HBA_COLLI
ID HBA_COLLI Reviewed; 142 AA.
AC P21871; O12986; Q91249;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Hemoglobin subunit alpha-A;
DE AltName: Full=Alpha-A-globin;
DE AltName: Full=Hemoglobin alpha-A chain;
GN Name=HBAA;
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2263473; DOI=10.1093/nar/18.23.7135;
RA Eguchi Y., Nakashima Y., Oshiro M., Takei H.;
RT "Complete nucleotide sequence of a pigeon alpha-globin cDNA.";
RL Nucleic Acids Res. 18:7135-7135(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9177291; DOI=10.1006/bbrc.1997.6667;
RA Ikehara T., Eguchi Y., Kayo S., Takei H.;
RT "Isolation and sequencing of two alpha-globin genes alpha(A) and alpha(D)
RT in pigeon and evidence for embryo-specific expression of the alpha(D)-
RT globin gene.";
RL Biochem. Biophys. Res. Commun. 234:450-453(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=2610857; DOI=10.1007/bf01025603;
RA Sultana C., Abbasi A., Zaidi Z.H.;
RT "Primary structure of hemoglobin alpha-chain of Columba livia (gray wild
RT pigeon).";
RL J. Protein Chem. 8:629-646(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-136.
RX PubMed=6689309; DOI=10.1016/0378-1119(83)90171-3;
RA Pletnev A.G., Scobeleva N.A., Frolova L.Y., Kisselev L.L.;
RT "Nucleotide sequence of the anemic pigeon alpha-globin gene. Structural
RT rearrangements in the cloned cDNA.";
RL Gene 25:93-100(1983).
CC -!- FUNCTION: Involved in oxygen transport from the lung 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 EMBL; X56349; CAA39793.1; -; mRNA.
DR EMBL; AB001981; BAA19669.1; -; Genomic_DNA.
DR EMBL; K01179; AAA49449.1; -; mRNA.
DR PIR; JC5514; JC5514.
DR RefSeq; XP_005508518.1; XM_005508461.1.
DR PDB; 2R80; X-ray; 1.44 A; A/C=2-142.
DR PDB; 3DHR; X-ray; 2.00 A; A/C/E/G=1-142.
DR PDB; 3MJU; X-ray; 3.50 A; A=2-142.
DR PDBsum; 2R80; -.
DR PDBsum; 3DHR; -.
DR PDBsum; 3MJU; -.
DR AlphaFoldDB; P21871; -.
DR SMR; P21871; -.
DR STRING; 8932.XP_005508518.1; -.
DR GeneID; 102090851; -.
DR KEGG; clv:102090851; -.
DR eggNOG; KOG3378; Eukaryota.
DR OrthoDB; 1398217at2759; -.
DR EvolutionaryTrace; P21871; -.
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; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2610857"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-A"
FT /id="PRO_0000052605"
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 CONFLICT 9
FT /note="S -> N (in Ref. 4; AAA49449)"
FT /evidence="ECO:0000305"
FT CONFLICT 14..20
FT /note="VFAKIGG -> IFGKIAA (in Ref. 4; AAA49449)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="A -> G (in Ref. 2; BAA19669)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="A -> V (in Ref. 4; AAA49449)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="V -> L (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="L -> C (in Ref. 2 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="V -> P (in Ref. 4; AAA49449)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:2R80"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:2R80"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:2R80"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:2R80"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:2R80"
SQ SEQUENCE 142 AA; 15273 MW; A4CE77962BBE6EFB CRC64;
MVLSANDKSN VKAVFAKIGG QAGDLGGEAL ERLFITYPQT KTYFPHFDLS HGSAQIKGHG
KKVAEALVEA ANHIDDIAGA LSKLSDLHAQ KLRVDPVNFK LLGHCFLVVV AVHFPSLLTP
EVHASLDKFV LAVGTVLTAK YR
