ID   HBA_SPHPU               Reviewed;         141 AA.
AC   P10059;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Hemoglobin subunit alpha-A;
DE   AltName: Full=Alpha-A-globin;
DE   AltName: Full=Hemoglobin alpha-A chain;
GN   Name=HBAA;
OS   Sphenodon punctatus (Tuatara) (Hatteria punctata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Sphenodontia; Sphenodontidae; Sphenodon.
OX   NCBI_TaxID=8508;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3214555; DOI=10.1515/bchm3.1988.369.2.755;
RA   Abbasi A., Wells R.M.G., Brittain T., Braunitzer G.;
RT   "Primary structure of the hemoglobins from Sphenodon (Sphenodon punctatus,
RT   Tuatara, Rynchocephalia). Evidence for the expression of alpha D-gene.";
RL   Biol. Chem. Hoppe-Seyler 369:755-764(1988).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: There are three forms of hemoglobin in Sphenodon: A, A' and D.
CC       Hb A is a tetramer of two alpha-A and two beta-1, Hb A' is a tetramer
CC       of two alpha-a and two beta-2, Hb D is a tetramer of two alpha-D and
CC       two beta-2.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: Sphenodon Hbs have properties not found in other
CC       reptiles: poor cooperativity, high affinity for oxygen, small Bohr and
CC       haldane effects, appreciable phosphate effects (those properties are
CC       also found in the Hbs of primitive urodele and caecilian amphibians).
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S01136; HATJA.
DR   AlphaFoldDB; P10059; -.
DR   SMR; P10059; -.
DR   Proteomes; UP000694392; Unplaced.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   InterPro; IPR002339; Hemoglobin_pi.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
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   Reference proteome; Transport.
FT   CHAIN           1..141
FT                   /note="Hemoglobin subunit alpha-A"
FT                   /id="PRO_0000052767"
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;  15454 MW;  F72D8BDD2D25C501 CRC64;
     MLSASDKANV KAIWSKVCVH AEEYGAETLE RMFTVYPSTK TYFPHFDLTH GSAQVKAHGK
     KVVNAMGEAV NHLDDMAGAL LKLSDLHAQK LRVDPVNFKL LAQCFLVVLG VHHPAALTPE
     VHASLDKFLC AVGLVLTAKY R