HBB_BOVIN
ID HBB_BOVIN Reviewed; 145 AA.
AC P02070;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
DE Contains:
DE RecName: Full=Spinorphin;
GN Name=HBB;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A).
RX PubMed=6322113; DOI=10.1093/nar/12.3.1641;
RA Schimenti J.C., Duncan C.H.;
RT "Ruminant globin gene structures suggest an evolutionary role for Alu-type
RT repeats.";
RL Nucleic Acids Res. 12:1641-1655(1984).
RN [2]
RP PROTEIN SEQUENCE (ALLELES A AND B).
RX PubMed=6048711; DOI=10.1016/0003-9861(67)90606-6;
RA Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Babin D.R.;
RT "A comparison of amino acid sequences in the beta-chains of adult bovine
RT hemoglobins A and B.";
RL Arch. Biochem. Biophys. 120:124-135(1967).
RN [3]
RP PROTEIN SEQUENCE OF 31-37, AND FUNCTION OF SPINORPHIN.
RX PubMed=8343155; DOI=10.1006/bbrc.1993.1880;
RA Nishimura K., Hazato T.;
RT "Isolation and identification of an endogenous inhibitor of enkephalin-
RT degrading enzymes from bovine spinal cord.";
RL Biochem. Biophys. Res. Commun. 194:713-719(1993).
RN [4]
RP PARTIAL PROTEIN SEQUENCE (ALLELES C-RHODESIA AND D-ZAMBIA).
RX PubMed=4561255; DOI=10.1016/0003-9861(72)90210-x;
RA Schroeder W.A., Shelton J.R., Shelton J.B., Apell G., Huisman T.H.J.,
RA Smith L.L., Carr W.R.;
RT "Amino acid sequences in the beta-chains of adult bovine hemoglobins C-
RT Rhodesia and D-Zambia.";
RL Arch. Biochem. Biophys. 152:222-232(1972).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8411160; DOI=10.1006/jmbi.1993.1530;
RA Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J.;
RT "A novel allosteric mechanism in haemoglobin. Structure of bovine
RT deoxyhaemoglobin, absence of specific chloride-binding sites and origin of
RT the chloride-linked Bohr effect in bovine and human haemoglobin.";
RL J. Mol. Biol. 233:536-545(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=11369847; DOI=10.1110/ps.48301;
RA Safo M.K., Abraham D.J.;
RT "The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1
RT A resolution and its relationship to the quaternary structures of other
RT hemoglobin crystal forms.";
RL Protein Sci. 10:1091-1099(2001).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000269|PubMed:8343155}.
CC -!- FUNCTION: [Spinorphin]: Functions as an endogenous inhibitor of
CC enkephalin-degrading enzymes such as DPP3, and may thereby play a role
CC as a regulator of pain and inflammation. {ECO:0000269|PubMed:8343155}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: Four allelic beta chains have been found in bovine
CC hemoglobins. A and B alleles were found in Jersey cattle and C and D
CC alleles were found in Angoni cattle (East African short-horn zebu). The
CC sequence shown is that of the allele A. {ECO:0000269|PubMed:4561255,
CC ECO:0000269|PubMed:6048711, ECO:0000269|PubMed:6322113}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/HB/";
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DR EMBL; X00376; CAA25111.1; -; Genomic_DNA.
DR EMBL; M63453; AAA30408.1; -; Genomic_DNA.
DR PIR; B93504; HBBOB.
DR RefSeq; NP_776342.1; NM_173917.2.
DR PDB; 1FSX; X-ray; 2.10 A; B/D=1-145.
DR PDB; 1G08; X-ray; 1.90 A; B/D=1-145.
DR PDB; 1G09; X-ray; 2.04 A; B/D=1-145.
DR PDB; 1G0A; X-ray; 2.04 A; B/D=1-145.
DR PDB; 1HDA; X-ray; 2.20 A; B/D=1-145.
