ID   HBBC_GYMUN              Reviewed;         146 AA.
AC   P84204;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Hemoglobin cathodic subunit beta;
DE   AltName: Full=Hemoglobin cathodic beta chain;
OS   Gymnothorax unicolor (Brown moray) (Muraenophis unicolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Anguilliformes; Muraenidae;
OC   Gymnothorax.
OX   NCBI_TaxID=296138;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Erythrocyte {ECO:0000269|PubMed:11454005};
RX   PubMed=11454005; DOI=10.1046/j.1432-1327.2001.02333.x;
RA   Tamburrini M., Verde C., Olianas A., Giardina B., Corda M., Sanna M.T.,
RA   Fais A., Deiana A.M., di Prisco G., Pellegrini M.;
RT   "The hemoglobin system of the brown moray Gymnothorax unicolor:
RT   structure/function relationships.";
RL   Eur. J. Biochem. 268:4104-4111(2001).
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       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: cathodic and anodic.
CC       Cathodic Hb has high oxygen affinity, low cooperativity and displays a
CC       small reverse Bohr effect. Anodic Hb has low oxygen affinity and
CC       cooperativity and displays a normal Bohr effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P84204; -.
DR   SMR; P84204; -.
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_0000052969"
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:0000250|UniProtKB:P02142,
FT                   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:0000250|UniProtKB:P02142,
FT                   ECO:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   146 AA;  16051 MW;  3A6069489EE1788D CRC64;
     VEWSSSERST ITSLWGKVIP AEIGPVAFAR VLIVYPWTQR YFGNFGDLSN IAAISGNAKV
     AAHGKVVLDG VDKAVKNLDN IKGAYTSLSL LHSEKLNVDP DNFKLLGDCL TIVLATKFGA
     EFTPKVQAVW QKFLIVLIHA LSRQYF