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Hemoglobin subunit beta (Beta-globin) (Hemoglobin beta chain) [Cleaved into: Spinorphin]

 HBB_BOVIN               Reviewed;         145 AA.
P02070;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
22-NOV-2017, entry version 148.
RecName: Full=Hemoglobin subunit beta;
AltName: Full=Beta-globin;
AltName: Full=Hemoglobin beta chain;
Contains:
RecName: Full=Spinorphin;
Name=HBB;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE A).
PubMed=6322113; DOI=10.1093/nar/12.3.1641;
Schimenti J.C., Duncan C.H.;
"Ruminant globin gene structures suggest an evolutionary role for Alu-
type repeats.";
Nucleic Acids Res. 12:1641-1655(1984).
[2]
PROTEIN SEQUENCE (ALLELES A AND B).
PubMed=6048711; DOI=10.1016/0003-9861(67)90606-6;
Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Babin D.R.;
"A comparison of amino acid sequences in the beta-chains of adult
bovine hemoglobins A and B.";
Arch. Biochem. Biophys. 120:124-135(1967).
[3]
PROTEIN SEQUENCE OF 31-37, AND FUNCTION OF SPINORPHIN.
PubMed=8343155; DOI=10.1006/bbrc.1993.1880;
Nishimura K., Hazato T.;
"Isolation and identification of an endogenous inhibitor of
enkephalin-degrading enzymes from bovine spinal cord.";
Biochem. Biophys. Res. Commun. 194:713-719(1993).
[4]
PARTIAL PROTEIN SEQUENCE (ALLELES C-RHODESIA AND D-ZAMBIA).
PubMed=4561255; DOI=10.1016/0003-9861(72)90210-X;
Schroeder W.A., Shelton J.R., Shelton J.B., Apell G., Huisman T.H.J.,
Smith L.L., Carr W.R.;
"Amino acid sequences in the beta-chains of adult bovine hemoglobins
C-Rhodesia and D-Zambia.";
Arch. Biochem. Biophys. 152:222-232(1972).
[5]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=8411160; DOI=10.1006/jmbi.1993.1530;
Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J.;
"A novel allosteric mechanism in haemoglobin. Structure of bovine
deoxyhaemoglobin, absence of specific chloride-binding sites and
origin of the chloride-linked Bohr effect in bovine and human
haemoglobin.";
J. Mol. Biol. 233:536-545(1993).
[6]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=11369847; DOI=10.1110/ps.48301;
Safo M.K., Abraham D.J.;
"The X-ray structure determination of bovine carbonmonoxy hemoglobin
at 2.1 A resoultion and its relationship to the quaternary structures
of other hemoglobin crystal froms.";
Protein Sci. 10:1091-1099(2001).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues. {ECO:0000269|PubMed:8343155}.
-!- FUNCTION: Spinorphin: functions as an endogenous inhibitor of
enkephalin-degrading enzymes such as DPP3, and may thereby play a
role as a regulator of pain and inflammation.
{ECO:0000269|PubMed:8343155}.
-!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
-!- TISSUE SPECIFICITY: Red blood cells.
-!- POLYMORPHISM: Four allelic beta chains have been found in bovine
hemoglobins. A and B alleles were found in Jersey cattle and C and
D alleles were found in Angoni cattle (East African short-horn
zebu). The sequence shown is that of the allele A.
{ECO:0000269|PubMed:4561255, ECO:0000269|PubMed:6048711,
ECO:0000269|PubMed:6322113}.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/HB/";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X00376; CAA25111.1; -; Genomic_DNA.
EMBL; M63453; AAA30408.1; -; Genomic_DNA.
PIR; B93504; HBBOB.
RefSeq; NP_776342.1; NM_173917.2.
UniGene; Bt.23726; -.
PDB; 1FSX; X-ray; 2.10 A; B/D=1-145.
PDB; 1G08; X-ray; 1.90 A; B/D=1-145.
PDB; 1G09; X-ray; 2.04 A; B/D=1-145.
PDB; 1G0A; X-ray; 2.04 A; B/D=1-145.
PDB; 1HDA; X-ray; 2.20 A; B/D=1-145.
PDB; 2QSP; X-ray; 1.85 A; B/D=1-145.
PDB; 2QSS; X-ray; 1.75 A; B/D=1-145.
PDB; 3CIU; X-ray; 3.50 A; B/D=1-145.
PDB; 3PI8; X-ray; 2.20 A; B/D=1-145.
