ID   HBBA_ANGAN              Reviewed;         147 AA.
AC   P80946;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Hemoglobin anodic subunit beta;
DE   AltName: Full=Hemoglobin anodic beta chain;
GN   Name=hbb1;
OS   Anguilla anguilla (European freshwater eel) (Muraena anguilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Anguillidae;
OC   Anguilla.
OX   NCBI_TaxID=7936;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Erythrocyte;
RX   PubMed=9188451; DOI=10.1074/jbc.272.25.15628;
RA   Fago A., Bendixen E., Malte H., Weber R.E.;
RT   "The anodic hemoglobin of Anguilla anguilla. Molecular basis for allosteric
RT   effects in a root-effect hemoglobin.";
RL   J. Biol. Chem. 272:15628-15635(1997).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: cathodic and anodic. The
CC       cathodic Hb and anodic Hb display small and large Bohr effects
CC       respectively. In addition, the cathodic Hb displays a reverse Bohr
CC       effect and appreciable phosphate effects.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P80946; -.
DR   SMR; P80946; -.
DR   PRIDE; P80946; -.
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..147
FT                   /note="Hemoglobin anodic subunit beta"
FT                   /id="PRO_0000052870"
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   147 AA;  16770 MW;  C447A8450208969F CRC64;
     VEWTEDERTA IKSKWLKINI EEIGPQAMRR LLIVCPWTQR HFANFGNLST AAAIMNNDKV
     AKHGTTVMGG LDRAIQNMDD IKNAYRQLSV MHSEKLHVDP DNFRLLAEHI TLCMAAKFGP
     TEFTADVQEA WQKFLMAVTS ALARQYH