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Protein

Hemoglobin subunit alpha-A

Gene

HBAA

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in oxygen transport from the lung to the various peripheral tissues.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Iron (heme distal ligand)
Metal bindingi88 – 881Iron (heme proximal ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-GGA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-GGA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-GGA-2168880. Scavenging of heme from plasma.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit alpha-A
Alternative name(s):
Alpha-A-globin
Hemoglobin alpha-A chain
Gene namesi
Name:HBAA
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 142141Hemoglobin subunit alpha-APRO_0000052599Add
BLAST

Proteomic databases

PaxDbiP01994.
PRIDEiP01994.

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038904.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 284Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YF1X-ray2.75C20-30[»]
3BEVX-ray2.10C20-30[»]
ProteinModelPortaliP01994.
SMRiP01994. Positions 2-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01994.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01994.
KOiK13822.
OMAiDKFLCAV.
PhylomeDBiP01994.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSAADKNN VKGIFTKIAG HAEEYGAETL ERMFTTYPPT KTYFPHFDLS
60 70 80 90 100
HGSAQIKGHG KKVVAALIEA ANHIDDIAGT LSKLSDLHAH KLRVDPVNFK
110 120 130 140
LLGQCFLVVV AIHHPAALTP EVHASLDKFL CAVGTVLTAK YR
Length:142
Mass (Da):15,429
Last modified:January 23, 2007 - v2
Checksum:i56847D9227928E2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901H → D in AAD32581 (Ref. 10) Curated
Sequence conflicti93 – 953RVD → TGG in CAA23678 (PubMed:6253930).Curated
Sequence conflicti111 – 1111A → T (PubMed:6894907).Curated
Sequence conflicti121 – 1211E → K in CAA23678 (PubMed:6253930).Curated
Sequence conflicti122 – 1221V → I (PubMed:6894907).Curated
Sequence conflicti128 – 1281K → N in CAA23678 (PubMed:6253930).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59989 Genomic DNA. Translation: CAA42606.1.
V00379 mRNA. Translation: CAA23678.1.
V00380 mRNA. Translation: CAA23679.1.
V00410 Genomic DNA. Translation: CAA23701.1.
M15379 Genomic DNA. Translation: AAA48582.1. Sequence problems.
AY016020 Genomic DNA. Translation: AAL35404.1.
AF098919 Genomic DNA. Translation: AAM09073.1.
AF125311 Genomic DNA. Translation: AAD32581.1.
M35068 mRNA. Translation: AAA48583.1.
PIRiS18673. HACH2.
RefSeqiNP_001004376.1. NM_001004376.2.
UniGeneiGga.34361.

Genome annotation databases

EnsembliENSGALT00000039695; ENSGALP00000038904; ENSGALG00000007468.
GeneIDi416652.
KEGGigga:416652.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59989 Genomic DNA. Translation: CAA42606.1.
V00379 mRNA. Translation: CAA23678.1.
V00380 mRNA. Translation: CAA23679.1.
V00410 Genomic DNA. Translation: CAA23701.1.
M15379 Genomic DNA. Translation: AAA48582.1. Sequence problems.
AY016020 Genomic DNA. Translation: AAL35404.1.
AF098919 Genomic DNA. Translation: AAM09073.1.
AF125311 Genomic DNA. Translation: AAD32581.1.
M35068 mRNA. Translation: AAA48583.1.
PIRiS18673. HACH2.
RefSeqiNP_001004376.1. NM_001004376.2.
UniGeneiGga.34361.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YF1X-ray2.75C20-30[»]
3BEVX-ray2.10C20-30[»]
ProteinModelPortaliP01994.
SMRiP01994. Positions 2-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000038904.

Proteomic databases

PaxDbiP01994.
PRIDEiP01994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000039695; ENSGALP00000038904; ENSGALG00000007468.
GeneIDi416652.
KEGGigga:416652.

Organism-specific databases

CTDi416652.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01994.
KOiK13822.
OMAiDKFLCAV.
PhylomeDBiP01994.

Enzyme and pathway databases

ReactomeiR-GGA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-GGA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-GGA-2168880. Scavenging of heme from plasma.

Miscellaneous databases

EvolutionaryTraceiP01994.
PROiP01994.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Adult chicken alpha-globin gene expression in transfected QT6 quail cells: evidence for a negative regulatory element in the alpha D gene region."
    Lewis W., Lee J.D., Dodgson J.B.
    Nucleic Acids Res. 19:5321-5329(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: White leghorn.
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. "The nucleotide sequence of the adult chicken alpha-globin genes."
    Dodgson J.B., Engel J.D.
    J. Biol. Chem. 258:4623-4629(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "Adult chicken alpha-globin genes alpha A and alpha D: no anemic shock alpha-globin exists in domestic chickens."
    Dodgson J.B., McCune K.C., Rusling D.J., Krust A., Engel J.D.
    Proc. Natl. Acad. Sci. U.S.A. 78:5998-6002(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Chicken globin genes. Nucleotide sequence of cDNA clones coding for the alpha-globin expressed during hemolytic anemia."
    Richards R.I., Wells J.R.E.
    J. Biol. Chem. 255:9306-9311(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  6. "Complete nucleotide sequence of a chicken alpha-globin cDNA."
    Liu A.Y., Salser W.
    Gene 13:409-415(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  7. "Complete nucleotide sequence of a cloned chicken alpha-globin cDNA."
    Deacon N.J., Shine J., Naora H.
    Nucleic Acids Res. 8:1187-1199(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. "Comparative genome analysis delimits a chromosomal domain and identifies key regulatory elements in the alpha globin cluster."
    Flint J., Tufarelli C., Peden J., Clark K., Daniels R.J., Hardison R., Miller W., Philipsen S., Tan-Un K.C., McMorrow T., Frampton J., Alter B.P., Frischauf A.-M., Higgs D.R.
    Hum. Mol. Genet. 10:371-382(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  9. "Organization of the chicken domain of alpha-globin genes."
    Zhao Z., Sjakste N., De Moura-Gallo C.V., Ioudinkova E.S., Razin S.V., Scherrer K.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  10. "Easy access to the alpha-A-globin gene of galliform birds by EPIC-PCR."
    Fehrer J.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-111.
    Strain: White leghorn.
  11. "Identification of a new chicken alpha-globin structural gene by complementary DNA cloning."
    Cummings I.W., Liu A.Y., Salser W.A.
    Nature 276:418-419(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 61-84.
  12. "Sequence studies on the tryptic peptides and the chymotryptic peptides from the alpha polypeptide chain of aII component of the chicken hemoglobin. Biochemical studies on hemoglobins and myoglobins. 8."
    Matsuda G., Takei H., Wu K.C., Shiozawa T., Ota Y.
    Int. J. Pept. Protein Res. 4:291-302(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-142.

Entry informationi

Entry nameiHBA_CHICK
AccessioniPrimary (citable) accession number: P01994
Secondary accession number(s): Q9PWP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

This alpha chain is from the adult major tetrameric component, which has been called hemoglobin A or AII.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.