ID HBA_TREBE Reviewed; 142 AA. AC P80043; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 27-MAR-2024, entry version 121. DE RecName: Full=Hemoglobin subunit alpha; DE AltName: Full=Alpha-globin; DE AltName: Full=Hemoglobin alpha chain; GN Name=hba; OS Trematomus bernacchii (Emerald rockcod) (Pseudotrematomus bernacchii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus. OX NCBI_TaxID=40690; RN [1] RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY (2.5 RP ANGSTROMS). RC TISSUE=Blood; RX PubMed=1560461; DOI=10.1016/0022-2836(92)91007-c; RA Camardella L., Caruso C., D'Avino R., di Prisco G., Rutigliano B., RA Tamburrini M., Fermi G., Perutz M.F.; RT "Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid RT sequence, oxygen equilibria and crystal structure of its carbonmonoxy RT derivative."; RL J. Mol. Biol. 224:449-460(1992). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND ACETYLATION AT SER-1. RX PubMed=7623382; DOI=10.1006/jmbi.1995.0405; RA Ito N., Komiyama N.H., Fermi G.; RT "Structure of deoxyhaemoglobin of the antarctic fish Pagothenia bernacchii RT with an analysis of the structural basis of the Root effect by comparison RT of the liganded and unliganded haemoglobin structures."; RL J. Mol. Biol. 250:648-658(1995). CC -!- FUNCTION: Involved in oxygen transport from gills to the various CC peripheral tissues. {ECO:0000269|PubMed:1560461}. CC -!- SUBUNIT: Hb1 is a heterotetramer of two alpha chains and two beta CC chains. HbC is a heterotetramer of two alpha chains and two beta-C CC chains. {ECO:0000269|PubMed:1560461}. CC -!- TISSUE SPECIFICITY: Red blood cells. CC -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1 (major) and two CC minor hemoglobins (about 1-2% of the total). Hb1 has a strong alkaline CC Bohr effect, and at low pH exhibits the reduced ligand affinity and CC cooperativity that comprise the Root effect. 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; S21677; S21677. DR PDB; 1HBH; X-ray; 2.20 A; A/C=1-142. DR PDB; 1PBX; X-ray; 2.50 A; A=1-142. DR PDB; 1S5X; X-ray; 2.40 A; A=1-142. DR PDB; 1S5Y; X-ray; 2.50 A; A/C=1-142. DR PDB; 2H8D; X-ray; 1.78 A; A/C=1-142. DR PDB; 2H8F; X-ray; 1.30 A; A/C=1-142. DR PDB; 2PEG; X-ray; 1.48 A; A=1-142. DR PDB; 3GKV; X-ray; 1.40 A; A=1-142. DR PDB; 3GQG; X-ray; 1.73 A; A/C=1-142. DR PDB; 4G51; X-ray; 2.50 A; A/C=1-142. DR PDB; 4IRO; X-ray; 2.20 A; A/C=1-142. DR PDB; 4ODC; X-ray; 1.54 A; A=1-142. DR PDBsum; 1HBH; -. DR PDBsum; 1PBX; -. DR PDBsum; 1S5X; -. DR PDBsum; 1S5Y; -. DR PDBsum; 2H8D; -. DR PDBsum; 2H8F; -. DR PDBsum; 2PEG; -. DR PDBsum; 3GKV; -. DR PDBsum; 3GQG; -. DR PDBsum; 4G51; -. DR PDBsum; 4IRO; -. DR PDBsum; 4ODC; -. DR AlphaFoldDB; P80043; -. DR SMR; P80043; -. DR MINT; P80043; -. DR iPTMnet; P80043; -. DR EvolutionaryTrace; P80043; -. DR GO; GO:0005833; C:hemoglobin complex; ISS:UniProtKB. 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; ISS:UniProtKB. DR GO; GO:0015671; P:oxygen transport; ISS:UniProtKB. DR CDD; cd08927; Hb-alpha-like; 1. DR Gene3D; 1.10.490.10; Globins; 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 PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF48; HEMOGLOBIN SUBUNIT ALPHA; 1. 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 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron; KW Metal-binding; Oxygen transport; Transport. FT CHAIN 1..142 FT /note="Hemoglobin subunit alpha" FT /id="PRO_0000052712" FT BINDING 59 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00238" FT BINDING 88 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 MOD_RES 1 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:7623382" FT HELIX 4..17 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 18..20 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 21..35 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 37..43 FT /evidence="ECO:0007829|PDB:2H8F" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:1PBX" FT HELIX 54..72 FT /evidence="ECO:0007829|PDB:2H8F" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 77..80 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 82..90 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 97..113 FT /evidence="ECO:0007829|PDB:2H8F" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:2H8F" FT HELIX 120..137 FT /evidence="ECO:0007829|PDB:2H8F" FT TURN 138..140 FT /evidence="ECO:0007829|PDB:2H8F" SQ SEQUENCE 142 AA; 15632 MW; 24C8759C565202A4 CRC64; SLSDKDKAAV RALWSKIGKS ADAIGNDALS RMIVVYPQTK TYFSHWPDVT PGSPHIKAHG KKVMGGIALA VSKIDDLKTG LMELSEQHAY KLRVDPANFK ILNHCILVVI STMFPKEFTP EAHVSLDKFL SGVALALAER YR //