ID   HBA2_GADMO              Reviewed;         143 AA.
AC   O42425;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Hemoglobin subunit alpha-2;
DE   AltName: Full=Alpha-2-globin;
DE   AltName: Full=Hemoglobin alpha-2 chain;
GN   Name=hba2; Synonyms=hba;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RA   Tipping D.R., Birley A.J.;
RT   "Molecular genetic indicators of selection in haemoglobin encoding loci of
RT   the Atlantic cod, Gadus morhua.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 2-143, FUNCTION, SUBUNIT, AND ACETYLATION AT SER-2.
RC   TISSUE=Blood;
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}.
CC   -!- SUBUNIT: Hb 2 is a heterotetramer of two alpha-2 and two beta-2 chains.
CC       {ECO:0000269|PubMed:16717098}.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   EMBL; X98195; CAA66866.1; -; mRNA.
DR   PDB; 6HIT; X-ray; 2.50 A; A/C/E/G=2-143.
DR   PDBsum; 6HIT; -.
DR   AlphaFoldDB; O42425; -.
DR   SMR; O42425; -.
DR   STRING; 8049.ENSGMOP00000006057; -.
DR   iPTMnet; O42425; -.
DR   Proteomes; UP000694546; Unplaced.
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   3D-structure; Acetylation; Direct protein sequencing; Heme; Iron;
KW   Metal-binding; Oxygen transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:16717098"
FT   CHAIN           2..143
FT                   /note="Hemoglobin subunit alpha-2"
FT                   /id="PRO_0000052637"
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   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   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:16717098"
FT   HELIX           5..17
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           18..21
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           22..36
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           38..44
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           55..73
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   TURN            74..76
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           78..81
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           83..90
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           97..99
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           100..114
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:6HIT"
FT   HELIX           121..139
FT                   /evidence="ECO:0007829|PDB:6HIT"
SQ   SEQUENCE   143 AA;  15784 MW;  FFFBD93E07E0F09F CRC64;
     MSLSSKQKAT VKDFFSKMST RSDDIGAEAL SRLVAVYPQT KSYFSHWKDA SPGSAPVRKH
     GITTMGGVYD AVGKIDDLKG GLLSLSELHA FMLRVDPVNF KLLAHCMLVC MSMIFPEEFT
     PQVHVAVDKF LAQLALALAE KYR