ID   HBA_LATCH               Reviewed;         142 AA.
AC   P23740;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   02-SEP-2026, entry version 113.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=HBA;
OS   Latimeria chalumnae (Coelacanth).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1958318; DOI=10.1515/bchm3.1991.372.2.599;
RA   Gorr T., Kleinschmidt T., Sgouros J.G., Kasang L.;
RT   "A 'living fossil' sequence: primary structure of the coelacanth (Latimeria
RT   chalumnae) hemoglobin -- evolutionary and functional aspects.";
RL   Biol. Chem. Hoppe-Seyler 372:599-612(1991).
RN   [2]
RP   PHYLOGENETIC COMPARISONS.
RX   PubMed=2034288; DOI=10.1038/351394a0;
RA   Gorr T., Kleinschmidt T., Fricke H.;
RT   "Close tetrapod relationships of the coelacanth Latimeria indicated by
RT   haemoglobin sequences.";
RL   Nature 351:394-397(1991).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains (an
CC       easy dimerization is also reported).
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; S15411; S15411.
DR   AlphaFoldDB; P23740; -.
DR   SMR; P23740; -.
DR   STRING; 7897.ENSLACP00000006614; -.
DR   eggNOG; KOG3378; Eukaryota.
DR   InParanoid; P23740; -.
DR   OMA; MVKAFWA; -.
DR   Proteomes; UP000008672; Unassembled WGS sequence.
DR   GO; GO:0072562; C:blood microparticle; IEA:TreeGrafter.
DR   GO; GO:0031838; C:haptoglobin-hemoglobin complex; IEA:TreeGrafter.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0031720; F:haptoglobin binding; IEA:TreeGrafter.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0043177; F:organic acid binding; IEA:TreeGrafter.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen carrier activity; IEA:TreeGrafter.
DR   GO; GO:0004601; F:peroxidase activity; IEA:TreeGrafter.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:TreeGrafter.
DR   CDD; cd08927; Hb-alpha-like; 1.
DR   FunFam; 1.10.490.10:FF:000002; Hemoglobin subunit alpha; 1.
DR   Gene3D; 1.10.490.10; Globins; 1.
DR   InterPro; IPR000971; Globin.
DR   InterPro; IPR009050; Globin-like_sf.
DR   InterPro; IPR012292; Globin/Proto.
DR   InterPro; IPR002338; Hemoglobin_a-typ.
DR   InterPro; IPR050056; Hemoglobin_oxygen_transport.
DR   PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..142
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000052662"
FT   DOMAIN          1..142
FT                   /note="Globin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
FT   BINDING         59
FT                   /ligand="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   142 AA;  15867 MW;  86ADC5E51EAFEB4E CRC64;
     GLTAADKTLI KSIWGKVEKE TEAIGVEALV RLFKCFPQSK VYFDHFTDLS PSSQKLHAHA
     KVVLGALTKA VNHLDNITDT LHDISLVHAK KLLVDPVNFE LLGHCLEVAL AAHFATDFTP
     EVHLAIDKFL YEVEKALFET YR
//