ID   HBAD_CHENI              Reviewed;         141 AA.
AC   P83124; Q5CD79;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Hemoglobin subunit alpha-D;
DE   AltName: Full=Alpha-D-globin;
DE   AltName: Full=Hemoglobin alpha-D chain;
GN   Name=HBAD;
OS   Chelonoidis niger (Galapagos giant tortoise) (Geochelone nigra).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Testudinidae; Chelonoidis.
OX   NCBI_TaxID=66189;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE.
RC   TISSUE=Erythrocyte;
RX   PubMed=12012783; DOI=10.2108/zsj.19.197;
RA   Shishikura F.;
RT   "The primary structure of hemoglobin D from the Aldabra giant tortoise,
RT   Geochelone gigantea.";
RL   Zool. Sci. 19:197-206(2002).
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 reptiles, 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   EMBL; AB116521; BAC81726.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83124; -.
DR   SMR; P83124; -.
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_0000052830"
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"
FT   CONFLICT        16
FT                   /note="T -> K (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="T -> I (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="G -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="R -> K (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75
FT                   /note="D -> N (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   141 AA;  16097 MW;  C65CA53BC7060920 CRC64;
     MLTEDDKQLI QHVWETVLEH QEDFGAEALE RMFTVYPSTK TYFPHFDLHH GSEQIRHHGK
     KVVGALGDAV RHIDDLSATL SELSNLHAYN LRVDPVNFKL LSHCFQVVLG AHLGREYTPQ
     VQVAYDKFLA AVSAVLAEKY R