HBA_HORSE
ID HBA_HORSE Reviewed; 142 AA.
AC P01958; Q28384;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946};
GN Name=HBA;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6093055; DOI=10.1093/nar/12.20.7847;
RA Clegg J.B., Goodbourn S.E.Y., Braend M.;
RT "Genetic organization of the polymorphic equine alpha globin locus and
RT sequence of the BII alpha 1 gene.";
RL Nucleic Acids Res. 12:7847-7858(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2835578; DOI=10.1093/oxfordjournals.molbev.a040456;
RA Clegg J.B.;
RT "Gene conversions in the horse alpha-globin gene complex.";
RL Mol. Biol. Evol. 4:492-503(1987).
RN [3]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=7409745;
RA Matsuda G., Maita T., Braunitzer G., Schrank B.;
RT "Hemoglobins, XXXIII. Note on the sequence of the hemoglobins of the
RT horse.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:1107-1116(1980).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=940162; DOI=10.1016/0022-2836(76)90227-8;
RA Ladner R.C., Air G.M., Fogg J.H.;
RT "A correction to the sequence of the alpha chains of horse haemoglobin.";
RL J. Mol. Biol. 103:675-677(1976).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=5659617; DOI=10.1038/219029a0;
RA Perutz M.F., Miurhead H., Cox J.M., Goaman L.C., Mathews F.S.,
RA McGandy E.L., Webb L.E.;
RT "Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8-A
RT resolution: (1) X-ray analysis.";
RL Nature 219:29-32(1968).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=5659637; DOI=10.1038/219131a0;
RA Perutz M.F., Muirhead H., Cox J.M., Goaman L.C.;
RT "Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A
RT resolution: the atomic model.";
RL Nature 219:131-139(1968).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=561852; DOI=10.1016/0022-2836(77)90256-x;
RA Ladner R.C., Heidner E.J., Perutz M.F.;
RT "The structure of horse methaemoglobin at 2.0-A resolution.";
RL J. Mol. Biol. 114:385-414(1977).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of
CC the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks
CC cannabinoid receptor CNR1 and subsequent signaling.
CC {ECO:0000250|UniProtKB:P01946}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: Horse has two non-allelic alpha chains, slow and fast.
CC The slow chain sequence is shown. {ECO:0000269|PubMed:2835578,
CC ECO:0000269|PubMed:6093055}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The man behind the molecular
CC lung - Issue 21 of April 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/021";
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DR EMBL; X01086; CAA25564.1; -; Genomic_DNA.
DR EMBL; M17902; AAD15306.1; -; Genomic_DNA.
DR EMBL; M17903; AAA30948.1; -; Genomic_DNA.
DR EMBL; X07053; CAA30097.1; -; Genomic_DNA.
DR PIR; I46302; HAHO.
DR RefSeq; NP_001078901.1; NM_001085432.1.
DR PDB; 1G0B; X-ray; 1.90 A; A=2-142.
DR PDB; 1IBE; X-ray; 1.80 A; A=2-142.
DR PDB; 1IWH; X-ray; 1.55 A; A=2-142.
DR PDB; 1NS6; X-ray; 2.05 A; A=2-142.
DR PDB; 1NS9; X-ray; 1.60 A; A=2-142.
DR PDB; 1Y8H; X-ray; 3.10 A; A/C=2-142.
DR PDB; 1Y8I; X-ray; 2.60 A; A/C=2-142.
DR PDB; 1Y8K; X-ray; 2.30 A; A/C=2-142.
DR PDB; 2D5X; X-ray; 1.45 A; A=2-142.
DR PDB; 2DHB; X-ray; 2.80 A; A=2-142.
DR PDB; 2MHB; X-ray; 2.00 A; A=2-142.
DR PDB; 2ZLT; X-ray; 1.90 A; A=2-142.
DR PDB; 2ZLU; X-ray; 2.00 A; A=2-142.
DR PDB; 2ZLV; X-ray; 2.00 A; A=2-142.
DR PDB; 2ZLW; X-ray; 2.90 A; A/C=2-142.
DR PDB; 2ZLX; X-ray; 2.80 A; A/C=2-142.
DR PDB; 5C6E; Other; 1.70 A; A=2-142.
DR PDB; 6R2O; X-ray; 2.46 A; A/C=2-142.
DR PDB; 6SVA; X-ray; 1.92 A; A=2-141.
DR PDBsum; 1G0B; -.
DR PDBsum; 1IBE; -.
DR PDBsum; 1IWH; -.
DR PDBsum; 1NS6; -.
DR PDBsum; 1NS9; -.
DR PDBsum; 1Y8H; -.
DR PDBsum; 1Y8I; -.
DR PDBsum; 1Y8K; -.
DR PDBsum; 2D5X; -.
DR PDBsum; 2DHB; -.
DR PDBsum; 2MHB; -.
DR PDBsum; 2ZLT; -.
DR PDBsum; 2ZLU; -.
DR PDBsum; 2ZLV; -.
DR PDBsum; 2ZLW; -.
DR PDBsum; 2ZLX; -.
DR PDBsum; 5C6E; -.
DR PDBsum; 6R2O; -.
DR PDBsum; 6SVA; -.
DR AlphaFoldDB; P01958; -.
DR SMR; P01958; -.
DR MINT; P01958; -.
DR STRING; 9796.ENSECAP00000043334; -.
DR PeptideAtlas; P01958; -.
DR PRIDE; P01958; -.
DR GeneID; 100036557; -.
DR KEGG; ecb:100036557; -.
DR CTD; 15121; -.
DR InParanoid; P01958; -.
DR OrthoDB; 1398217at2759; -.
DR EvolutionaryTrace; P01958; -.
DR Proteomes; UP000002281; Unplaced.
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; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7409745"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052652"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455881"
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 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 8
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 12
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 17
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 41
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT VARIANT 25
FT /note="Y -> F (exist in both chains)"
FT VARIANT 61
FT /note="K -> Q (in fast chain)"
FT /evidence="ECO:0000269|PubMed:2835578,
FT ECO:0000269|PubMed:6093055"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:2D5X"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:1NS6"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:2D5X"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:2D5X"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:2D5X"
SQ SEQUENCE 142 AA; 15245 MW; 33BB917E15C9CD15 CRC64;
MVLSAADKTN VKAAWSKVGG HAGEYGAEAL ERMFLGFPTT KTYFPHFDLS HGSAQVKAHG
KKVGDALTLA VGHLDDLPGA LSNLSDLHAH KLRVDPVNFK LLSHCLLSTL AVHLPNDFTP
AVHASLDKFL SSVSTVLTSK YR
