P67816 · HBA_VICPA
- ProteinHemoglobin subunit alpha
- GeneHBA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids141 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in oxygen transport from the lung to the various peripheral tissues.
Hemopressin
Hemopressin acts as an antagonist peptide of the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks cannabinoid receptor CNR1 and subsequent signaling.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | blood microparticle | |
Cellular Component | haptoglobin-hemoglobin complex | |
Cellular Component | hemoglobin complex | |
Molecular Function | haptoglobin binding | |
Molecular Function | heme binding | |
Molecular Function | iron ion binding | |
Molecular Function | organic acid binding | |
Molecular Function | oxygen binding | |
Molecular Function | oxygen carrier activity | |
Molecular Function | peroxidase activity | |
Biological Process | hydrogen peroxide catabolic process |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameHemoglobin subunit alpha
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Tylopoda > Camelidae > Vicugna
Accessions
- Primary accessionP67816
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain, modified residue, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000052659 | 1-141 | Hemoglobin subunit alpha | |||
Sequence: VLSSKDKANIKTAFGKIGGHAADYGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTKAADHLDDLPSALSALSDLHAHKLRVDPVNFKLLSHCLLVTVAAHHPGDFTPAVHASLDKFLANVSTVLTSKYR | ||||||
Modified residue | 3 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 7 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 11 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 16 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 16 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 24 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 40 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 49 | Phosphoserine | ||||
Sequence: S | ||||||
Peptide | PRO_0000455887 | 95-103 | Hemopressin | |||
Sequence: PVNFKLLSH | ||||||
Modified residue | 102 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 108 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 124 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 134 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 137 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 138 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Expression
Tissue specificity
Red blood cells.
Interaction
Subunit
Heterotetramer of two alpha chains and two beta chains.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-141 | Globin | ||||
Sequence: VLSSKDKANIKTAFGKIGGHAADYGAEALERMFLGFPTTKTYFPHFDLSHGSAQVKAHGKKVGDALTKAADHLDDLPSALSALSDLHAHKLRVDPVNFKLLSHCLLVTVAAHHPGDFTPAVHASLDKFLANVSTVLTSKYR |
Sequence similarities
Belongs to the globin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length141
- Mass (Da)15,126
- Last updated1988-04-01 v1
- Checksum7E8513D558678E67
Keywords
- Technical term