Reviewed, UniProtKB/Swiss-Prot P80188 (NGAL_HUMAN)

Names and origin

Protein names

Recommended name:
    Neutrophil gelatinase-associated lipocalin
      Short name=NGAL
Alternative name(s):
    p25
    25 kDa alpha-2-microglobulin-related subunit of MMP-9
    Lipocalin-2
    Oncogene 24p3

Gene names

Name:	LCN2
Synonyms:	HNL, NGAL

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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	Transport of small lipophilic substances Potential.
Subunit structure	Forms a covalently linked, disulfide-bridged heterodimer with the 92 kDa type V collagenase (MMP-9).
Subcellular location	Secreted.
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 lungs. Not found in the small intestine or peripheral blood leukocytes. Ref.2
Sequence similarities	Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro 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

20

Ref.5

Chain

21 – 198

178

Neutrophil gelatinase-associated lipocalin

PRO_0000017933

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid Ref.5

Glycosylation

85

1

N-linked (GlcNAc...) Ref.5 Ref.7 Ref.8 Ref.9 Ref.10

Disulfide bond

96 ↔ 195

Experimental info

Sequence conflict

82

1

K → N AA sequence Ref.6

Sequence conflict

155

1

I → V AA sequence Ref.6

Sequence conflict

178

1

S → Y in CAA67574. Ref.2

Secondary structure

1

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198

Helix Strand Turn

Details...

Helix

33 – 35

3

Turn

44 – 47

4

Beta strand

49 – 58

10

Beta strand

65 – 67

3

Beta strand

73 – 78

6

Beta strand

84 – 92

9

Beta strand

95 – 105

11

Beta strand

111 – 114

4

Helix

117 – 119

3

Beta strand

123 – 133

11

Beta strand

135 – 147

13

Beta strand

150 – 162

13

Helix

166 – 177

12

Turn

178 – 180

3

Helix

183 – 185

3

Turn

194 – 196

3

Sequences

	Sequence		Length	Mass (Da)
	P80188-1 [UniParc]. Last modified November 1, 1995. Version 2. Checksum: CD761805723FEF1E	FASTA	198	22,588
	10 20 30 40 50 60 MPLGLLWLGL ALLGALHAQA QDSTSDLIPA PPLSKVPLQQ NFQDNQFQGK WYVVGLAGNA 70 80 90 100 110 120 ILREDKDPQK MYATIYELKE DKSYNVTSVL FRKKKCDYWI RTFVPGCQPG EFTLGNIKSY 130 140 150 160 170 180 PGLTSYLVRV VSTNYNQHAM VFFKKVSQNR EYFKITLYGR TKELTSELKE NFIRFSKSLG 190 LPENHIVFPV PIDQCIDG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a cDNA encoding NGAL: a lipocalin expressed in human neutrophils." Bundgaard J.R., Sengelov H., Borregaard N., Kjeldsen L. Biochem. Biophys. Res. Commun. 202:1468-1475(1994) [PubMed: 8060329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular characterization and pattern of tissue expression of the gene for neutrophil gelatinase-associated lipocalin from humans." Cowland J.B., Borregaard N. Genomics 45:17-23(1997) [PubMed: 9339356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Tissue: Bone marrow.
[3]	"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: Pancreas.
[4]	"Cloning and expression of human neutrophil lipocalin cDNA derived from bone marrow and ovarian cancer cells." Bartsch S., Tschesche H. FEBS Lett. 357:255-259(1995) [PubMed: 7835423] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-198, PARTIAL PROTEIN SEQUENCE.
[5]	"Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase." Kjeldsen L., Johnsen A.H., Sengelov H., Borregaard N. J. Biol. Chem. 268:10425-10432(1993) [PubMed: 7683678] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-198. Tissue: Neutrophil.
[6]	"A 25 kDa alpha 2-microglobulin-related protein is a component of the 125 kDa form of human gelatinase." Triebel S., Blaeser J., Reinke H., Tschesche H. FEBS Lett. 314:386-388(1992) [PubMed: 1281792] [Abstract] Cited for: PROTEIN SEQUENCE OF 51-61; 71-90; 132-136; 152-160 AND 178-192. Tissue: Neutrophil.
[7]	"A proteomic analysis of human bile." Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A. Mol. Cell. Proteomics 3:715-728(2004) [PubMed: 15084671] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, MASS SPECTROMETRY. Tissue: Bile.
[8]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry." Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A. J. Proteome Res. 5:1493-1503(2006) [PubMed: 16740002] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, MASS SPECTROMETRY. Tissue: Saliva.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-85, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin." Goetz D.H., Willie S.T., Armen R.S., Bratt T., Borregaard N., Strong R.K. Biochemistry 39:1935-1941(2000) [PubMed: 10684642] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 21-298.
[12]	"The solution structure and dynamics of human neutrophil gelatinase-associated lipocalin." Coles M., Diercks T., Muehlenweg B., Bartsch S., Zolzer V., Tschesche H., Kessler H. J. Mol. Biol. 289:139-157(1999) [PubMed: 10339412] [Abstract] Cited for: STRUCTURE BY NMR OF 21-198.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X83006 mRNA. Translation: CAA58127.1.
X99133 Genomic DNA. Translation: CAA67574.1.
BC033089 mRNA. Translation: AAH33089.1.
S75256 mRNA. Translation: AAD14168.1.

