HBA4_ONCMY
ID HBA4_ONCMY Reviewed; 142 AA.
AC P14527;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Hemoglobin subunit alpha-4;
DE AltName: Full=Alpha-4-globin;
DE AltName: Full=Hemoglobin alpha-4 chain;
GN Name=hba4;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX PubMed=2706274; DOI=10.1016/0167-4838(89)90043-5;
RA Petruzzelli R., Barra D., Sensi L., Bossa F., Brunori M.;
RT "Amino acid sequence of alpha-chain of hemoglobin IV from trout (Salmo
RT irideus).";
RL Biochim. Biophys. Acta 995:255-258(1989).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; S03995; S03995.
DR PDB; 2R1H; X-ray; 1.90 A; A/C=1-142.
DR PDB; 3BOM; X-ray; 1.35 A; A/C=1-142.
DR PDBsum; 2R1H; -.
DR PDBsum; 3BOM; -.
DR AlphaFoldDB; P14527; -.
DR SMR; P14527; -.
DR iPTMnet; P14527; -.
DR EvolutionaryTrace; P14527; -.
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 3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Transport.
FT CHAIN 1..142
FT /note="Hemoglobin subunit alpha-4"
FT /id="PRO_0000052759"
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:2706274"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 37..42
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:3BOM"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 98..113
FT /evidence="ECO:0007829|PDB:3BOM"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3BOM"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:3BOM"
SQ SEQUENCE 142 AA; 15803 MW; F23E3258D250F66C CRC64;
SLSAKDKANV KAIWGKILPK SDEIGEQALS RMLVVYPQTK AYFSHWASVA PGSAPVKKHG
ITIMNQIDDC VGHMDDLFGF LTKLSELHAT KLRVDPTNFK ILAHNLIVVI AAYFPAEFTP
EIHLSVDKFL QQLALALAEK YR
