P01959 (HBA_EQUAS) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 86.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Hemoglobin subunit alpha Alternative name(s): Alpha-globin Hemoglobin alpha chain | |||||
| Gene names |
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| Organism | Equus asinus (Donkey) | |||||
| Taxonomic identifier | 9793 [NCBI] | |||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus › ![]() |
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. |
| Sequence similarities | Belongs to the globin family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Oxygen transport Transport |
| Ligand | Heme Iron Metal-binding |
| PTM | Acetylation |
| Technical term | 3D-structure Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular_component | hemoglobin complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | heme binding Inferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro oxygen bindingInferred from electronic annotation. Source: InterPro oxygen transporter activityInferred 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 | 1 | 1 | Removed Ref.2 | |||||||||||||||||||||||||||
| Chain | 2 – 142 | 141 | Hemoglobin subunit alpha | PRO_0000052624 | ||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||
| Metal binding | 59 | 1 | Iron (heme distal ligand) | |||||||||||||||||||||||||||
| Metal binding | 88 | 1 | Iron (heme proximal ligand) | |||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||
| Modified residue | 17 | 1 | N6-acetyllysine By similarity | |||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||
| Sequence conflict | 132 | 1 | T → S AA sequence Ref.2 | |||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Helix | 5 – 18 | 14 | ||||||||||||||||||||||||||||
| Helix | 19 – 21 | 3 | ||||||||||||||||||||||||||||
| Helix | 22 – 36 | 15 | ||||||||||||||||||||||||||||
| Helix | 38 – 43 | 6 | ||||||||||||||||||||||||||||
| Helix | 54 – 72 | 19 | ||||||||||||||||||||||||||||
| Helix | 74 – 76 | 3 | ||||||||||||||||||||||||||||
| Helix | 77 – 80 | 4 | ||||||||||||||||||||||||||||
| Helix | 82 – 88 | 7 | ||||||||||||||||||||||||||||
| Turn | 89 – 92 | 4 | ||||||||||||||||||||||||||||
| Helix | 97 – 113 | 17 | ||||||||||||||||||||||||||||
| Turn | 115 – 117 | 3 | ||||||||||||||||||||||||||||
| Helix | 120 – 136 | 17 | ||||||||||||||||||||||||||||
| Turn | 137 – 141 | 5 | ||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Phylogenetic relationships within the genus Equus and the evolution of alpha and theta globin genes." Oakenfull E.A., Clegg J.B. J. Mol. Evol. 47:772-783(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1 AND HBA2). |
| [2] | "Amino-acid replacements in horse haemoglobin." Kilmartin J.V., Clegg J.B. Nature 213:269-271(1967) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-142. |
| [3] | "Crystal structure of haemoglobin from donkey (Equus asinus) at 3A resolution." Balasundaresan D., Saraboji K., Ponnuswamy M.N. Biochimie 88:719-723(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | U69894 Genomic DNA. Translation: AAD13640.1. U69895 Genomic DNA. Translation: AAD13641.1. | ||||||||||||
| PIR | HAHOD. A02282. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P01959. | ||||||||||||
| SMR | P01959. Positions 2-142. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOVERGEN | HBG009709. | ||||||||||||
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 | P01959. | ||||||||||||
Entry information
| Entry name | HBA_EQUAS | ||||||||
| Accession | Primary (citable) accession number: P01959 Secondary accession number(s): P82988 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
