HBB_CHICK
ID HBB_CHICK Reviewed; 147 AA.
AC P02112; Q90594; Q90863; Q90938;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6833240; DOI=10.1016/s0021-9258(18)32764-9;
RA Dolan M., Dodgson J.B., Engel J.D.;
RT "Analysis of the adult chicken beta-globin gene. Nucleotide sequence of the
RT locus, microheterogeneity at the 5'-end of beta-globin mRNA, and aberrant
RT nuclear RNA species.";
RL J. Biol. Chem. 258:3983-3990(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=514809; DOI=10.1093/nar/7.5.1137;
RA Richards R.I., Shine J., Ullrich A., Wells J.R.E., Goodman H.M.;
RT "Molecular cloning and sequence analysis of adult chicken betal globin
RT cDNA.";
RL Nucleic Acids Res. 7:1137-1146(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8307571; DOI=10.1016/s0888-7543(05)80364-7;
RA Reitman M., Grasso J.A., Blumenthal R., Lewit P.;
RT "Primary sequence, evolution, and repetitive elements of the Gallus gallus
RT (chicken) beta-globin cluster.";
RL Genomics 18:616-626(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE, AND VARIANT SER-70.
RA Larrick J.W., Espinoza D.O.;
RT "Mutant hemoglobin (Beta chain thr 69-->ser) with high oxygen affinity from
RT Gallus gallus native to the altiplano of Peru.";
RL Submitted (JAN-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RX PubMed=6263308; DOI=10.1021/bi00511a005;
RA Day L.E., Hirst A.J., Lai E.C., Mace M.J., Woo S.L.;
RT "5' domain and nucleotide sequence of an adult chicken chromosomal beta-
RT globin gene.";
RL Biochemistry 20:2091-2098(1981).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-44.
RX PubMed=6266925; DOI=10.1016/0378-1119(81)90021-4;
RA Padayatty J., Cummings I., Manske C.L., Higuchi R., Woo S., Salser W.;
RT "Cloning of chicken globin cDNA in bacterial plasmids.";
RL Gene 13:417-422(1981).
RN [7]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=773926; DOI=10.1093/oxfordjournals.jbchem.a131029;
RA Maita T., Mizuno K., Matsuda G.;
RT "Peptic peptides from the beta polypeptide chain of AII component of
RT chicken hemoglobin.";
RL J. Biochem. 78:1311-1319(1975).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10037733; DOI=10.1074/jbc.274.10.6411;
RA Knapp J.E., Oliveira M.A., Xie Q., Ernst S.R., Riggs A.F., Hackert M.L.;
RT "The structural and functional analysis of the hemoglobin D component from
RT chicken.";
RL J. Biol. Chem. 274:6411-6420(1999).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. The beta chain is a component of adult hemoglobin A
CC and D.
CC -!- SUBUNIT: Heterotetramer of 2 alpha (or alpha-D) and 2 beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; V00409; CAA23700.1; -; Genomic_DNA.
DR EMBL; J00860; AAA48805.1; -; mRNA.
DR EMBL; L17432; AAD03347.1; -; Genomic_DNA.
DR EMBL; J00857; AAA48804.1; -; Genomic_DNA.
DR EMBL; M10380; AAA48803.1; -; mRNA.
DR EMBL; M73995; AAA48996.1; -; mRNA.
DR PIR; I50249; HBCH.
DR RefSeq; NP_990820.1; NM_205489.1.
DR RefSeq; XP_015156250.1; XM_015300764.1.
DR PDB; 1HBR; X-ray; 2.30 A; B/D=2-147.
DR PDBsum; 1HBR; -.
DR AlphaFoldDB; P02112; -.
DR SMR; P02112; -.
DR BioGRID; 676732; 1.
DR IntAct; P02112; 1.
DR STRING; 9031.ENSGALP00000035593; -.
DR Allergome; 8240; Gal d HG.
DR PaxDb; P02112; -.
DR Ensembl; ENSGALT00000036373; ENSGALP00000035593; ENSGALG00000047152.
DR GeneID; 396485; -.
DR KEGG; gga:396485; -.
DR CTD; 396485; -.
DR VEuPathDB; HostDB:geneid_396485; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000157809; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P02112; -.
DR OMA; INGLWSK; -.
DR OrthoDB; 1370439at2759; -.
DR PhylomeDB; P02112; -.
DR Reactome; R-GGA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-GGA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-GGA-2168880; Scavenging of heme from plasma.
DR Reactome; R-GGA-6798695; Neutrophil degranulation.
DR Reactome; R-GGA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-GGA-9707616; Heme signaling.
DR EvolutionaryTrace; P02112; -.
DR PRO; PR:P02112; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000047152; Expressed in lung and 12 other tissues.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0030492; F:hemoglobin binding; ISS:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; ISS:AgBase.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:773926"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052925"
FT BINDING 64
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 93
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 70
FT /note="T -> S"
FT /evidence="ECO:0000269|Ref.4"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 59..76
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 87..94
FT /evidence="ECO:0007829|PDB:1HBR"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 101..119
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1HBR"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:1HBR"
SQ SEQUENCE 147 AA; 16466 MW; F5E6C77C6DE1E9F3 CRC64;
MVHWTAEEKQ LITGLWGKVN VAECGAEALA RLLIVYPWTQ RFFASFGNLS SPTAILGNPM
VRAHGKKVLT SFGDAVKNLD NIKNTFSQLS ELHCDKLHVD PENFRLLGDI LIIVLAAHFS
KDFTPECQAA WQKLVRVVAH ALARKYH
