HBA_ODOVI
ID HBA_ODOVI Reviewed; 141 AA.
AC P01972;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Hemoglobin subunit alpha-1/2;
DE AltName: Full=Alpha-1/2-globin;
DE AltName: Full=Hemoglobin alpha-1/2 chain;
OS Odocoileus virginianus virginianus (Virginia white-tailed deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Odocoileinae; Odocoileus.
OX NCBI_TaxID=9875;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=5045934; DOI=10.1016/0003-9861(72)90531-0;
RA Harris M.J., Wilson J.B., Huisman T.H.J.;
RT "Structural studies of hemoglobin alpha-chains from Virginia white-tailed
RT deer.";
RL Arch. Biochem. Biophys. 151:540-548(1972).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
RA Schmidt W.C. Jr., Girling R.L., Houston T.E., Sproul G.D., Amma E.L.,
RA Huisman T.H.J.;
RT "The structure of sickling deer type III hemoglobin by molecular
RT replacement.";
RL Acta Crystallogr. B 33:335-342(1977).
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 -!- POLYMORPHISM: There are three alleles of the alpha-1 chain (alpha-1*1,
CC alpha-1*2 and alpha-1*3). The sequence shown is alpha-1*1. The alpha-2
CC chain is non-allelic.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02296; HADE1V.
DR PDB; 1HDS; X-ray; 1.98 A; A/C=1-141.
DR PDBsum; 1HDS; -.
DR SMR; P01972; -.
DR EvolutionaryTrace; P01972; -.
DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
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 CHAIN 1..141
FT /note="Hemoglobin subunit alpha-1/2"
FT /id="PRO_0000052708"
FT BINDING 58
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 87
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 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 7
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 11
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 16
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 40
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT VARIANT 5
FT /note="A -> T (in alpha-1*2 chain)"
FT VARIANT 20
FT /note="N -> K (in alpha-2 chain)"
FT VARIANT 24
FT /note="Y -> F (in alpha-2 chain and alpha-1*3 chain)"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 22..28
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 54..69
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 84..88
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 98..112
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1HDS"
FT HELIX 119..135
FT /evidence="ECO:0007829|PDB:1HDS"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1HDS"
SQ SEQUENCE 141 AA; 15127 MW; 5B2EBB566F902D4F CRC64;
VLSAABKSBV KAAWGKVGGN AAPYGAZALZ RMFLSFPTTK TYFPHFBLSH GSAZVKAHGZ
KVABALTKAV GHLBBLPGTL SBLSBLHAHK LRVBPVBFKL LSHSLLVTLA THLPBBFTPA
VHASLBKFLA BVSTVLTSKY R
