HBBA_CAPHI
ID HBBA_CAPHI Reviewed; 145 AA.
AC P02077; P79429;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Hemoglobin subunit beta-A;
DE AltName: Full=Alanine beta-globin;
DE AltName: Full=Beta-A-globin;
DE AltName: Full=Hemoglobin beta-A chain;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6277503; DOI=10.1016/0092-8674(81)90419-0;
RA Schon E.A., Cleary M.L., Haynes J.R., Lingrel J.B.;
RT "Structure and evolution of goat gamma-, beta C- and beta A-globin genes:
RT three developmentally regulated genes contain inserted elements.";
RL Cell 27:359-369(1981).
RN [2]
RP PARTIAL PROTEIN SEQUENCE (ALLELE A).
RX PubMed=6026247; DOI=10.1016/s0021-9258(18)95996-x;
RA Huisman T.H.J., Adams H.R., Dimmock M.O., Edwards W.E., Wilson J.B.;
RT "The structure of goat hemoglobins. I. Structural studies of the beta
RT chains of the hemoglobins of normal and anemic goats.";
RL J. Biol. Chem. 242:2534-2541(1967).
RN [3]
RP PARTIAL PROTEIN SEQUENCE (ALLELE D).
RX PubMed=5697993; DOI=10.1016/0003-9861(68)90242-7;
RA Adams H.R., Boyd E.M., Wilson J.B., Miller A., Huisman T.H.J.;
RT "The structure of goat hemoglobins. 3. Hemoglobin D, a beta chain variant
RT with one apparent amino acid substitution (21 Asp-->His).";
RL Arch. Biochem. Biophys. 127:398-405(1968).
RN [4]
RP PARTIAL PROTEIN SEQUENCE (ALLELE E).
RX PubMed=5433580; DOI=10.1016/0003-9861(70)90368-1;
RA Wrightstone R.N., Wilson J.B., Miller A., Huisman T.H.J.;
RT "The structure of goat hemoglobins. IV. A third beta chain variant (betaE)
RT with three apparent amino acid substitutions.";
RL Arch. Biochem. Biophys. 138:451-456(1970).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-97 AND 114-119.
RX PubMed=6248519; DOI=10.1016/s0021-9258(18)43745-3;
RA Haynes J.R., Rosteck P.R. Jr., Schon E.A., Gallagher P.M., Burks D.J.,
RA Smith K., Lingrel J.B.;
RT "The isolation of the beta A-, beta C-, and gamma-globin genes and a
RT presumptive embryonic globin gene from a goat DNA recombinant library.";
RL J. Biol. Chem. 255:6355-6367(1980).
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 at least three alleles. The sequence shown is
CC that of allele A. {ECO:0000269|PubMed:5433580,
CC ECO:0000269|PubMed:5697993, ECO:0000269|PubMed:6026247}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; M15387; AAA30913.1; -; Genomic_DNA.
DR EMBL; K00657; AAA30911.1; -; Genomic_DNA.
DR EMBL; K00658; AAA30912.1; -; Genomic_DNA.
DR PIR; A90817; HBGTA.
DR RefSeq; XP_005689872.2; XM_005689815.3.
DR PDB; 2RI4; X-ray; 2.70 A; B/D/J/L=1-145.
DR PDB; 3D1A; X-ray; 2.61 A; B/D=1-145.
DR PDB; 3EU1; X-ray; 3.00 A; B/D=1-145.
DR PDBsum; 2RI4; -.
DR PDBsum; 3D1A; -.
DR PDBsum; 3EU1; -.
DR AlphaFoldDB; P02077; -.
DR SMR; P02077; -.
DR STRING; 9925.ENSCHIP00000018470; -.
DR GeneID; 102175876; -.
DR KEGG; chx:102175876; -.
DR OrthoDB; 1370439at2759; -.
DR EvolutionaryTrace; P02077; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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; cd08925; Hb-beta-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; IPR002337; Hemoglobin_b.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00814; BETAHAEM.
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; Reference proteome; Transport.
FT CHAIN 1..145
FT /note="Hemoglobin subunit beta-A"
FT /id="PRO_0000052909"
FT BINDING 62
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 91
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 VARIANT 20
FT /note="D -> H (in allele D)"
FT /evidence="ECO:0000269|PubMed:5697993"
FT VARIANT 86
FT /note="Q -> H (in allele E)"
FT /evidence="ECO:0000269|PubMed:5433580"
FT VARIANT 103
FT /note="K -> R (in allele E)"
FT /evidence="ECO:0000269|PubMed:5433580"
FT VARIANT 124
FT /note="L -> V (in allele E)"
FT /evidence="ECO:0000269|PubMed:5433580"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:3D1A"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3D1A"
SQ SEQUENCE 145 AA; 16021 MW; 6C59F105A940F4D0 CRC64;
MLTAEEKAAV TGFWGKVKVD EVGAEALGRL LVVYPWTQRF FEHFGDLSSA DAVMNNAKVK
AHGKKVLDSF SNGMKHLDDL KGTFAQLSEL HCDKLHVDPE NFKLLGNVLV VVLARHHGSE
FTPLLQAEFQ KVVAGVANAL AHRYH
