HBB_ANSIN
ID HBB_ANSIN Reviewed; 146 AA.
AC P02118;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Anser indicus (Bar-headed goose) (Anas indica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anserinae; Anser.
OX NCBI_TaxID=8846;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7106705;
RA Oberthur W., Braunitzer G., Wurdinger I.;
RT "Hemoglobins, XLVII. Hemoglobins of the bar-headed goose (Anser indicus):
RT primary structure and physiology of respiration, systematic and
RT evolution.";
RL Hoppe-Seyler's Z. Physiol. Chem. 363:581-590(1982).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8568892; DOI=10.1006/jmbi.1996.0040;
RA Zhang J., Hua Z., Tame J.R.H., Lu G., Zhang R., Gu X.;
RT "The crystal structure of a high oxygen affinity species of haemoglobin
RT (bar-headed goose haemoglobin in the oxy form).";
RL J. Mol. Biol. 255:484-493(1996).
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}.
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DR PIR; A02438; HBGSI.
DR PDB; 1A4F; X-ray; 2.00 A; B=1-146.
DR PDB; 1C40; X-ray; 2.30 A; B=1-146.
DR PDB; 1HV4; X-ray; 2.80 A; B/D/F/H=1-146.
DR PDBsum; 1A4F; -.
DR PDBsum; 1C40; -.
DR PDBsum; 1HV4; -.
DR AlphaFoldDB; P02118; -.
DR SMR; P02118; -.
DR MINT; P02118; -.
DR EvolutionaryTrace; P02118; -.
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 PRINTS; PR00814; BETAHAEM.
DR SUPFAM; SSF46458; SSF46458; 1.
DR PROSITE; PS01033; GLOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW Oxygen transport; Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052873"
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 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 HELIX 5..15
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:1A4F"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1A4F"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:1A4F"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1HV4"
SQ SEQUENCE 146 AA; 16291 MW; 473E9A70E5602A53 CRC64;
VHWSAEEKQL ITGLWGKVNV ADCGAEALAR LLIVYPWTQR FFSSFGNLSS PTAILGNPMV
RAHGKKVLTS FGDAVKNLDN IKNTFAQLSE LHCDKLHVDP ENFRLLGDIL IIVLAAHFAK
EFTPDCQAAW QKLVRVVAHA LARKYH