HBB_HEMAK
ID HBB_HEMAK Reviewed; 142 AA.
AC P56692;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Hemitrygon akajei (Red stingray) (Dasyatis akajei).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Myliobatiformes; Dasyatidae; Hemitrygon.
OX NCBI_TaxID=2704970;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF
RP 2-142 IN COMPLEX WITH HEME.
RC TISSUE=Blood;
RX PubMed=10393295; DOI=10.1107/s0907444999005934;
RA Chong K.T., Miyazaki G., Morimoto H., Oda Y., Park S.-Y.;
RT "Structures of the deoxy and CO forms of haemoglobin from Dasyatis akajei,
RT a cartilaginous fish.";
RL Acta Crystallogr. D 55:1291-1300(1999).
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; AB023723; BAA75250.1; -; mRNA.
DR PDB; 1CG5; X-ray; 1.60 A; B=2-142.
DR PDB; 1CG8; X-ray; 1.90 A; B=2-142.
DR PDBsum; 1CG5; -.
DR PDBsum; 1CG8; -.
DR AlphaFoldDB; P56692; -.
DR SMR; P56692; -.
DR MINT; P56692; -.
DR EvolutionaryTrace; P56692; -.
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 INIT_MET 1
FT /note="Removed"
FT CHAIN 2..142
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052944"
FT BINDING 60
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 89
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:10393295,
FT ECO:0007744|PDB:1CG5, ECO:0007744|PDB:1CG8"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 55..73
FT /evidence="ECO:0007829|PDB:1CG5"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 97..114
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1CG5"
FT HELIX 120..138
FT /evidence="ECO:0007829|PDB:1CG5"
SQ SEQUENCE 142 AA; 16420 MW; FBDD4F2939155A14 CRC64;
MVKLSEDQEH YIKGVWKDVD HKQITAKALE RVFVVYPWTT RLFSKLQGLF SANDIGVQQH
ADKVQRALGE AIDDLKKVEI NFQNLSGKHQ EIGVDTQNFK LLGQTFMVEL ALHYKKTFRP
KEHAAAYKFF RLVAEALSSN YH