DR PDB; 2QSP; X-ray; 1.85 A; B/D=1-145.
DR PDB; 2QSS; X-ray; 1.75 A; B/D=1-145.
DR PDB; 3CIU; X-ray; 3.50 A; B/D=1-145.
DR PDB; 3PI8; X-ray; 2.20 A; B/D=1-145.
DR PDB; 3PI9; X-ray; 2.90 A; B/D=1-145.
DR PDB; 3PIA; X-ray; 2.10 A; B/D=1-145.
DR PDB; 6IHX; X-ray; 1.46 A; B/D=1-144.
DR PDB; 6II1; X-ray; 1.34 A; B/D=1-145.
DR PDBsum; 1FSX; -.
DR PDBsum; 1G08; -.
DR PDBsum; 1G09; -.
DR PDBsum; 1G0A; -.
DR PDBsum; 1HDA; -.
DR PDBsum; 2QSP; -.
DR PDBsum; 2QSS; -.
DR PDBsum; 3CIU; -.
DR PDBsum; 3PI8; -.
DR PDBsum; 3PI9; -.
DR PDBsum; 3PIA; -.
DR PDBsum; 6IHX; -.
DR PDBsum; 6II1; -.
DR AlphaFoldDB; P02070; -.
DR SMR; P02070; -.
DR STRING; 9913.ENSBTAP00000050256; -.
DR Allergome; 8242; Bos d HG.
DR PaxDb; P02070; -.
DR PeptideAtlas; P02070; -.
DR PRIDE; P02070; -.
DR Ensembl; ENSBTAT00000057323; ENSBTAP00000050256; ENSBTAG00000037644.
DR GeneID; 280813; -.
DR KEGG; bta:280813; -.
DR CTD; 3043; -.
DR VEuPathDB; HostDB:ENSBTAG00000037644; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000156216; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P02070; -.
DR OMA; PKALCRC; -.
DR OrthoDB; 1370439at2759; -.
DR TreeFam; TF333268; -.
DR Reactome; R-BTA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-BTA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-BTA-2168880; Scavenging of heme from plasma.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-BTA-9707616; Heme signaling.
DR EvolutionaryTrace; P02070; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000037644; Expressed in thymus and 93 other tissues.
DR ExpressionAtlas; P02070; baseline and differential.
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:0031721; F:hemoglobin alpha binding; IBA:GO_Central.
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; IBA:GO_Central.
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; Acetylation; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Transport.
FT CHAIN 1..145
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052892"
FT PEPTIDE 31..37
FT /note="Spinorphin"
FT /id="PRO_0000424225"
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 MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 92
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT VARIANT 15
FT /note="G -> S (in allele B)"
FT /evidence="ECO:0000269|PubMed:6048711"
FT VARIANT 18
FT /note="K -> H (in allele B)"
FT /evidence="ECO:0000269|PubMed:6048711"
FT VARIANT 20
FT /note="D -> G (in allele D-Zambia)"
FT /evidence="ECO:0000269|PubMed:4561255"
FT VARIANT 43
FT /note="S -> T (in allele D-Zambia)"
FT /evidence="ECO:0000269|PubMed:4561255"
FT VARIANT 119
FT /note="K -> N (in allele B)"
FT VARIANT 131
FT /note="K -> Q (in allele C-Rhodesia)"
FT /evidence="ECO:0000269|PubMed:4561255"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2QSS"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:6II1"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6II1"
SQ SEQUENCE 145 AA; 15954 MW; FD62217E8477CFD4 CRC64;
MLTAEEKAAV TAFWGKVKVD EVGGEALGRL LVVYPWTQRF FESFGDLSTA DAVMNNPKVK
AHGKKVLDSF SNGMKHLDDL KGTFAALSEL HCDKLHVDPE NFKLLGNVLV VVLARNFGKE
FTPVLQADFQ KVVAGVANAL AHRYH
