HBB_MUSGR
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 03-AUG-2022, entry version 92.
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}.
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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; -; 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 SUPFAM; SSF46458; SSF46458; 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
