HBA_GYPRU
ID HBA_GYPRU Reviewed; 141 AA.
AC P08256;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Hemoglobin subunit alpha-A/A';
DE AltName: Full=Alpha-A/A'-globin;
DE AltName: Full=Hemoglobin alpha-A/A' chain;
GN Name=HBAA;
OS Gyps rueppelli (Rueppell's griffon) (Vultur rueppellii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Gyps.
OX NCBI_TaxID=8967;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3401327; DOI=10.1515/bchm3.1988.369.1.217;
RA Hiebl I., Weber R.E., Schneeganss D., Kosters J., Braunitzer G.;
RT "High-altitude respiration of birds. Structural adaptations in the major
RT and minor hemoglobin components of adult Ruppell's Griffon (Gyps
RT rueppellii, Aegypiinae): a new molecular pattern for hypoxic tolerance.";
RL Biol. Chem. Hoppe-Seyler 369:217-232(1988).
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 -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC alpha-A. {ECO:0000269|PubMed:3401327}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; S00527; HAGRAR.
DR AlphaFoldDB; P08256; -.
DR SMR; P08256; -.
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 Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW Transport.
FT CHAIN 1..141
FT /note="Hemoglobin subunit alpha-A/A'"
FT /id="PRO_0000052647"
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 34
FT /note="T -> I (in alpha-A')"
SQ SEQUENCE 141 AA; 15483 MW; 95A91E499171D121 CRC64;
VLSANDKTNV KNVFTKITGH AEDYGAETLE RMFTTYPPTK TYFPHFDLHH GSAQIKAHGK
KVVGALIEAV NHIDDIAGAL SKLSDLHAQK LRVDPVNFKL LGQCFLVVVA IHHPSVLTPE
VHASLDKFLC AVGNVLTAKY R