ID   HBA1_COTGO              Reviewed;         143 AA.
AC   P84653;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Hemoglobin subunit alpha-1;
DE   AltName: Full=Alpha-1-globin;
DE   AltName: Full=Hemoglobin alpha-1 chain;
GN   Name=hba1;
OS   Cottoperca gobio (Frogmouth) (Aphritis gobio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca.
OX   NCBI_TaxID=56716;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-143, AND SUBUNIT.
RC   TISSUE=Blood {ECO:0000269|Ref.1};
RA   Giordano D., Grassi L., Parisi E., Bargelloni L., di Prisco G., Verde C.;
RT   "Embryonic beta-globin in the non-Antartic notothenioid fish Cottoperca
RT   gobio (Bovichtidae).";
RL   Polar Biol. 30:75-82(2006).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-143, SUBUNIT, AND ACETYLATION AT SER-2.
RC   TISSUE=Blood {ECO:0000269|PubMed:19292863};
RX   PubMed=19292863; DOI=10.1111/j.1742-4658.2009.06954.x;
RA   Giordano D., Boechi L., Vergara A., Marti M.A., Samuni U., Dantsker D.,
RA   Grassi L., Estrin D.A., Friedman J.M., Mazzarella L., di Prisco G.,
RA   Verde C.;
RT   "The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically
RT   basal species--oxygen-binding equilibria, kinetics and molecular
RT   dynamics.";
RL   FEBS J. 276:2266-2277(2009).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000305}.
CC   -!- SUBUNIT: Hb 1 is a heterotetramer of two alpha-1 and two beta chains.
CC       {ECO:0000269|PubMed:19292863, ECO:0000269|Ref.1}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 and Hb2. They display
CC       the Bohr and root effects. {ECO:0000269|PubMed:19292863}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P84653; -.
DR   SMR; P84653; -.
DR   iPTMnet; P84653; -.
DR   Ensembl; ENSCGOT00000014598; ENSCGOP00000013506; ENSCGOG00000006588.
DR   Proteomes; UP000504630; Genome assembly.
DR   GO; GO:0005833; C:hemoglobin complex; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0015671; P:oxygen transport; ISS:UniProtKB.
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; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..143
FT                   /note="Hemoglobin subunit alpha-1"
FT                   /evidence="ECO:0000269|PubMed:19292863"
FT                   /id="PRO_0000250611"
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                   /evidence="ECO:0000250|UniProtKB:P45718,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000250|UniProtKB:P45718,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:19292863"
SQ   SEQUENCE   143 AA;  15816 MW;  4117BA6C9A124E11 CRC64;
     MSLTEKDKAA VRALWGKISK SADAIGADAL SRMLFVYPQT KTYFTHWPDL SPGSVHVKKH
     GKNVMGGIAL AVSKIDDLTN GLMELSEQHA YQLRVDPANF KILSHCILVV VSIMYPKDFT
     PEAHVSLDKF LSGVSLALAE RYR