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

 HBB_CHICK               Reviewed;         147 AA.
P02112; Q90594; Q90863; Q90938;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 139.
RecName: Full=Hemoglobin subunit beta;
AltName: Full=Beta-globin;
AltName: Full=Hemoglobin beta chain;
Name=HBB;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE.
PubMed=6833240;
Dolan M., Dodgson J.B., Engel J.D.;
"Analysis of the adult chicken beta-globin gene. Nucleotide sequence
of the locus, microheterogeneity at the 5'-end of beta-globin mRNA,
and aberrant nuclear RNA species.";
J. Biol. Chem. 258:3983-3990(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=514809; DOI=10.1093/nar/7.5.1137;
Richards R.I., Shine J., Ullrich A., Wells J.R.E., Goodman H.M.;
"Molecular cloning and sequence analysis of adult chicken betal globin
cDNA.";
Nucleic Acids Res. 7:1137-1146(1979).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8307571; DOI=10.1016/S0888-7543(05)80364-7;
Reitman M., Grasso J.A., Blumenthal R., Lewit P.;
"Primary sequence, evolution, and repetitive elements of the Gallus
gallus (chicken) beta-globin cluster.";
Genomics 18:616-626(1993).
[4]
NUCLEOTIDE SEQUENCE, AND VARIANT SER-70.
Larrick J.W., Espinoza D.O.;
"Mutant hemoglobin (Beta chain thr 69-->ser) with high oxygen affinity
from Gallus gallus native to the altiplano of Peru.";
Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
PubMed=6263308; DOI=10.1021/bi00511a005;
Day L.E., Hirst A.J., Lai E.C., Mace M.J., Woo S.L.;
"5' domain and nucleotide sequence of an adult chicken chromosomal
beta-globin gene.";
Biochemistry 20:2091-2098(1981).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-44.
PubMed=6266925; DOI=10.1016/0378-1119(81)90021-4;
Padayatty J., Cummings I., Manske C.L., Higuchi R., Woo S., Salser W.;
"Cloning of chicken globin cDNA in bacterial plasmids.";
Gene 13:417-422(1981).
[7]
PROTEIN SEQUENCE OF 2-147.
PubMed=773926; DOI=10.1093/oxfordjournals.jbchem.a131029;
Maita T., Mizuno K., Matsuda G.;
"Peptic peptides from the beta polypeptide chain of AII component of
chicken hemoglobin.";
J. Biochem. 78:1311-1319(1975).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=10037733; DOI=10.1074/jbc.274.10.6411;
Knapp J.E., Oliveira M.A., Xie Q., Ernst S.R., Riggs A.F.,
Hackert M.L.;
"The structural and functional analysis of the hemoglobin D component
from chicken.";
J. Biol. Chem. 274:6411-6420(1999).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues. The beta chain is a component of adult
hemoglobin A and D.
-!- SUBUNIT: Heterotetramer of 2 alpha (or alpha-D) and 2 beta chains.
-!- TISSUE SPECIFICITY: Red blood cells.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-----------------------------------------------------------------------
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EMBL; V00409; CAA23700.1; -; Genomic_DNA.
EMBL; J00860; AAA48805.1; -; mRNA.
EMBL; L17432; AAD03347.1; -; Genomic_DNA.
EMBL; J00857; AAA48804.1; -; Genomic_DNA.
EMBL; M10380; AAA48803.1; -; mRNA.
EMBL; M73995; AAA48996.1; -; mRNA.
PIR; I50249; HBCH.
RefSeq; NP_990820.1; NM_205489.1.
RefSeq; XP_015156250.1; XM_015300764.1.
UniGene; Gga.4981; -.
PDB; 1HBR; X-ray; 2.30 A; B/D=2-147.
PDBsum; 1HBR; -.
ProteinModelPortal; P02112; -.
SMR; P02112; -.
BioGrid; 676732; 1.
IntAct; P02112; 1.
STRING; 9031.ENSGALP00000035593; -.
Allergome; 8240; Gal d HG.
PaxDb; P02112; -.
PRIDE; P02112; -.
Ensembl; ENSGALT00000036373; ENSGALP00000035593; ENSGALG00000028273.
Ensembl; ENSGALT00000055900; ENSGALP00000053742; ENSGALG00000028273.
Ensembl; ENSGALT00000071094; ENSGALP00000045986; ENSGALG00000035309.
Ensembl; ENSGALT00000076082; ENSGALP00000044628; ENSGALG00000035309.
GeneID; 396485; -.
KEGG; gga:107055600; -.
KEGG; gga:396485; -.
CTD; 396485; -.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
GeneTree; ENSGT00760000119197; -.
HOGENOM; HOG000036868; -.
HOVERGEN; HBG009709; -.
InParanoid; P02112; -.
OMA; FTPECQA; -.
OrthoDB; EOG091G0R7W; -.
PhylomeDB; P02112; -.
Reactome; R-GGA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-GGA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-GGA-2168880; Scavenging of heme from plasma.
Reactome; R-GGA-6798695; Neutrophil degranulation.
Reactome; R-GGA-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P02112; -.
PRO; PR:P02112; -.
Proteomes; UP000000539; Chromosome 1.
Bgee; ENSGALG00000028273; -.
ExpressionAtlas; P02112; baseline and differential.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0030492; F:hemoglobin binding; ISS:AgBase.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; ISS:AgBase.
GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
CDD; cd08925; Hb-beta_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like_sf.
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; Complete proteome; Direct protein sequencing; Heme;
Iron; Metal-binding; Oxygen transport; Polymorphism;
Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:773926}.
CHAIN 2 147 Hemoglobin subunit beta.
/FTId=PRO_0000052925.
METAL 64 64 Iron (heme distal ligand).
METAL 93 93 Iron (heme proximal ligand).
VARIANT 70 70 T -> S. {ECO:0000269|Ref.4}.
HELIX 6 16 {ECO:0000244|PDB:1HBR}.
HELIX 21 35 {ECO:0000244|PDB:1HBR}.
HELIX 37 46 {ECO:0000244|PDB:1HBR}.
HELIX 52 57 {ECO:0000244|PDB:1HBR}.
HELIX 59 76 {ECO:0000244|PDB:1HBR}.
HELIX 82 85 {ECO:0000244|PDB:1HBR}.
HELIX 87 94 {ECO:0000244|PDB:1HBR}.
TURN 95 97 {ECO:0000244|PDB:1HBR}.
HELIX 101 119 {ECO:0000244|PDB:1HBR}.
HELIX 120 122 {ECO:0000244|PDB:1HBR}.
HELIX 125 142 {ECO:0000244|PDB:1HBR}.
SEQUENCE 147 AA; 16466 MW; F5E6C77C6DE1E9F3 CRC64;
MVHWTAEEKQ LITGLWGKVN VAECGAEALA RLLIVYPWTQ RFFASFGNLS SPTAILGNPM
VRAHGKKVLT SFGDAVKNLD NIKNTFSQLS ELHCDKLHVD PENFRLLGDI LIIVLAAHFS
KDFTPECQAA WQKLVRVVAH ALARKYH


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