HBB_ANSAN
ID HBB_ANSAN Reviewed; 146 AA.
AC P02117;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Anser anser anser (Western greylag goose).
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=8844;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7346378;
RA Oberthur W., Braunitzer G., Kalas S.;
RT "Hemoglobins, XLII. Studies on the hemoglobin of the greylag goose (Anser
RT anser). The primary structures of the alpha- and beta-chains of the main
RT component.";
RL Hoppe-Seyler's Z. Physiol. Chem. 362:1101-1112(1981).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS).
RX PubMed=11717498; DOI=10.1107/s0907444901016493;
RA Liang Y.H., Liu X.Z., Liu S.H., Lu G.Y.;
RT "The structure of greylag goose oxy haemoglobin: the roles of four
RT mutations compared with bar-headed goose haemoglobin.";
RL Acta Crystallogr. D 57:1850-1856(2001).
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; A02437; HBGS.
DR PDB; 1FAW; X-ray; 3.09 A; B/D=1-146.
DR PDBsum; 1FAW; -.
DR AlphaFoldDB; P02117; -.
DR SMR; P02117; -.
DR EvolutionaryTrace; P02117; -.
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_0000052872"
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:1FAW"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1FAW"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:1FAW"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:1FAW"
SQ SEQUENCE 146 AA; 16305 MW; 473E9A70E561F123 CRC64;
VHWSAEEKQL ITGLWGKVNV ADCGAEALAR LLIVYPWTQR FFSSFGNLSS PTAILGNPMV
RAHGKKVLTS FGDAVKNLDN IKNTFAQLSE LHCDKLHVDP ENFRLLGDIL IIVLAAHFAK
EFTPECQAAW QKLVRVVAHA LARKYH
