HBA_COTJA
ID HBA_COTJA Reviewed; 142 AA.
AC P24589;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Hemoglobin subunit alpha-A;
DE AltName: Full=Alpha-A-globin;
DE AltName: Full=Hemoglobin alpha-A chain;
GN Name=HBAA;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1859627; DOI=10.1515/bchm3.1991.372.1.113;
RA Eguchi Y., Takei H., Oshiro M., Toda T., Nakashima Y.;
RT "Protein structure and cDNA nucleotide sequence of the Japanese quail alpha
RT A globin.";
RL Biol. Chem. Hoppe-Seyler 372:113-118(1991).
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 -!- MISCELLANEOUS: This alpha-A chain is from the major component, which
CC has been called the Q-II component.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; X57680; CAA40868.1; -; mRNA.
DR PIR; S13452; S13452.
DR PDB; 3MJP; X-ray; 2.76 A; A/C=2-142.
DR PDBsum; 3MJP; -.
DR AlphaFoldDB; P24589; -.
DR SMR; P24589; -.
DR Proteomes; UP000694412; Unplaced.
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; Heme; Iron; Metal-binding; Oxygen transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-A"
FT /id="PRO_0000052607"
FT BINDING 59
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 88
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 HELIX 5..18
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 22..33
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 40..43
FT /evidence="ECO:0007829|PDB:3MJP"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 54..65
FT /evidence="ECO:0007829|PDB:3MJP"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3MJP"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:3MJP"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:3MJP"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:3MJP"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:3MJP"
SQ SEQUENCE 142 AA; 15308 MW; 1EF17357B09239C9 CRC64;
MVLSAADKTN VKGIFAKIAG HAEEYGAEAL DRMFTTYPQT KTYFPHFDVS HGSAQIKGHG
KKVAAALVEA ANHIDDIAGT LSKLSDLHAQ KLRVDPVNFK LLGQCFLVVV AIHHPAALTP
EVHASLDKFL CAVGTVLTAK YR
