ID   HBA2_TRENE              Reviewed;         142 AA.
AC   P45719;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Hemoglobin subunit alpha-2;
DE   AltName: Full=Alpha-2-globin;
DE   AltName: Full=Hemoglobin alpha-2 chain;
GN   Name=hba2;
OS   Trematomus newnesi (Dusky notothen).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Trematomus.
OX   NCBI_TaxID=35730;
RN   [1]
RP   PROTEIN SEQUENCE, ACETYLATION AT SER-1, FUNCTION, AND SUBUNIT.
RX   PubMed=8144556; DOI=10.1016/s0021-9258(17)36935-1;
RA   D'Avino R., Caruso C., Tamburrini M., Romano M., Rutigliano B.,
RA   Polverino de Laureto P., Camardella L., Carratore V., di Prisco G.;
RT   "Molecular characterization of the functionally distinct hemoglobins of the
RT   Antarctic fish Trematomus newnesi.";
RL   J. Biol. Chem. 269:9675-9681(1994).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:8144556}.
CC   -!- SUBUNIT: Hb2 is a heterotetramer of two alpha-2 chains and two beta
CC       chains. {ECO:0000269|PubMed:8144556}.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1 (major, about 65-
CC       70% of the total), Hb2 (about 5% of the total) and HbC (about 20-25% of
CC       the total). Hb1 and Hb2 display a very weak Bohr effect and no Root
CC       effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; B54403; B54403.
DR   AlphaFoldDB; P45719; -.
DR   SMR; P45719; -.
DR   iPTMnet; P45719; -.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
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-2"
FT                   /id="PRO_0000052788"
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:8144556"
SQ   SEQUENCE   142 AA;  15828 MW;  3ABE814AF3482D46 CRC64;
     SLSTKDKETV KAFWSKVSGK TEDIGNDALS RMLVVYPQTK IYFSHWKELT PGSAPVRKHG
     MTVMKGVGDA VSKIEDLTAG LTELSELHAF TLRVDPGNFK ILSHNILVVF AIMFPNDFTP
     QVHVSMDKFL AALSRALSEK YR