PDB; 3PI9; X-ray; 2.90 A; B/D=1-145.
PDB; 3PIA; X-ray; 2.10 A; B/D=1-145.
PDBsum; 1FSX; -.
PDBsum; 1G08; -.
PDBsum; 1G09; -.
PDBsum; 1G0A; -.
PDBsum; 1HDA; -.
PDBsum; 2QSP; -.
PDBsum; 2QSS; -.
PDBsum; 3CIU; -.
PDBsum; 3PI8; -.
PDBsum; 3PI9; -.
PDBsum; 3PIA; -.
ProteinModelPortal; P02070; -.
SMR; P02070; -.
STRING; 9913.ENSBTAP00000043063; -.
Allergome; 8242; Bos d HG.
PaxDb; P02070; -.
PeptideAtlas; P02070; -.
PRIDE; P02070; -.
Ensembl; ENSBTAT00000045694; ENSBTAP00000043063; ENSBTAG00000038748.
GeneID; 280813; -.
KEGG; bta:280813; -.
CTD; 3043; -.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
GeneTree; ENSGT00760000119197; -.
HOGENOM; HOG000036868; -.
HOVERGEN; HBG009709; -.
InParanoid; P02070; -.
KO; K13823; -.
OMA; WTRRFFE; -.
OrthoDB; EOG091G0R7W; -.
TreeFam; TF333268; -.
Reactome; R-BTA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-BTA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-BTA-2168880; Scavenging of heme from plasma.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-983231; Factors involved in megakaryocyte development and platelet production.
EvolutionaryTrace; P02070; -.
PMAP-CutDB; P02070; -.
Proteomes; UP000009136; Chromosome 15.
Bgee; ENSBTAG00000038748; -.
ExpressionAtlas; P02070; baseline and differential.
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 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; Acetylation; Complete proteome;
Direct protein sequencing; Heme; Iron; Metal-binding;
Oxygen transport; Phosphoprotein; Polymorphism; Reference proteome;
S-nitrosylation; Transport.
CHAIN 1 145 Hemoglobin subunit beta.
/FTId=PRO_0000052892.
PEPTIDE 31 37 Spinorphin.
/FTId=PRO_0000424225.
METAL 62 62 Iron (heme distal ligand).
METAL 91 91 Iron (heme proximal ligand).
MOD_RES 11 11 Phosphothreonine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 58 58 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 81 81 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68871}.
MOD_RES 92 92 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P68871}.
VARIANT 15 15 G -> S (in allele B).
{ECO:0000269|PubMed:6048711}.
VARIANT 18 18 K -> H (in allele B).
{ECO:0000269|PubMed:6048711}.
VARIANT 20 20 D -> G (in allele D-Zambia).
{ECO:0000269|PubMed:4561255}.
VARIANT 43 43 S -> T (in allele D-Zambia).
{ECO:0000269|PubMed:4561255}.
VARIANT 119 119 K -> N (in allele B).
VARIANT 131 131 K -> Q (in allele C-Rhodesia).
{ECO:0000269|PubMed:4561255}.
HELIX 4 14 {ECO:0000244|PDB:2QSS}.
HELIX 21 33 {ECO:0000244|PDB:2QSS}.
HELIX 35 44 {ECO:0000244|PDB:2QSS}.
HELIX 50 55 {ECO:0000244|PDB:2QSS}.
HELIX 57 73 {ECO:0000244|PDB:2QSS}.
HELIX 77 79 {ECO:0000244|PDB:2QSS}.
HELIX 80 83 {ECO:0000244|PDB:2QSS}.
HELIX 85 93 {ECO:0000244|PDB:2QSS}.
HELIX 100 117 {ECO:0000244|PDB:2QSS}.
HELIX 118 120 {ECO:0000244|PDB:2QSS}.
HELIX 123 140 {ECO:0000244|PDB:2QSS}.
HELIX 141 144 {ECO:0000244|PDB:2QSS}.
SEQUENCE 145 AA; 15954 MW; FD62217E8477CFD4 CRC64;
MLTAEEKAAV TAFWGKVKVD EVGGEALGRL LVVYPWTQRF FESFGDLSTA DAVMNNPKVK
AHGKKVLDSF SNGMKHLDDL KGTFAALSEL HCDKLHVDPE NFKLLGNVLV VVLARNFGKE
FTPVLQADFQ KVVAGVANAL AHRYH


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