ID   HBA1_ONCMY              Reviewed;         144 AA.
AC   P02019;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Hemoglobin subunit alpha-1;
DE   AltName: Full=Alpha-1-globin;
DE   AltName: Full=Hemoglobin alpha-1 chain;
GN   Name=hba1;
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=708770; DOI=10.1016/0005-2795(78)90077-6;
RA   Bossa F., Barra D., Petruzzelli R., Martini F., Brunori M.;
RT   "Primary structure of hemoglobin from trout (Salmo irideus). Amino acid
RT   sequence of alpha chain of Hb trout I.";
RL   Biochim. Biophys. Acta 536:298-305(1978).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=8683580; DOI=10.1006/jmbi.1996.0355;
RA   Tame J.R.H., Wilson J.C., Weber R.E.;
RT   "The crystal structures of trout Hb I in the deoxy and carbonmonoxy
RT   forms.";
RL   J. Mol. Biol. 259:749-760(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   -!- MISCELLANEOUS: This hemoglobin has two more residues, 32-Asp-Lys-33,
CC       than other fish hemoglobins.
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; A02348; HATR1.
DR   PDB; 1OUT; X-ray; 2.30 A; A=1-143.
DR   PDB; 1OUU; X-ray; 2.50 A; A/C=1-143.
DR   PDBsum; 1OUT; -.
DR   PDBsum; 1OUU; -.
DR   AlphaFoldDB; P02019; -.
DR   SMR; P02019; -.
DR   MINT; P02019; -.
DR   iPTMnet; P02019; -.
DR   PRIDE; P02019; -.
DR   EvolutionaryTrace; P02019; -.
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..144
FT                   /note="Hemoglobin subunit alpha-1"
FT                   /id="PRO_0000052758"
FT   BINDING         61
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         90
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:708770"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           21..31
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           34..37
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           39..45
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           56..74
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   TURN            75..77
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           79..82
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           84..92
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           99..115
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:1OUT"
FT   HELIX           122..140
FT                   /evidence="ECO:0007829|PDB:1OUT"
SQ   SEQUENCE   144 AA;  15306 MW;  DB683115939E78EA CRC64;
     SLTAKDKSVV KAFWGKISGK ADVVGAEALG RDKMLTAYPQ TKTYFSHWAD LSPGSGPVKK
     HGGIIMGAIG KAVGLMDDLV GGMSALSDLH AFKLRVDPGN FKILSHNILV TLAIHFPSDF
     TPEVHIAVDK FLAAVSAALA DKYR