LKDNNIVFSV PTDQCIDN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of rat alpha 2 mu globulin-related protein." Chan Y.-L., Paz V., Wool I.G. Nucleic Acids Res. 16:11368-11368(1988) [PubMed: 2462726] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Ovary.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X13295 mRNA. Translation: CAA31657.1.
BC089053 mRNA. Translation: AAH89053.1.

IPI

IPI00205907.

PIR

S01989.

RefSeq

NP_570097.1. NM_130741.1.

UniGene

Rn.11303.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K23	NMR	-	A	21-198	[»]

ProteinModelPortal

P30152.

SMR

P30152. Positions 21-197.

ModBase

Search...

Protein-protein interaction databases

STRING

P30152.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000018776; ENSRNOP00000018776; ENSRNOG00000013973.

GeneID

170496.

KEGG

rno:170496.

UCSC

NM_130741. rat.

Organism-specific databases

CTD

3934.

RGD

69408. Lcn2.

Phylogenomic databases

eggNOG

roNOG16531.

GeneTree

ENSGT00530000063610.

HOVERGEN

HBG106490.

InParanoid

P30152.

OMA

PIDQCID.

OrthoDB

EOG447FVG.

PhylomeDB

P30152.

Gene expression databases

ArrayExpress

P30152.

Genevestigator

P30152.

GermOnline

ENSRNOG00000013973. Rattus norvegicus.

Family and domain databases

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR003087. N_gelatinase.
[Graphical view]

Gene3D

G3DSA:2.40.128.20. Calycin. 1 hit.

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00179. LIPOCALIN.
PR01275. NGELATINASE.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

620993.

Entry information

Entry name

NGAL_RAT

Accession

Primary (citable) accession number: P30152
Secondary accession number(s): Q5HZF1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	October 5, 2010
Last modified:	December 14, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents