ID   HBA1_BORSA              Reviewed;         143 AA.
AC   Q1AGS9; P84605;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Hemoglobin subunit alpha-1;
DE   AltName: Full=Alpha-1-globin;
DE   AltName: Full=Hemoglobin alpha-1 chain;
GN   Name=hba1;
OS   Boreogadus saida (Polar cod) (Gadus saida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Boreogadus.
OX   NCBI_TaxID=44932;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAZ99822.1}
RP   PROTEIN SEQUENCE OF 2-143, NUCLEOTIDE SEQUENCE [MRNA] OF 45-143, FUNCTION,
RP   SUBUNIT, AND ACETYLATION AT SER-2.
RC   TISSUE=Blood {ECO:0000269|PubMed:16717098}, and
RC   Spleen {ECO:0000269|PubMed:16717098};
RX   PubMed=16717098; DOI=10.1074/jbc.m513080200;
RA   Verde C., Balestrieri M., de Pascale D., Pagnozzi D., Lecointre G.,
RA   di Prisco G.;
RT   "The oxygen transport system in three species of the boreal fish family
RT   Gadidae. Molecular phylogeny of hemoglobin.";
RL   J. Biol. Chem. 281:22073-22084(2006).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:16717098, ECO:0000305}.
CC   -!- SUBUNIT: Hb 1 is a heterotetramer of two alpha-1 and two beta-1 chains.
CC       {ECO:0000269|PubMed:16717098}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; DQ125470; AAZ99822.1; -; mRNA.
DR   AlphaFoldDB; Q1AGS9; -.
DR   SMR; Q1AGS9; -.
DR   iPTMnet; Q1AGS9; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:16717098"
FT   CHAIN           2..143
FT                   /note="Hemoglobin subunit alpha-1"
FT                   /id="PRO_0000247577"
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: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:0000255|PROSITE-ProRule:PRU00238"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:16717098"
FT   CONFLICT        79
FT                   /note="Missing (in Ref. 1; AAZ99822)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   143 AA;  15725 MW;  FB37867E3F9E597A CRC64;
     MSLSAKDKAT VKDFFGKMST RSDDIGAEAL SRLVAVYPQT KSYFAHWKSA SPGSAPVRKH
     GITIMGGVYD AVGKIDDLKA GLLSLSELHA FMLRVDPVNF KLLAHCMLVC MSMVFPEEFT
     PQVHVAVDKF LAQLALALCE KYR