HBA_SHEEP
ID HBA_SHEEP Reviewed; 142 AA.
AC P68240; P01970;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Hemoglobin subunit alpha-1/2;
DE AltName: Full=Alpha-1/2-globin;
DE AltName: Full=Hemoglobin alpha-1/2 chain;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE OF 2-142.
RC STRAIN=Clan breed, and Soay;
RX PubMed=6033754; DOI=10.1042/bj1030129;
RA Beale D.;
RT "A partial amino acid sequence for sheep haemoblogin A.";
RL Biochem. J. 103:129-140(1967).
RN [2]
RP PROTEIN SEQUENCE OF 2-142.
RC STRAIN=Rambouillet;
RX PubMed=5658545; DOI=10.1016/s0021-9258(19)34193-6;
RA Wilson J.B., Brandt G., Huisman T.H.J.;
RT "The structure of sheep hemoglobins. 3. Structural studies on the alpha
RT chain of hemoglobin A.";
RL J. Biol. Chem. 243:3687-3692(1968).
RN [3]
RP VARIANT ASP-16.
RX PubMed=5680274; DOI=10.1016/0005-2795(68)90219-5;
RA Huisman T.H.J., Dozy A.M., Wilson J.B., Efremov G.D., Vaskov B.;
RT "Sheep hemoglobin D, an alpha-chain variant with one apparent amino acid
RT substitution (alpha 15 Gly-->Asp).";
RL Biochim. Biophys. Acta 160:467-469(1968).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000250}.
CC -!- POLYMORPHISM: Different alleles are known. The alpha-A allelic variant
CC contains Gly-16. {ECO:0000269|PubMed:5680274}.
CC -!- MISCELLANEOUS: Adult sheep and other mammalian species produce unequal
CC amounts of alpha-globin from their non-allelic loci.
CC -!- MISCELLANEOUS: The alpha-1 sequence is shown.
CC -!- MISCELLANEOUS: Sheep insoluble core region (positions 101-140) contains
CC 1 more Gly, one more Glu, and two fewer Ser than the corresponding
CC region shown (PubMed:6033754). According to PubMed:5658545 it contains
CC one more Thr and one less Ser. {ECO:0000305|PubMed:6033754}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PDB; 2QU0; X-ray; 2.70 A; A/C=2-142.
DR PDBsum; 2QU0; -.
DR AlphaFoldDB; P68240; -.
DR SMR; P68240; -.
DR STRING; 9940.ENSOARP00000011736; -.
DR PRIDE; P68240; -.
DR eggNOG; KOG3378; Eukaryota.
DR EvolutionaryTrace; P68240; -.
DR Proteomes; UP000002356; 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:5658545,
FT ECO:0000269|PubMed:6033754"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-1/2"
FT /id="PRO_0000052584"
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 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 36
FT /note="Phosphoserine"
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 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 16
FT /note="G -> D (in allele alpha-D)"
FT /evidence="ECO:0000269|PubMed:5680274"
FT VARIANT 20
FT /note="G -> S (in alpha-2)"
FT VARIANT 76
FT /note="D -> Y (in alpha-1-B)"
FT VARIANT 114
FT /note="L -> H (in alpha-2)"
FT VARIANT 116
FT /note="N -> S (in alpha-2)"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:2QU0"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:2QU0"
SQ SEQUENCE 142 AA; 15164 MW; 1C3CF84DEB3C2176 CRC64;
MVLSAADKSN VKAAWGKVGG NAGAYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
EKVAAALTKA VGHLDDLPGT LSDLSDLHAH KLRVDPVNFK LLSHSLLVTL ACHLPNDFTP
AVHASLDKFL ANVSTVLTSK YR
