Hemoglobin subunit alpha - Mus musculus (Mouse)

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P01942 (HBA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. History...

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

Documents (3) |

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:
Hemoglobin subunit alpha

Alternative name(s):
Alpha-globin
Hemoglobin alpha chain

Gene names

Name:	Hba
Synonyms:	Hba-a1

Organism

Mus musculus (Mouse) [Reference proteome]

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	142 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	Involved in oxygen transport from the lung to the various peripheral tissues.
Subunit structure	Heterotetramer of two alpha chains and two beta chains.
Tissue specificity	Red blood cells.
Polymorphism	In inbred mouse strains there are at least 6 alleles that can occur at the HBA locus: A, B, C, D, F, or G. Strains carrying the A and F alleles produce a single kind of alpha chain, whereas those carrying B, C, D, or G each produce 2 kinds of chains. The sequence shown is that of the B₁ and D₁ allele chains.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Coding sequence diversity	Polymorphism
Ligand	Heme Iron Metal-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to stilbenoid Inferred from expression pattern PubMed 17086191. Source: UniProtKB
Cellular_component	hemoglobin complex Inferred from electronic annotation. Source: InterPro
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.2

Chain

2 – 142

141

Hemoglobin subunit alpha

PRO_0000052694

Sites

Metal binding

Iron (heme distal ligand)

Metal binding

Iron (heme proximal ligand)

Amino acid modifications

Modified residue

N6-acetyllysine By similarity

Natural variations

Natural variant

G → V in allele chain C(1) and in strain NB. Ref.6 Ref.7 Ref.8

Natural variant

V → I in allele chain C(1) and in strain NB. Ref.6 Ref.7 Ref.8

Natural variant

S → N in allele chains A, C(2), D(2), F, G(1) and G(2) and in strain C57BL. Ref.6 Ref.7 Ref.8

Natural variant

S → T in allele chain B(2) and in 1 BALB/C strain sequence. Ref.6 Ref.7 Ref.8

Natural variant

G → A in allele chains F and G(2). Ref.6 Ref.7 Ref.8

Secondary structure

142

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P01942 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 2F70043BFF66E24A
Show »

FASTA

142

15,085

        10         20         30         40         50         60 
MVLSGEDKSN IKAAWGKIGG HGAEYGAEAL ERMFASFPTT KTYFPHFDVS HGSAQVKGHG 

        70         80         90        100        110        120 
KKVADALASA AGHLDDLPGA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL ASHHPADFTP 

       130        140 
AVHASLDKFL ASVSTVLTSK YR

« Hide

References

[1]	"The complete sequence of a chromosomal mouse alpha-globin gene reveals elements conserved throughout vertebrate evolution." Nishioka Y., Leder P. Cell 18:875-882(1979) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: BALB/c.
[2]	"Hemoglobins of mice: sequence and possible ambiguity at one position of the alpha chain." Popp R.A. J. Mol. Biol. 27:9-16(1967) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142. Strain: BALB/c, C57BL/6 and NB.
[3]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 18-57; 94-100 AND 129-140, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[4]	"Comparison of cloned mouse alpha- and beta-globin genes: conservation of intervening sequence locations and extragenic homology." Leder A., Miller H.I., Hamer D.H., Seidman J.G., Norman B., Sullivan M., Leder P. Proc. Natl. Acad. Sci. U.S.A. 75:6187-6191(1978) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-99.
[5]	"Characterization and kinetics of synthesis of 15S beta-globin RNA, a putative precursor of beta-globin mRNA." Curtis P.J., Mantei N., Weissmann C. Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 84-109.
[6]	"Studies on the mouse hemoglobin loci. 8. A fourth alpha-chain phenotype." Popp R.A. J. Hered. 60:126-133(1969) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
[7]	Popp R.A. (In) Altman P.A., Katz D.D. (eds.); Inbred and genetically defined strains of laboratory animals, pp.105-105, Federation of American Societies for Experimental Biology, Bethesda (1979) Cited for: VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
[8]	"The primary structure of genetic variants of mouse hemoglobin." Popp R.A., Bailiff E.G., Skow L.C., Whitney J.B. III Biochem. Genet. 20:199-208(1982) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00714 Genomic DNA. Translation: CAA24095.1.
M10703 Genomic DNA. Translation: AAA37782.2.
M10840 mRNA. Translation: AAA37784.1.

IPI

IPI00469114.

PIR

HAMS. A90791.

UniGene

Mm.196110.
Mm.459653.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HRW	X-ray	2.80	A/C	2-142	[»]

ProteinModelPortal

P01942.

SMR

P01942. Positions 2-142.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34118N.

IntAct

P01942. 6 interactions.

PTM databases

PhosphoSite

P01942.

2D gel databases

REPRODUCTION-2DPAGE

IPI00469114.
P01942.

SWISS-2DPAGE

P01942.

Proteomic databases

PaxDb

P01942.

PRIDE

P01942.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Organism-specific databases

MGI

MGI:96015. Hba-a1.

Phylogenomic databases

eggNOG

NOG283543.

HOGENOM

HOG000036867.

HOVERGEN

HBG009709.

InParanoid

P01942.

OrthoDB

EOG47M209.

Gene expression databases

CleanEx

MM_HBA-A1.

Genevestigator

P01942.

GermOnline

ENSMUSG00000069917. Mus musculus.
ENSMUSG00000069919. Mus musculus.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR002338. Haemoglobin_a.
IPR018331. Haemoglobin_alpha_chain.
IPR002339. Haemoglobin_pi.
[Graphical view]

PANTHER

PTHR11442:SF14. PTHR11442:SF14. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00612. ALPHAHAEM.
PR00815. PIHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P01942.

SOURCE

Search...

Entry information

Entry name

HBA_MOUSE

Accession

Primary (citable) accession number: P01942

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 119 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

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

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents