HBA_EQUAS
ID HBA_EQUAS Reviewed; 142 AA.
AC P01959; P82988;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
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=HBA1;
GN and
GN Name=HBA2;
OS Equus asinus (Donkey) (Equus africanus asinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9793;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HBA1 AND HBA2).
RX PubMed=9847419; DOI=10.1007/pl00006436;
RA Oakenfull E.A., Clegg J.B.;
RT "Phylogenetic relationships within the genus Equus and the evolution of
RT alpha and theta globin genes.";
RL J. Mol. Evol. 47:772-783(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-142.
RX PubMed=6030605; DOI=10.1038/213269a0;
RA Kilmartin J.V., Clegg J.B.;
RT "Amino-acid replacements in horse haemoglobin.";
RL Nature 213:269-271(1967).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=16488065; DOI=10.1016/j.biochi.2006.01.001;
RA Balasundaresan D., Saraboji K., Ponnuswamy M.N.;
RT "Crystal structure of haemoglobin from donkey (Equus asinus) at 3A
RT resolution.";
RL Biochimie 88:719-723(2006).
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 -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; U69894; AAD13640.1; -; Genomic_DNA.
DR EMBL; U69895; AAD13641.1; -; Genomic_DNA.
DR PIR; A02282; HAHOD.
DR PDB; 1S0H; X-ray; 3.00 A; A=2-142.
DR PDBsum; 1S0H; -.
DR AlphaFoldDB; P01959; -.
DR SMR; P01959; -.
DR PeptideAtlas; P01959; -.
DR OMA; FGKIGGQ; -.
DR EvolutionaryTrace; P01959; -.
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; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6030605"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052624"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455869"
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 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 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 CONFLICT 132
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:1S0H"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:1S0H"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1S0H"
FT HELIX 120..136
FT /evidence="ECO:0007829|PDB:1S0H"
FT TURN 137..141
FT /evidence="ECO:0007829|PDB:1S0H"
SQ SEQUENCE 142 AA; 15220 MW; 93B837BC15C1D175 CRC64;
MVLSAADKTN VKAAWSKVGG NAGEFGAEAL ERMFLGFPTT KTYFPHFDLS HGSAQVKAHG
KKVGDALTLA VGHLDDLPGA LSNLSDLHAH KLRVDPVNFK LLSHCLLSTL AVHLPNDFTP
AVHASLDKFL STVSTVLTSK YR
