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 14-DEC-2022, entry version 90. 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}. 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 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; Globin-like; 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 //