ID   HBA_CYGMA               Reviewed;         142 AA.
AC   P23016;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=hba;
OS   Cygnodraco mawsoni (Antarctic dragonfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Bathydraconidae; Cygnodraco.
OX   NCBI_TaxID=8216;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT SER-1.
RX   PubMed=2065095; DOI=10.1016/0167-4838(91)90569-l;
RA   Caruso C., Rutigliano B., Romano M., di Prisco G.;
RT   "The hemoglobins of the cold-adapted Antarctic teleost Cygnodraco
RT   mawsoni.";
RL   Biochim. Biophys. Acta 1078:273-282(1991).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Hb1 is a heterotetramer of two alpha chains and two beta-1
CC       chains, while Hb2 is a heterotetramer of two alpha chains and two beta-
CC       2 chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 (major) and Hb2
CC       (about 5% of the total). They display the Bohr and root effects.
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; S16184; S16184.
DR   AlphaFoldDB; P23016; -.
DR   SMR; P23016; -.
DR   iPTMnet; P23016; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
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; 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   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   Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..142
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000052612"
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:2065095"
SQ   SEQUENCE   142 AA;  15713 MW;  CA4F1A43C4A17DB7 CRC64;
     SLSDKDKAAV KALWTTISKS SDAIGNDALS RMIVVYPQTK TYFSHWPDVT PGSTHIRDHG
     KKVMGGISLA VSKIDDLKTG LFELSEQHAF KLRVDPANFK ILNHCILVVI ATMFPKEFTP
     EAHVSLDKFL SGVALALAER YR