ID   HBB_CHRRI               Reviewed;         146 AA.
AC   P08261;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Hemoglobin subunit beta/beta';
DE   AltName: Full=Beta/beta'-globin;
DE   AltName: Full=Hemoglobin beta/beta' chain;
GN   Name=HBB;
OS   Chroicocephalus ridibundus (Black-headed gull) (Larus ridibundus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Charadriiformes; Laridae; Chroicocephalus.
OX   NCBI_TaxID=1192867;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3166738; DOI=10.1515/bchm3.1988.369.1.341;
RA   Godovac-Zimmermann J., Kosters J., Braunitzer G., Goltenboth R.;
RT   "Structural adaptation of bird hemoglobins to high-altitude respiration and
RT   the primary sequences of black-headed gull (Larus ridibundus,
RT   Charadriiformes) alpha A- and beta/beta'-chains.";
RL   Biol. Chem. Hoppe-Seyler 369:341-348(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   -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC       beta. {ECO:0000269|PubMed:3166738}.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S00815; HBGLB.
DR   AlphaFoldDB; P08261; -.
DR   SMR; P08261; -.
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/beta'"
FT                   /id="PRO_0000052984"
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   VARIANT         78
FT                   /note="L -> I (in beta')"
FT                   /evidence="ECO:0000269|PubMed:3166738"
SQ   SEQUENCE   146 AA;  16260 MW;  D50618FDB6303568 CRC64;
     VHWSAEEKQL ITGLWGKVNV ADCGAEALAR LLIVYPWTQR FFASFGNLSS PTAINGNPMV
     RAHGKKVLTS FGEAVKNLDN IKNTFAQLSE LHCDKLHVDP ENFRLLGDIL IIVLAAHFAK
     DFTPDSQAAW QKLVRVVAHA LARKYH