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Hemoglobin subunit beta-A (Alanine beta-globin) (Beta-A-globin) (Hemoglobin beta-A chain)

 HBBA_CAPHI              Reviewed;         145 AA.
P02077; P79429;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-MAY-2017, entry version 103.
RecName: Full=Hemoglobin subunit beta-A;
AltName: Full=Alanine beta-globin;
AltName: Full=Beta-A-globin;
AltName: Full=Hemoglobin beta-A chain;
Capra hircus (Goat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Capra.
NCBI_TaxID=9925;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6277503; DOI=10.1016/0092-8674(81)90419-0;
Schon E.A., Cleary M.L., Haynes J.R., Lingrel J.B.;
"Structure and evolution of goat gamma-, beta C- and beta A-globin
genes: three developmentally regulated genes contain inserted
elements.";
Cell 27:359-369(1981).
[2]
PARTIAL PROTEIN SEQUENCE (ALLELE A).
PubMed=6026247;
Huisman T.H.J., Adams H.R., Dimmock M.O., Edwards W.E., Wilson J.B.;
"The structure of goat hemoglobins. I. Structural studies of the beta
chains of the hemoglobins of normal and anemic goats.";
J. Biol. Chem. 242:2534-2541(1967).
[3]
PARTIAL PROTEIN SEQUENCE (ALLELE D).
PubMed=5697993; DOI=10.1016/0003-9861(68)90242-7;
Adams H.R., Boyd E.M., Wilson J.B., Miller A., Huisman T.H.J.;
"The structure of goat hemoglobins. 3. Hemoglobin D, a beta chain
variant with one apparent amino acid substitution (21 Asp-->His).";
Arch. Biochem. Biophys. 127:398-405(1968).
[4]
PARTIAL PROTEIN SEQUENCE (ALLELE E).
PubMed=5433580; DOI=10.1016/0003-9861(70)90368-1;
Wrightstone R.N., Wilson J.B., Miller A., Huisman T.H.J.;
"The structure of goat hemoglobins. IV. A third beta chain variant
(betaE) with three apparent amino acid substitutions.";
Arch. Biochem. Biophys. 138:451-456(1970).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-97 AND 114-119.
PubMed=6248519;
Haynes J.R., Rosteck P.R. Jr., Schon E.A., Gallagher P.M., Burks D.J.,
Smith K., Lingrel J.B.;
"The isolation of the beta A-, beta C-, and gamma-globin genes and a
presumptive embryonic globin gene from a goat DNA recombinant
library.";
J. Biol. Chem. 255:6355-6367(1980).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues.
-!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
-!- TISSUE SPECIFICITY: Red blood cells.
-!- POLYMORPHISM: There are at least three alleles. The sequence shown
is that of allele A. {ECO:0000269|PubMed:5433580,
ECO:0000269|PubMed:5697993, ECO:0000269|PubMed:6026247}.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
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EMBL; M15387; AAA30913.1; -; Genomic_DNA.
EMBL; K00657; AAA30911.1; -; Genomic_DNA.
EMBL; K00658; AAA30912.1; -; Genomic_DNA.
PIR; A90817; HBGTA.
RefSeq; XP_005689872.2; XM_005689815.3.
UniGene; Chi.34344; -.
PDB; 2RI4; X-ray; 2.70 A; B/D/J/L=1-145.
PDB; 3D1A; X-ray; 2.61 A; B/D=1-145.
PDB; 3EU1; X-ray; 3.00 A; B/D=1-145.
PDBsum; 2RI4; -.
PDBsum; 3D1A; -.
PDBsum; 3EU1; -.
ProteinModelPortal; P02077; -.
SMR; P02077; -.
PRIDE; P02077; -.
GeneID; 102175876; -.
KEGG; chx:102175876; -.
HOVERGEN; HBG009709; -.
KO; K13823; -.
EvolutionaryTrace; P02077; -.
GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
CDD; cd08925; Hb-beta_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like.
InterPro; IPR002337; Haemoglobin_b.
Pfam; PF00042; Globin; 1.
PRINTS; PR00814; BETAHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
Oxygen transport; Polymorphism; Transport.
CHAIN 1 145 Hemoglobin subunit beta-A.
/FTId=PRO_0000052909.
METAL 62 62 Iron (heme distal ligand).
METAL 91 91 Iron (heme proximal ligand).
VARIANT 20 20 D -> H (in allele D).
{ECO:0000269|PubMed:5697993}.
VARIANT 86 86 Q -> H (in allele E).
{ECO:0000269|PubMed:5433580}.
VARIANT 103 103 K -> R (in allele E).
{ECO:0000269|PubMed:5433580}.
VARIANT 124 124 L -> V (in allele E).
{ECO:0000269|PubMed:5433580}.
HELIX 4 14 {ECO:0000244|PDB:3D1A}.
HELIX 19 33 {ECO:0000244|PDB:3D1A}.
HELIX 35 40 {ECO:0000244|PDB:3D1A}.
HELIX 42 44 {ECO:0000244|PDB:3D1A}.
HELIX 50 54 {ECO:0000244|PDB:3D1A}.
HELIX 57 73 {ECO:0000244|PDB:3D1A}.
HELIX 77 79 {ECO:0000244|PDB:3D1A}.
HELIX 80 83 {ECO:0000244|PDB:3D1A}.
HELIX 85 93 {ECO:0000244|PDB:3D1A}.
HELIX 100 117 {ECO:0000244|PDB:3D1A}.
HELIX 118 120 {ECO:0000244|PDB:3D1A}.
HELIX 123 141 {ECO:0000244|PDB:3D1A}.
HELIX 142 144 {ECO:0000244|PDB:3D1A}.
SEQUENCE 145 AA; 16021 MW; 6C59F105A940F4D0 CRC64;
MLTAEEKAAV TGFWGKVKVD EVGAEALGRL LVVYPWTQRF FEHFGDLSSA DAVMNNAKVK
AHGKKVLDSF SNGMKHLDDL KGTFAQLSEL HCDKLHVDPE NFKLLGNVLV VVLARHHGSE
FTPLLQAEFQ KVVAGVANAL AHRYH


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