ID   HBAD_ERYML              Reviewed;         141 AA.
AC   P16417;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Hemoglobin subunit alpha-D;
DE   AltName: Full=Alpha-D-globin;
DE   AltName: Full=Hemoglobin alpha-D chain;
GN   Name=HBAD;
OS   Erythrolamprus miliaris (South American water snake) (Liophis miliaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Dipsadidae; Erythrolamprus.
OX   NCBI_TaxID=8582;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2925617; DOI=10.1016/s0021-9258(18)83575-x;
RA   Matsuura M.S.A., Fushitani K., Riggs A.;
RT   "The amino acid sequences of the alpha and beta chains of hemoglobin from
RT   the snake, Liophis miliaris.";
RL   J. Biol. Chem. 264:5515-5521(1989).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: The deoxy-Hb is a heterotetramer of two alpha and two beta
CC       chains, but oxygenation results in dissociation to dimers.
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; A32854; A32854.
DR   AlphaFoldDB; P16417; -.
DR   SMR; P16417; -.
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_0000052832"
FT   BINDING         57
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;  15775 MW;  14FBA19A3A81CD40 CRC64;
     VLTAEDRRLL QASVGKLGCR LEDIGADALN RLLITFPQSK TYFSHFNLSP GSKDIIHQGE
     KVGKALDSAL KHLDDIRGTL SQLSDLHAYN LRVDPVNFQL LSKCIHVSLA THLRNEYSAS
     VTLAWDKFLE LVADVLSEKY R