ID   HBB_GYPRU               Reviewed;         146 AA.
AC   P68063; P07418;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Gyps rueppelli (Rueppell's griffon) (Vultur rueppellii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC   Accipitrinae; Gyps.
OX   NCBI_TaxID=8967;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3401327; DOI=10.1515/bchm3.1988.369.1.217;
RA   Hiebl I., Weber R.E., Schneeganss D., Kosters J., Braunitzer G.;
RT   "High-altitude respiration of birds. Structural adaptations in the major
RT   and minor hemoglobin components of adult Ruppell's Griffon (Gyps
RT   rueppellii, Aegypiinae): a new molecular pattern for hypoxic tolerance.";
RL   Biol. Chem. Hoppe-Seyler 369:217-232(1988).
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; S00539; HBGRR.
DR   AlphaFoldDB; P68063; -.
DR   SMR; P68063; -.
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   Direct protein sequencing; Heme; Iron; Metal-binding; Oxygen transport;
KW   Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052970"
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"
SQ   SEQUENCE   146 AA;  16233 MW;  A3244A77B9E616C1 CRC64;
     VHWTAEEKQL ITGLWGKVNV ADCGAEALAR LLIVYPWTQR FFASFGNLSS PTAIIGNPMV
     RAHGKKVLTS FGEAVKNLDN IKNTFAQLSE LHCDKLHVDP ENFRLLGDIL IIVLAAHFGK
     DFSPDCQAAW QKLVRAVAHA LARKYH