HBA_TREBE
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 03-AUG-2022, entry version 116.
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}.
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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; -; 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 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="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 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 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
