ID   HBA1_ELEMC              Reviewed;         142 AA.
AC   K7N5M5; P86713;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 2.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Hemoglobin subunit alpha 1 {ECO:0000250|UniProtKB:P10777};
DE   AltName: Full=Alpha-1-globin {ECO:0000250|UniProtKB:P10777};
DE   AltName: Full=Hemoglobin alpha-1 chain {ECO:0000303|PubMed:23086282};
GN   Name=hba1 {ECO:0000250|UniProtKB:P10777};
OS   Eleginops maclovinus (Patagonian blennie) (Eleginus maclovinus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Eleginopidae; Eleginops.
OX   NCBI_TaxID=56733 {ECO:0000312|PDB:4ESA};
RN   [1] {ECO:0000312|PDB:4ESA}
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS)
RP   OF 1-142 IN COMPLEX WITH HEME AND CARBON MONOXIDE, AND ACETYLATION AT
RP   SER-1.
RC   TISSUE=Blood {ECO:0000303|PubMed:23086282};
RX   PubMed=23086282; DOI=10.1039/c2mb25210d;
RA   Coppola D., Abbruzzetti S., Nicoletti F., Merlino A., Gambacurta A.,
RA   Giordano D., Howes B.D., De Sanctis G., Vitagliano L., Bruno S.,
RA   di Prisco G., Mazzarella L., Smulevich G., Coletta M., Viappiani C.,
RA   Vergara A., Verde C.;
RT   "ATP regulation of the ligand-binding properties in temperate and cold-
RT   adapted haemoglobins. X-ray structure and ligand-binding kinetics in the
RT   sub-Antarctic fish Eleginops maclovinus.";
RL   Mol. Biosyst. 8:3295-3304(2012).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000303|PubMed:23086282}.
CC   -!- SUBUNIT: Hb1 is a heterotetramer of two alpha-1 chains and two beta-1
CC       chains. Hb2 is a heterotetramer of two alpha-2 chains and two beta-1
CC       chains. HbC is a heterotetramer of two alpha-1 chains and two beta-2
CC       chains. {ECO:0000269|PubMed:23086282}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: This fish has three hemoglobins: Hb1, Hb2 and HbC
CC       accounting for about 70%, 5% and 25% of the total, respectively. Hb1
CC       has high oxygen affinity and displays strong Bohr, Root and phosphate
CC       effects. {ECO:0000269|PubMed:23086282}.
CC   -!- SIMILARITY: Belongs to the globin family.
CC       {ECO:0000255|RuleBase:RU000356}.
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DR   PDB; 4ESA; X-ray; 1.45 A; A/C=1-142.
DR   PDB; 6RP5; X-ray; 1.49 A; A=1-142.
DR   PDBsum; 4ESA; -.
DR   PDBsum; 6RP5; -.
DR   AlphaFoldDB; K7N5M5; -.
DR   SMR; K7N5M5; -.
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; Transport.
FT   CHAIN           1..142
FT                   /note="Hemoglobin subunit alpha 1"
FT                   /id="PRO_0000430573"
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                   /evidence="ECO:0000269|PubMed:23086282"
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                   /evidence="ECO:0000269|PubMed:23086282"
FT   MOD_RES         1
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000312|PDB:4ESA"
FT   HELIX           4..17
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           18..20
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:6RP5"
FT   HELIX           54..72
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           77..80
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           82..89
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:6RP5"
FT   HELIX           96..113
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   HELIX           120..137
FT                   /evidence="ECO:0007829|PDB:4ESA"
FT   TURN            138..140
FT                   /evidence="ECO:0007829|PDB:4ESA"
SQ   SEQUENCE   142 AA;  15636 MW;  BB2F4F281C13DA4A CRC64;
     SLSDKDKAAV KLLWSKISKS SDAIGNDALS RMIVVYPQTK TYFAHWPDLS PGSPHVKAHG
     KTVMGGIALA VSKIDDLRAG LLDLSEQHAY KLRVDPANFK ILSHCILVVI SMMFPKEFTP
     EAHVSLDKFL SGVSLALSER YR