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 27-MAR-2024, entry version 164. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8PUQ; X-ray; 1.95 A; B=1-146. DR PDB; 8PUR; X-ray; 1.85 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 PDBsum; 8PUQ; -. DR PDBsum; 8PUR; -. DR AlphaFoldDB; P02062; -. DR SMR; P02062; -. DR MINT; P02062; -. DR STRING; 9796.ENSECAP00000024476; -. DR PaxDb; 9796-ENSECAP00000024476; -. DR PeptideAtlas; P02062; -. DR HOGENOM; CLU_003827_10_0_1; -. DR InParanoid; P02062; -. 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; Globins; 1. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin-like_sf. DR InterPro; IPR012292; Globin/Proto. DR InterPro; IPR002337; Hemoglobin_b. DR PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1. DR PANTHER; PTHR11442:SF42; HEMOGLOBIN SUBUNIT BETA; 1. DR Pfam; PF00042; Globin; 1. DR PRINTS; PR00814; BETAHAEM. DR SUPFAM; SSF46458; Globin-like; 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 //