ID   HBB_CHEKU               Reviewed;         146 AA.
AC   P80271;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=hbb;
OS   Chelidonichthys kumu (Bluefin gurnard) (Trigla kumu).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Triglioidei; Triglidae; Chelidonichthys.
OX   NCBI_TaxID=334942;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBUNIT.
RX   PubMed=8281934; DOI=10.1111/j.1432-1033.1993.tb18438.x;
RA   Fago A., Romano M., Tamburrini M., Coletta M., D'Avino R., di Prisco G.;
RT   "A polymerising Root-effect fish hemoglobin with high subunit
RT   heterogeneity. Correlation with primary structure.";
RL   Eur. J. Biochem. 218:829-835(1993).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:8281934}.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains. Can
CC       form polymers. {ECO:0000269|PubMed:8281934}.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: Displays a strong alkaline Bohr effect, and at low pH
CC       exhibits the reduced ligand affinity and cooperativity that comprise
CC       the Root effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S43023; S43023.
DR   AlphaFoldDB; P80271; -.
DR   SMR; P80271; -.
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; Disulfide bond; Heme; Iron; Metal-binding;
KW   Oxygen transport; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052924"
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   DISULFID        49
FT                   /note="Interchain (with another beta chain)"
SQ   SEQUENCE   146 AA;  16458 MW;  7E7250E4B779C128 CRC64;
     VEWTDFERAT IQDIFSKMDY ETVGPATLTR TVIVYPWTLR YFAKFGNICS TAAILGNKEI
     AKHGTTILHG LDRGVKNMDD IKNTYAELSK LHSEKLHVDP DNFRLLSDCL TIVVAAKMGK
     DFTGEVQAAF QKFLSVVVNS LGRQYH