ID   HBA_STRCA               Reviewed;         141 AA.
AC   P01981;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Hemoglobin subunit alpha-A;
DE   AltName: Full=Alpha-A-globin;
DE   AltName: Full=Hemoglobin alpha-A chain;
GN   Name=HBAA;
OS   Struthio camelus (Common ostrich).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC   Struthio.
OX   NCBI_TaxID=8801;
RN   [1]
RP   PROTEIN SEQUENCE (MAJOR CHAIN).
RX   PubMed=6840701;
RA   Oberthur W., Braunitzer G., Baumann R., Wright P.G.;
RT   "Primary structures of the alpha and beta chains from the major hemoglobin
RT   component of the ostrich (Struthio camelus) and American rhea (Rhea
RT   americana) (Struthioformes). Aspects of respiratory physiology and
RT   taxonomy.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 364:119-134(1983).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   PubMed=7399417;
RA   Oberthur W., Voelter W., Braunitzer G.;
RT   "The sequence of the hemoglobin of barheaded goose (Anser indicus) and
RT   ostrich (Struthio camelus). Inositol pentaphosphate as a modulator of the
RT   evolution rate: the surprising sequence alpha 63 (E12) valine.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 361:969-975(1980).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; A91712; HAOS.
DR   PDB; 3A59; X-ray; 3.41 A; A/C/E/G=1-141.
DR   PDB; 3FS4; X-ray; 2.22 A; A/C=1-141.
DR   PDBsum; 3A59; -.
DR   PDBsum; 3FS4; -.
DR   AlphaFoldDB; P01981; -.
DR   SMR; P01981; -.
DR   EvolutionaryTrace; P01981; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   CDD; cd08927; Hb-alpha-like; 1.
DR   Gene3D; 1.10.490.10; -; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR002338; Hemoglobin_a-typ.
DR   InterPro; IPR002339; Hemoglobin_pi.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   SUPFAM; SSF46458; SSF46458; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha-A"
FT                   /id="PRO_0000052769"
FT   BINDING         58
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="distal binding residue"
FT   BINDING         87
FT                   /ligand="heme b"
FT                   /ligand_id="ChEBI:CHEBI:60344"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="proximal binding residue"
FT   VARIANT         109
FT                   /note="V -> A"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:3A59"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:3A59"
FT   HELIX           53..71
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           82..87
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   TURN            88..90
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           96..112
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   TURN            114..116
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           119..136
FT                   /evidence="ECO:0007829|PDB:3FS4"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:3FS4"
SQ   SEQUENCE   141 AA;  15446 MW;  73DD27C593FF374B CRC64;
     VLSGTDKTNV KGIFSKISSH AEEYGAETLE RMFITYPQTK TYFPHFDLHH GSAQIKAHGK
     KVANALIEAV NHIDDISGAL SKLSDLHAQK LRVDPVNFKL LGQCFLVVVA IHHPSALTPE
     VHASLDKFLC AVGAVLTAKY R