ID   HBAD_DRYME              Reviewed;         141 AA.
AC   P0C0U7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Hemoglobin subunit alpha-D;
DE   AltName: Full=Alpha-D-globin;
DE   AltName: Full=Hemoglobin alpha-D chain;
OS   Drymarchon melanurus erebennus (Texas indigo snake) (Drymarchon corais
OS   erebennus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Colubridae; Colubrinae; Drymarchon.
OX   NCBI_TaxID=358746;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=12553727; DOI=10.1515/bc.2002.214;
RA   Stoeckelhuber M., Gorr T., Kleinschmidt T.;
RT   "The primary structure of three hemoglobin chains from the indigo snake
RT   (Drymarchon corais erebennus, Serpentes): first evidence for alphaD chains
RT   and two beta chain types in snakes.";
RL   Biol. Chem. 383:1907-1916(2002).
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   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P0C0U7; -.
DR   SMR; P0C0U7; -.
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_0000052827"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   141 AA;  15821 MW;  EAE147E4BAD4ADB1 CRC64;
     VLTAEDRRLL QASVGKLGCR LEDIGADALN RLLIVFPQSK TYFSHFNLSP GSKDIVHQGE
     KVGKALDSAL KHLDDIRGTL SQLSDLHAYN LRVDPVNFQL LSKCLHVSLA THLRNEYNAS
     TCLAWDKFLE QVADVLCEKY R