HBB_HORSE
ID HBB_HORSE Reviewed; 146 AA.
AC P02062;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7409745;
RA Matsuda G., Maita T., Braunitzer G., Schrank B.;
RT "Hemoglobins, XXXIII. Note on the sequence of the hemoglobins of the
RT horse.";
RL Hoppe-Seyler's Z. Physiol. Chem. 361:1107-1116(1980).
RN [2]
RP PROTEIN SEQUENCE OF 1-82 AND 117-146.
RX PubMed=4876811; DOI=10.1139/o68-125;
RA Smith D.B.;
RT "Amino acid sequences of some tryptic peptides from the beta-chain of horse
RT hemoglobin.";
RL Can. J. Biochem. 46:825-843(1968).
RN [3]
RP DETERMINATION OF AMIDES, AND PROTEIN SEQUENCE OF 52-54.
RX PubMed=5529282; DOI=10.1139/o70-180;
RA Smith D.B., Chung W.P.;
RT "Amide groups of some tryptic peptides from the beta-chain of horse
RT hemoglobin.";
RL Can. J. Biochem. 48:1160-1164(1970).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=5659617; DOI=10.1038/219029a0;
RA Perutz M.F., Miurhead H., Cox J.M., Goaman L.C., Mathews F.S.,
RA McGandy E.L., Webb L.E.;
RT "Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8-A
RT resolution: (1) X-ray analysis.";
RL Nature 219:29-32(1968).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=5659637; DOI=10.1038/219131a0;
RA Perutz M.F., Muirhead H., Cox J.M., Goaman L.C.;
RT "Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8 A
RT resolution: the atomic model.";
RL Nature 219:131-139(1968).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH HEME.
RX PubMed=561852; DOI=10.1016/0022-2836(77)90256-x;
RA Ladner R.C., Heidner E.J., Perutz M.F.;
RT "The structure of horse methaemoglobin at 2.0-A resolution.";
RL J. Mol. Biol. 114:385-414(1977).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The man behind the molecular
CC lung - Issue 21 of April 2002;
CC URL="https://web.expasy.org/spotlight/back_issues/021";
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DR PIR; B91688; HBHO.
DR PDB; 1G0B; X-ray; 1.90 A; B=1-146.
DR PDB; 1IBE; X-ray; 1.80 A; B=1-146.
DR PDB; 1IWH; X-ray; 1.55 A; B=1-146.
DR PDB; 1NS6; X-ray; 2.05 A; B=1-146.
DR PDB; 1NS9; X-ray; 1.60 A; B=1-146.
DR PDB; 1Y8H; X-ray; 3.10 A; B/D=1-146.
DR PDB; 1Y8I; X-ray; 2.60 A; B/D=1-146.
DR PDB; 1Y8K; X-ray; 2.30 A; B/D=1-146.
DR PDB; 2D5X; X-ray; 1.45 A; B=1-146.
DR PDB; 2DHB; X-ray; 2.80 A; B=1-146.
DR PDB; 2MHB; X-ray; 2.00 A; B=1-146.
DR PDB; 2ZLT; X-ray; 1.90 A; B=1-146.
DR PDB; 2ZLU; X-ray; 2.00 A; B=1-146.
DR PDB; 2ZLV; X-ray; 2.00 A; B=1-146.
DR PDB; 2ZLW; X-ray; 2.90 A; B/D=1-146.
DR PDB; 2ZLX; X-ray; 2.80 A; B/D=1-146.
DR PDB; 5C6E; Other; 1.70 A; B=1-146.
DR PDB; 6R2O; X-ray; 2.46 A; B/D=1-145.
DR PDB; 6SVA; X-ray; 1.92 A; B=1-146.
DR PDBsum; 1G0B; -.
DR PDBsum; 1IBE; -.
DR PDBsum; 1IWH; -.
DR PDBsum; 1NS6; -.
DR PDBsum; 1NS9; -.
DR PDBsum; 1Y8H; -.
DR PDBsum; 1Y8I; -.
DR PDBsum; 1Y8K; -.
DR PDBsum; 2D5X; -.
DR PDBsum; 2DHB; -.
DR PDBsum; 2MHB; -.
DR PDBsum; 2ZLT; -.
DR PDBsum; 2ZLU; -.
DR PDBsum; 2ZLV; -.
DR PDBsum; 2ZLW; -.
DR PDBsum; 2ZLX; -.
DR PDBsum; 5C6E; -.
DR PDBsum; 6R2O; -.
DR PDBsum; 6SVA; -.
DR AlphaFoldDB; P02062; -.
DR SMR; P02062; -.
DR MINT; P02062; -.
DR STRING; 9796.ENSECAP00000024476; -.
DR PaxDb; P02062; -.
DR PeptideAtlas; P02062; -.
DR PRIDE; P02062; -.
DR HOGENOM; CLU_003827_10_0_1; -.
DR InParanoid; P02062; -.
DR OMA; TPDAVMN; -.
DR EvolutionaryTrace; P02062; -.
DR Proteomes; UP000002281; Unplaced.
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..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052975"
FT BINDING 63
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 /evidence="ECO:0000250|UniProtKB:P80044"
FT BINDING 92
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 /evidence="ECO:0000269|PubMed:561852, ECO:0007744|PDB:1G0B,
FT ECO:0007744|PDB:1IBE, ECO:0007744|PDB:1IWH,
FT ECO:0007744|PDB:1NS6, ECO:0007744|PDB:1NS9,
FT ECO:0007744|PDB:1Y8H, ECO:0007744|PDB:1Y8I,
FT ECO:0007744|PDB:1Y8K, ECO:0007744|PDB:2D5X,
FT ECO:0007744|PDB:2DHB, ECO:0007744|PDB:2MHB,
FT ECO:0007744|PDB:2ZLT, ECO:0007744|PDB:2ZLU,
FT ECO:0007744|PDB:2ZLV, ECO:0007744|PDB:2ZLW,
FT ECO:0007744|PDB:2ZLX"
FT MOD_RES 1
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 82
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 93
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 76..80
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:2D5X"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:2D5X"
SQ SEQUENCE 146 AA; 16008 MW; 734664793DA642EE CRC64;
VQLSGEEKAA VLALWDKVNE EEVGGEALGR LLVVYPWTQR FFDSFGDLSN PGAVMGNPKV
KAHGKKVLHS FGEGVHHLDN LKGTFAALSE LHCDKLHVDP ENFRLLGNVL VVVLARHFGK
DFTPELQASY QKVVAGVANA LAHKYH
