ID   HBA2_ANAMI              Reviewed;         143 AA.
AC   P83271;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Hemoglobin subunit alpha-2;
DE   AltName: Full=Alpha-2-globin;
DE   AltName: Full=Hemoglobin alpha-2 chain;
GN   Name=hba2;
OS   Anarhichas minor (Arctic spotted wolffish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Zoarcales; Anarhichadidae; Anarhichas.
OX   NCBI_TaxID=65739;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-143, FUNCTION, TISSUE SPECIFICITY, AND ACETYLATION AT
RP   SER-2.
RX   PubMed=12118003; DOI=10.1074/jbc.m202474200;
RA   Verde C., Carratore V., Riccio A., Tamburrini M., Parisi E., Di Prisco G.;
RT   "The functionally distinct hemoglobins of the Arctic spotted wolffish
RT   Anarhichas minor.";
RL   J. Biol. Chem. 277:36312-36320(2002).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:12118003}.
CC   -!- SUBUNIT: Hb2 is a heterotetramer of two alpha-2 chains and two beta-1
CC       chains; Hb3 is a heterotetramer of two alpha-2 chains and two beta-2
CC       chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:12118003}.
CC   -!- MISCELLANEOUS: Hb2 displays a low, effector-enhanced Bohr effect and no
CC       Root effect. Hb3 displays pronounced Bohr and Root effects, accompanied
CC       by strong organophosphate regulation.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P83271; -.
DR   SMR; P83271; -.
DR   iPTMnet; P83271; -.
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; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..143
FT                   /note="Hemoglobin subunit alpha-2"
FT                   /id="PRO_0000052545"
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:12118003"
SQ   SEQUENCE   143 AA;  15685 MW;  6C35DAE034AB5A94 CRC64;
     MSLTEKDKAA VIAMWGKIHK SADAIGADAL GRMLVVYPQT KTYFSHWSDL SPNSAPVKTH
     GKNVMSGVAL AVSKIDDMTK GLMALSEQHA FQLRVDPANF KILSHCILVV IASMFPKDFT
     PEAHVSMDKF FCGLSLALAE KYR