ID   HBAD_ALDGI              Reviewed;         141 AA.
AC   P83134; Q90Y76;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Hemoglobin D subunit alpha;
DE   AltName: Full=Hemoglobin D alpha chain;
OS   Aldabrachelys gigantea (Aldabra giant tortoise) (Geochelone gigantea).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Aldabrachelys.
OX   NCBI_TaxID=167804 {ECO:0000305};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Shishikura F.;
RT   "Alpha D-globin gene of hemoglobin D from the Aldabra giant tortoises,
RT   Geochelone gigantea.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-20.
RC   TISSUE=Erythrocyte;
RA   Shishikura F., Takami K.;
RT   "The amino acid sequences of the alpha- and beta-globin chains of
RT   hemoglobin from the Aldabra giant tortoises, Geochelone gigantea.";
RL   Zool. Sci. 18:515-526(2001).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues. {ECO:0000250|UniProtKB:P07417}.
CC   -!- SUBUNIT: Tetramer of two alpha chains and two beta chains.
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Hemoglobin A is the major, and hemoglobin D the minor
CC       hemoglobin of this species. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB072353; BAB68554.1; -; Genomic_DNA.
DR   PDB; 1V75; X-ray; 2.02 A; A=1-141.
DR   PDB; 1WMU; X-ray; 1.65 A; A=1-141.
DR   PDB; 2Z6N; X-ray; 1.86 A; A=1-141.
DR   PDBsum; 1V75; -.
DR   PDBsum; 1WMU; -.
DR   PDBsum; 2Z6N; -.
DR   AlphaFoldDB; P83134; -.
DR   SMR; P83134; -.
DR   EvolutionaryTrace; P83134; -.
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   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin D subunit alpha"
FT                   /id="PRO_0000052541"
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"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           37..42
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           53..71
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           76..79
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           81..89
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           95..113
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           114..116
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           119..136
FT                   /evidence="ECO:0007829|PDB:1WMU"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:1WMU"
SQ   SEQUENCE   141 AA;  16165 MW;  2931C3E22597D9D3 CRC64;
     MLTEDDKQLI QHVWEKVLEH QEDFGAEALE RMFIVYPSTK TYFPHFDLHH DSEQIRHHGK
     KVVGALGDAV KHIDNLSATL SELSNLHAYN LRVDPVNFKL LSHCFQVVLG AHLGREYTPQ
     VQVAYDKFLA AVSAVLAEKY R