IPI

IPI00299547.

PIR

JC2339.

RefSeq

NP_005555.2.

UniGene

Hs.204238

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DFV	X-ray	2.60	A/B	21-197	[»]
1L6M	X-ray	2.40	A/B/C	21-198	[»]
1NGL	NMR	-	A	21-198	[»]
1QQS	X-ray	2.40	A	24-197	[»]
1X71	X-ray	2.10	A/B/C	21-198	[»]
1X89	X-ray	2.10	A/B/C	21-198	[»]
1X8U	X-ray	2.20	A/B/C	21-198	[»]
3BY0	X-ray	2.57	A/B/C	1-198	[»]
3CBC	X-ray	2.17	A/B/C	1-198	[»]
3CMP	X-ray	2.80	A/B/C	1-198	[»]
3DSZ	X-ray	2.00	A/B	21-198	[»]
3DTQ	X-ray	2.50	A/B/C	21-198	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P80188.

Proteomic databases

PRIDE

P80188.

Genome annotation databases

Ensembl

ENST00000277480; ENSP00000277480; ENSG00000148346; Homo sapiens. [Genome view]
ENST00000372998; ENSP00000362089; ENSG00000148346; Homo sapiens. [Genome view]
ENST00000373013; ENSP00000362104; ENSG00000148346; Homo sapiens. [Genome view]
ENST00000373017; ENSP00000362108; ENSG00000148346; Homo sapiens. [Genome view]

GeneID

3934.

KEGG

hsa:3934.

UCSC

uc004bto.1. human.

Organism-specific databases

CTD

3934.

GeneCards

GC09P129951.

H-InvDB

HIX0008419.

HGNC

HGNC:6526. LCN2.

HPA

CAB016549.
CAB016550.
HPA002695.

MIM

600181. gene.

PharmGKB

PA26547.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P80188.

Gene expression databases

ArrayExpress

P80188.

Bgee

P80188.

CleanEx

HS_LCN2.

Genevestigator

P80188.

GermOnline

ENSG00000148346. Homo sapiens.

Family and domain databases

InterPro

IPR012674. Calycin.
IPR002345. Lipocalin.
IPR000566. Lipocln_cytFABP.
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.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

15451.

SOURCE

Search...

Entry information

Entry name

NGAL_HUMAN

Accession

Primary (citable) accession number: P80188
Secondary accession number(s): P30150, Q92683

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	November 1, 1995
Last modified:	October 13, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.