HBA_ANAPL
ID HBA_ANAPL Reviewed; 142 AA.
AC P01986;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hemoglobin subunit alpha-A;
DE AltName: Full=Alpha-A-globin;
DE AltName: Full=Hemoglobin alpha-A chain;
GN Name=HBAA;
OS Anas platyrhynchos (Mallard) (Anas boschas).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6895064; DOI=10.1111/j.1432-1033.1981.tb06333.x;
RA Paddock G.V., Gaubatz J.;
RT "Nucleotide sequence for a novel duck alpha-globin gene.";
RL Eur. J. Biochem. 117:269-273(1981).
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}.
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DR EMBL; X02008; CAA26039.1; -; mRNA.
DR PIR; A02309; HADK.
DR PDB; 3EOK; X-ray; 2.10 A; A=2-142.
DR PDBsum; 3EOK; -.
DR AlphaFoldDB; P01986; -.
DR SMR; P01986; -.
DR EvolutionaryTrace; P01986; -.
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; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-A"
FT /id="PRO_0000052547"
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:3EOK"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:3EOK"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3EOK"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:3EOK"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:3EOK"
SQ SEQUENCE 142 AA; 15365 MW; EA21F1750AE26503 CRC64;
MVLSAADKTN VKGVFSKIGG HAEEYGAETL ERMFIAYPQT KTYFPHFDLS HGSAQIKAHG
KKVAAALVEA VNHVDDIAGA LSKLSDLHAQ KLRVDPVNFK FLGHCFLVVV AIHHPAALTP
EVHASLDKFM CAVGAVLTAK YR
