HBA_LEIXA
ID HBA_LEIXA Reviewed; 143 AA.
AC P56250;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
GN Name=hba;
OS Leiostomus xanthurus (Spot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Sciaenidae; Leiostomus.
OX NCBI_TaxID=59837;
RN [1]
RP PROTEIN SEQUENCE, ACETYLATION AT SER-1, AND X-RAY CRYSTALLOGRAPHY (1.95
RP ANGSTROMS).
RX PubMed=8605630; DOI=10.1038/nsb0396-275;
RA Mylvaganam S.E., Bonaventura C., Bonaventura J., Getzoff E.D.;
RT "Structural basis for the root effect in haemoglobin.";
RL Nat. Struct. Biol. 3:275-283(1996).
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}.
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 PDB; 1SPG; X-ray; 1.95 A; A=1-143.
DR PDBsum; 1SPG; -.
DR AlphaFoldDB; P56250; -.
DR SMR; P56250; -.
DR MINT; P56250; -.
DR iPTMnet; P56250; -.
DR EvolutionaryTrace; P56250; -.
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..143
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052664"
FT BINDING 60
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 89
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:8605630"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 55..73
FT /evidence="ECO:0007829|PDB:1SPG"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 98..114
FT /evidence="ECO:0007829|PDB:1SPG"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:1SPG"
FT HELIX 121..138
FT /evidence="ECO:0007829|PDB:1SPG"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1SPG"
SQ SEQUENCE 143 AA; 15638 MW; 88570E5822D0D769 CRC64;
SLSATDKARV KALWDKIEGK SAELGAEALG RMLVSFPQTK IYFSEWGQDL GPQTPQVRNH
GAVIMAAVGK AVKSIDNLVG GLSQLSELHA FKLRVDPANF KILAHNIILV ISMYFPGDFT
PEVHLSVDKF LACLALALSE KYR
