HBA_ANSIN
ID HBA_ANSIN Reviewed; 142 AA.
AC P01990;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Hemoglobin subunit alpha-A;
DE AltName: Full=Alpha-A-globin;
DE AltName: Full=Hemoglobin alpha-A chain;
GN Name=HBAA;
OS Anser indicus (Bar-headed goose) (Anas indica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anserinae; Anser.
OX NCBI_TaxID=8846;
RN [1]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=7106705;
RA Oberthur W., Braunitzer G., Wurdinger I.;
RT "Hemoglobins, XLVII. Hemoglobins of the bar-headed goose (Anser indicus):
RT primary structure and physiology of respiration, systematic and
RT evolution.";
RL Hoppe-Seyler's Z. Physiol. Chem. 363:581-590(1982).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8568892; DOI=10.1006/jmbi.1996.0040;
RA Zhang J., Hua Z., Tame J.R.H., Lu G., Zhang R., Gu X.;
RT "The crystal structure of a high oxygen affinity species of haemoglobin
RT (bar-headed goose haemoglobin in the oxy form).";
RL J. Mol. Biol. 255:484-493(1996).
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 PIR; A02311; HAGSI.
DR PDB; 1A4F; X-ray; 2.00 A; A=2-142.
DR PDB; 1C40; X-ray; 2.30 A; A=2-142.
DR PDB; 1HV4; X-ray; 2.80 A; A/C/E/G=2-142.
DR PDBsum; 1A4F; -.
DR PDBsum; 1C40; -.
DR PDBsum; 1HV4; -.
DR AlphaFoldDB; P01990; -.
DR SMR; P01990; -.
DR MINT; P01990; -.
DR EvolutionaryTrace; P01990; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-A"
FT /id="PRO_0000052552"
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:1A4F"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:1A4F"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:1A4F"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1C40"
SQ SEQUENCE 142 AA; 15468 MW; 3E1691F128B173F0 CRC64;
MVLSAADKTN VKGVFSKISG HAEEYGAETL ERMFTAYPQT KTYFPHFDLQ HGSAQIKAHG
KKVVAALVEA VNHIDDIAGA LSKLSDLHAQ KLRVDPVNFK FLGHCFLVVV AIHHPSALTA
EVHASLDKFL CAVGTVLTAK YR