ID   HBAD_PHACA              Reviewed;         141 AA.
AC   P10781;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Hemoglobin subunit alpha-D;
DE   AltName: Full=Alpha-D-globin;
DE   AltName: Full=Hemoglobin alpha-D chain;
GN   Name=HBAD;
OS   Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Pelecaniformes; Phalacrocoracidae;
OC   Phalacrocorax.
OX   NCBI_TaxID=9209;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3245897; DOI=10.1515/bchm3.1988.369.2.1251;
RA   Huber K., Braunitzer G., Schneeganss D., Kosters J., Grimm F.;
RT   "The primary structure of the hemoglobin of the Cormorant (Phalacrocorax
RT   carbo, Pelecaniformes).";
RL   Biol. Chem. Hoppe-Seyler 369:1251-1258(1988).
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}.
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DR   PIR; S01806; HACODG.
DR   AlphaFoldDB; P10781; -.
DR   SMR; P10781; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
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-D"
FT                   /id="PRO_0000052835"
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;  15979 MW;  5D0C08FAB4B42035 CRC64;
     MLGAEETALV RGVWQKVESA KDEMGEETLT RMFLVYPKTK TYFPHFDLHH GSEQIRNHGK
     KVVTALGNAI QNLDNLRQTL ADLSNLHAYN LRVDPVNFKL LAQCFQVVLA VHLGQEYTPE
     VHVAFDKFLT AVAAVLAEKY R