ID   HBA_POGSC               Reviewed;         143 AA.
AC   P0C238;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Hemoglobin subunit alpha;
DE   AltName: Full=Alpha-globin;
DE   AltName: Full=Hemoglobin alpha chain;
GN   Name=hba;
OS   Pogonophryne scotti (Saddleback plunderfish) (Antarctic fish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Pogonophryne.
OX   NCBI_TaxID=36210;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-143, AND ACETYLATION AT SER-2.
RX   PubMed=9829976; DOI=10.1074/jbc.273.49.32452;
RA   Tamburrini M., Romano M., Carratore V., Kunzmann A., Coletta M.,
RA   di Prisco G.;
RT   "The hemoglobins of the antarctic fishes Atedidraco orianae and
RT   Pogonophryne scotti. Amino acid sequence, lack of cooperativity, and ligand
RT   binding properties.";
RL   J. Biol. Chem. 273:32452-32459(1998).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P0C238; -.
DR   SMR; P0C238; -.
DR   iPTMnet; P0C238; -.
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:0000250"
FT   CHAIN           2..143
FT                   /note="Hemoglobin subunit alpha"
FT                   /id="PRO_0000260297"
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:9829976"
SQ   SEQUENCE   143 AA;  15695 MW;  DE9446658425F88C CRC64;
     MSLSDKDKSA VKALWSKINK SADVIGNDAV SRMIVVYPQT KTYFAHWPDL TPGSTHIKAH
     GKKVMGGIAL AVSKIDDLKA GLSNLSEQHA FKLRVDPANF KILNHCIMVV ISSMFPKDFT
     PEAHVSLDKF LSAVALALAE KYR