Q9ER97 (NGB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroglobin

Gene names

Name:

Ngb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. Ref.3 Ref.4
Subunit structure	Monomer. Homodimer and homotetramer; disulfide-linked Probable. Ref.4
Subcellular location	Perikaryon By similarity.
Tissue specificity	Predominantly expressed in brain.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Heme Iron Metal-binding
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	perikaryon Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from direct assay Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 151

151

Neuroglobin

PRO_0000053392

Regions

Region

1 – 149

149

Globin

Sites

Metal binding

64

1

Iron (heme distal ligand)

Metal binding

96

1

Iron (heme proximal ligand) By similarity

Experimental info

Mutagenesis

64

1

H → L: Improved binding of dioxygen and carbon monoxide to the iron atom. Ref.4

Secondary structure

1

.

.

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.

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.

.

.

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.

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.

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.

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151

Helix Strand Turn

Details...

Helix

6 – 17

12

Helix

20 – 34

15

Helix

36 – 41

6

Helix

52 – 55

4

Helix

59 – 77

19

Beta strand

82 – 85

4

Helix

86 – 99

14

Helix

105 – 121

17

Helix

122 – 124

3

Helix

127 – 145

19

Helix

146 – 148

3

Sequences

	Sequence		Length	Mass (Da)
	Q9ER97 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 377BBE4BF723CCF1	FASTA	151	17,037
	10 20 30 40 50 60 MERPESELIR QSWRVVSRSP LEHGTVLFAR LFALEPSLLP LFQYNGRQFS SPEDCLSSPE 70 80 90 100 110 120 FLDHIRKVML VIDAAVTNVE DLSSLEEYLT SLGRKHRAVG VRLSSFSTVG ESLLYMLEKC 130 140 150 LGPDFTPATR TAWSRLYGAV VQAMSRGWDG E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A vertebrate globin expressed in the brain." Burmester T., Weich B., Reinhardt S., Hankeln T. Nature 407:520-522(2000) [PubMed: 11029004] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[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: Liver.
[3]	"The heme environment of mouse neuroglobin. Evidence for the presence of two conformations of the heme pocket." Couture M., Burmester T., Hankeln T., Rousseau D.L. J. Biol. Chem. 276:36377-36382(2001) [PubMed: 11473111] [Abstract] Cited for: FUNCTION.
[4]	"Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family." Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V., Aerts T., Marden M.C., Caubergs R., Moens L. J. Biol. Chem. 276:38949-38955(2001) [PubMed: 11473128] [Abstract] Cited for: FUNCTION, QUATERNARY STRUCTURE, MUTAGENESIS OF HIS-64.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ245945 mRNA. Translation: CAC11135.1.
BC024263 mRNA. Translation: AAH24263.1.

IPI

IPI00111750.

RefSeq

NP_071859.1. NM_022414.2.

UniGene

Mm.41395.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q1F	X-ray	1.50	A	1-151	[»]
1W92	X-ray	1.70	A	1-151	[»]
2VRY	X-ray	1.87	A	1-151	[»]
3GK9	X-ray	1.80	A	1-151	[»]
3GKT	X-ray	1.86	A	1-151	[»]
3GLN	X-ray	2.26	A	1-151	[»]

ProteinModelPortal

Q9ER97.

SMR

Q9ER97. Positions 3-150.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9ER97.

Proteomic databases

PRIDE

Q9ER97.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000021420; ENSMUSP00000021420; ENSMUSG00000021032.

GeneID

64242.

KEGG

mmu:64242.

Organism-specific databases

CTD

58157.

MGI

MGI:2151886. Ngb.

Phylogenomic databases

GeneTree

ENSGT00510000048375.

HOVERGEN

HBG039321.

PhylomeDB

Q9ER97.

Gene expression databases

ArrayExpress

Q9ER97.

Bgee

Q9ER97.

CleanEx

MM_NGB.

Genevestigator

Q9ER97.

GermOnline

ENSMUSG00000021032. Mus musculus.

Family and domain databases

InterPro

IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR000971. Globin_subset.
[Graphical view]

Gene3D

G3DSA:1.10.490.10. Globin_related. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

319968.

SOURCE

Search...

Entry information

Entry name

NGB_MOUSE

Accession

Primary (citable) accession number: Q9ER97

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	March 1, 2001
Last modified:	December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program