P02001 · HBAD_CHICK

  • Protein
    Hemoglobin subunit alpha-D
  • Gene
    HBAD
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

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

Miscellaneous

Ref.6 chain was isolated from Hbm, the least abundant of the four early chick hemoglobins.

Features

Showing features for binding site.

1141102030405060708090100110120130140
TypeIDPosition(s)Description
Binding site58Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); distal binding residue
Binding site87Fe (UniProtKB | ChEBI) of heme b (UniProtKB | ChEBI); proximal binding residue

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componenthaptoglobin-hemoglobin complex
Cellular Componenthemoglobin complex
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionorganic acid binding
Molecular Functionoxygen binding
Molecular Functionoxygen carrier activity
Biological Processcellular oxidant detoxification
Biological Processhydrogen peroxide catabolic process

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Hemoglobin subunit alpha-D
  • Alternative names
    • Alpha-D-globin
    • Hemoglobin alpha-D chain

Gene names

    • Name
      HBAD

Organism names

  • Taxonomic identifier
  • Strain
    • White leghorn
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Galloanserae > Galliformes > Phasianidae > Phasianinae > Gallus

Accessions

  • Primary accession
    P02001
  • Secondary accessions
    • Q549K7
    • Q78AJ9

Proteomes

Organism-specific databases

Phenotypes & Variants

Protein family/group databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000528221-141Hemoglobin subunit alpha-D

Proteomic databases

Expression

Tissue specificity

Red blood cells.

Developmental stage

In birds, the alpha-D chain occurs in a minor hemoglobin component, called hemoglobin d, which is expressed in late embryonic and adult life.

Gene expression databases

Interaction

Subunit

Heterotetramer of two alpha-D chains and two beta chains. The component D forms dimers of tetramers upon deoxygenation.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-141Globin

Sequence similarities

Belongs to the globin family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    141
  • Mass (Da)
    15,695
  • Last updated
    1986-07-21 v1
  • Checksum
    1FE426969B7B5384
MLTAEDKKLIQQAWEKAASHQEEFGAEALTRMFTTYPQTKTYFPHFDLSPGSDQVRGHGKKVLGALGNAVKNVDNLSQAMAELSNLHAYNLRVDPVNFKLLSQCIQVVLAVHMGKDYTPEVHAAFDKFLSAVSAVLAEKYR

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict16in Ref. 4 and 6
Sequence conflict33in Ref. 2; AAA48584
Sequence conflict107in Ref. 2 and 7
Sequence conflict109-110in Ref. 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M15378
EMBL· GenBank· DDBJ
AAA48584.1
EMBL· GenBank· DDBJ
Genomic DNA
V00411
EMBL· GenBank· DDBJ
CAA23702.1
EMBL· GenBank· DDBJ
Genomic DNA
X59989
EMBL· GenBank· DDBJ
CAA42605.1
EMBL· GenBank· DDBJ
Genomic DNA
AY016020
EMBL· GenBank· DDBJ
AAL35403.1
EMBL· GenBank· DDBJ
Genomic DNA
AF098919
EMBL· GenBank· DDBJ
AAM09072.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp