ID HBB_MUSGR Reviewed; 137 AA. AC Q9YGW1; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 22-FEB-2023, entry version 94. DE RecName: Full=Hemoglobin subunit beta; DE AltName: Full=Beta-globin; DE AltName: Full=Hemoglobin beta chain; GN Name=HBB; OS Mustelus griseus (Spotless smooth hound). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Triakidae; OC Mustelus. OX NCBI_TaxID=89020; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Miyazaki G., Yoshimatu K., Kawasaki Y., Suzuki T.; RT "Hemoglobin beta chain of spotless smooth hound (Mustelus griseus)."; RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-137 IN COMPLEX WITH HEME, AND RP METAL BINDING AT HIS-54 AND HIS-83. RX PubMed=11243818; DOI=10.1006/jmbi.2000.4446; RA Naoi Y., Chong K.T., Yoshimatsu K., Miyazaki G., Tame J.R., Park S.Y., RA Adachi S., Morimoto H.; RT "The functional similarity and structural diversity of human and RT cartilaginous fish hemoglobins."; RL J. Mol. Biol. 307:259-270(2001). CC -!- FUNCTION: Involved in oxygen transport from gills 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 --------------------------------------------------------------------------- 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 EMBL; AB023801; BAA75400.1; -; mRNA. DR PDB; 1GCV; X-ray; 2.00 A; B/D=2-137. DR PDB; 1GCW; X-ray; 2.00 A; B/D=2-136. DR PDBsum; 1GCV; -. DR PDBsum; 1GCW; -. DR AlphaFoldDB; Q9YGW1; -. DR SMR; Q9YGW1; -. DR EvolutionaryTrace; Q9YGW1; -. DR GO; GO:0005833; C:hemoglobin complex; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW. 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:SF7; HEMOGLOBIN SUBUNIT EPSILON; 1. DR Pfam; PF00042; Globin; 1. DR SUPFAM; SSF46458; Globin-like; 1. DR PROSITE; PS01033; GLOBIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Heme; Iron; Metal-binding; Oxygen transport; Transport. FT CHAIN 1..137 FT /note="Hemoglobin subunit beta" FT /id="PRO_0000053028" FT BINDING 54 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:0000269|PubMed:11243818" FT BINDING 83 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:11243818, FT ECO:0007744|PDB:1GCV, ECO:0007744|PDB:1GCW" FT HELIX 6..18 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 21..35 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 37..42 FT /evidence="ECO:0007829|PDB:1GCV" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 51..67 FT /evidence="ECO:0007829|PDB:1GCV" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 77..85 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 91..93 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 94..109 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:1GCV" FT HELIX 115..133 FT /evidence="ECO:0007829|PDB:1GCV" SQ SEQUENCE 137 AA; 16074 MW; 08F2165693645D98 CRC64; MVHWTQEERD EISKTFQGTD MKTVVTQALD RMFKVYPWTN RYFQKRTDFR SSIHAGIVVG ALQDAVKHMD DVKTLFKDLS KKHADDLHVD PGSFHLLTDC IIVELAYLRK DCFTPHIQGI WDKFFEVVID AISKQYH //