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Protein

Hemoglobin subunit alpha-A

Gene

HBAA

Organism
Struthio camelus (Common ostrich)
Status
Reviewed-Annotation score: Annotation score: 3 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 bindingi58 – 581Iron (heme distal ligand)
Metal bindingi87 – 871Iron (heme proximal ligand)

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit alpha-A
Alternative name(s):
Alpha-A-globin
Hemoglobin alpha-A chain
Gene namesi
Name:HBAA
OrganismiStruthio camelus (Common ostrich)
Taxonomic identifieri8801 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeStruthioniformesStruthionidaeStruthio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 141141Hemoglobin subunit alpha-APRO_0000052769Add
BLAST

Proteomic databases

PRIDEiP01981.

Expressioni

Tissue specificityi

Red blood cells.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Structurei

Secondary structure

1
141
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1714Combined sources
Helixi21 – 3515Combined sources
Helixi37 – 426Combined sources
Beta strandi44 – 463Combined sources
Beta strandi49 – 513Combined sources
Helixi53 – 7119Combined sources
Turni72 – 743Combined sources
Helixi76 – 805Combined sources
Helixi82 – 876Combined sources
Turni88 – 903Combined sources
Helixi96 – 11217Combined sources
Turni114 – 1163Combined sources
Helixi119 – 13618Combined sources
Helixi138 – 1403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A59X-ray3.41A/C/E/G1-141[»]
3FS4X-ray2.22A/C1-141[»]
ProteinModelPortaliP01981.
SMRiP01981. Positions 1-141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01981.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG009709.

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.

P01981-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
VLSGTDKTNV KGIFSKISSH AEEYGAETLE RMFITYPQTK TYFPHFDLHH
60 70 80 90 100
GSAQIKAHGK KVANALIEAV NHIDDISGAL SKLSDLHAQK LRVDPVNFKL
110 120 130 140
LGQCFLVVVA IHHPSALTPE VHASLDKFLC AVGAVLTAKY R
Length:141
Mass (Da):15,446
Last modified:July 21, 1986 - v1
Checksum:i73DD27C593FF374B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091V → A.

Sequence databases

PIRiA91712. HAOS.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

PIRiA91712. HAOS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A59X-ray3.41A/C/E/G1-141[»]
3FS4X-ray2.22A/C1-141[»]
ProteinModelPortaliP01981.
SMRiP01981. Positions 1-141.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP01981.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG009709.

Miscellaneous databases

EvolutionaryTraceiP01981.

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. "Primary structures of the alpha and beta chains from the major hemoglobin component of the ostrich (Struthio camelus) and American rhea (Rhea americana) (Struthioformes). Aspects of respiratory physiology and taxonomy."
    Oberthur W., Braunitzer G., Baumann R., Wright P.G.
    Hoppe-Seyler's Z. Physiol. Chem. 364:119-134(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (MAJOR CHAIN).
  2. "The sequence of the hemoglobin of barheaded goose (Anser indicus) and ostrich (Struthio camelus). Inositol pentaphosphate as a modulator of the evolution rate: the surprising sequence alpha 63 (E12) valine."
    Oberthur W., Voelter W., Braunitzer G.
    Hoppe-Seyler's Z. Physiol. Chem. 361:969-975(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiHBA_STRCA
AccessioniPrimary (citable) accession number: P01981
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 14, 2015
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.