ID   HBAD_AYTFU              Reviewed;         141 AA.
AC   P84791;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Hemoglobin subunit alpha-D;
DE   AltName: Full=Alpha-D-globin;
DE   AltName: Full=Hemoglobin alpha-D chain;
GN   Name=HBAD;
OS   Aythya fuligula (Tufted duck) (Anas fuligula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Aythyinae; Aythya.
OX   NCBI_TaxID=219594;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:15567161};
RX   PubMed=15567161; DOI=10.1016/j.bbrc.2004.10.209;
RA   Lutfullah G., Ali S.A., Abbasi A.;
RT   "Molecular mechanism of high altitude respiration: primary structure of a
RT   minor hemoglobin component from Tufted duck (Aythya fuligula,
RT   Anseriformes).";
RL   Biochem. Biophys. Res. Commun. 326:123-130(2005).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues. {ECO:0000305}.
CC   -!- SUBUNIT: Heterotetramer of two alpha-D chains and two beta chains.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: In birds, the alpha-D chain occurs in a minor
CC       hemoglobin component, called hemoglobin d, which is expressed in late
CC       embryonic and adult life. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=15745; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15567161};
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P84791; -.
DR   SMR; P84791; -.
DR   Proteomes; UP000504639; Genome assembly.
DR   GO; GO:0005833; C:hemoglobin complex; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
DR   GO; GO:0015671; P:oxygen transport; IDA:UniProtKB.
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; IPR002340; Hemoglobin_zeta.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00816; ZETAHAEM.
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   Reference proteome; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha-D"
FT                   /id="PRO_0000227532"
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"
SQ   SEQUENCE   141 AA;  15743 MW;  2942668AB5D08771 CRC64;
     MLTAEDKKLI TQLWEKVAGH QDDFGNEALQ RMFVTYPQTK TYFPHFDLHP GSEQVRGHGK
     KVAAALGNAV KSLDNISQAL SELSNLHAYN LRVDPVNFKL LAQCFQVVLA AHLGKDYTPD
     MHAAFDKFLS AVAAVLAEKY R