ID   HBBC_CONCO              Reviewed;         146 AA.
AC   P83478;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Hemoglobin cathodic subunit beta;
DE   AltName: Full=Hemoglobin cathodic beta chain;
OS   Conger conger (Conger eel) (Muraena conger).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Congridae; Conger.
OX   NCBI_TaxID=82655;
RN   [1]
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
RC   TISSUE=Erythrocyte;
RX   PubMed=12646043; DOI=10.1042/bj20021865;
RA   Pellegrini M., Giardina B., Verde C., Carratore V., Olianas A., Sollai L.,
RA   Sanna M.T., Castagnola M., Di Prisco G.;
RT   "Structural-functional characterization of the cathodic haemoglobin of the
RT   conger eel Conger conger: molecular modelling study of an additional
RT   phosphate-binding site.";
RL   Biochem. J. 372:679-686(2003).
CC   -!- FUNCTION: Involved in oxygen transport from the gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC       {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:12646043}.
CC   -!- MASS SPECTROMETRY: Mass=16020; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12646043};
CC   -!- MISCELLANEOUS: This fish has two types of hemoglobin: one cathodic Hb
CC       and two major anodic Hbs. The cathodic Hb displays a small normal Bohr
CC       effect and a reverse Bohr effect in the presence and absence of
CC       phosphate respectively. In addition, the cathodic HB displays a large
CC       phosphate effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P83478; -.
DR   SMR; P83478; -.
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 cathodic subunit beta"
FT                   /id="PRO_0000052934"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   146 AA;  16013 MW;  F6212EB6A2E23812 CRC64;
     VQWSSSERST ISTLWGKINV AEIGPQALAR VLIVYPWTQR YFGKFGDLSS VAAIVGNANG
     AKHGRTVLQA LGQAVNNMDN IKGTYAKLSQ KHSEELNVDP DNFRLLGDCL TVVLATKFGA
     EFPPEVQAVW QKFVAVVVSA LSRQYF