ID   HBAD_CAIMO              Reviewed;         141 AA.
AC   P02003;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Hemoglobin subunit alpha-D;
DE   AltName: Full=Alpha-D-globin;
DE   AltName: Full=Hemoglobin alpha-D chain;
GN   Name=HBAD;
OS   Cairina moschata (Muscovy duck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Cairina.
OX   NCBI_TaxID=8855;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10872328; DOI=10.1002/j.1460-2075.1983.tb01589.x;
RA   Erbil C., Niessing J.;
RT   "The primary structure of the duck alpha(D)-globin gene: an unusual 5'
RT   splice junction sequence.";
RL   EMBO J. 2:1339-1343(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30.
RX   PubMed=6290322; DOI=10.1016/0378-1119(82)90116-0;
RA   Niessing J., Erbil C., Neubauer V.;
RT   "The isolation and partial characterization of linked alpha A- and alpha D-
RT   globin genes from a duck DNA recombinant library.";
RL   Gene 18:187-191(1982).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha-D chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
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.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
CC   -!- CAUTION: The authors believe the gene from which the sequence was
CC       translated to be functional although the second intron begins with 'GC'
CC       rather than the usual 'GT'. {ECO:0000305}.
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DR   EMBL; X01831; CAA25966.2; -; Genomic_DNA.
DR   EMBL; J00925; AAA49147.1; -; Genomic_DNA.
DR   PIR; A02325; HADKMD.
DR   AlphaFoldDB; P02003; -.
DR   SMR; P02003; -.
DR   PRIDE; P02003; -.
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; 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   2: Evidence at transcript level;
KW   Heme; Iron; Metal-binding; Oxygen transport; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha-D"
FT                   /id="PRO_0000052821"
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;  15712 MW;  74BBB8950355B30B CRC64;
     MLTAEDKKLI VQVWEKVAGH QEEFGSEALQ RMFLAYPQTK TYFPHFDLHP GSEQVRGHGK
     KVAAALGNAV KSLDNLSQAL SELSNLHAYN LRVDPVNFKL LAQCFQVVLA AHLGKDYSPE
     MHAAFDKFLS AVAAVLAEKY R