HBBC_ANGAN
ID HBBC_ANGAN Reviewed; 146 AA.
AC P80727;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Hemoglobin cathodic subunit beta;
DE AltName: Full=Hemoglobin cathodic beta chain;
GN Name=hbb2;
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=7642546; DOI=10.1074/jbc.270.32.18897;
RA Fago A., Carratore V., di Prisco G., Feuerlein R.J., Sottrup-Jensen L.,
RA Weber R.E.;
RT "The cathodic hemoglobin of Anguilla anguilla. Amino acid sequence and
RT oxygen equilibria of a reverse Bohr effect hemoglobin with high oxygen
RT affinity and high phosphate sensitivity.";
RL J. Biol. Chem. 270:18897-18902(1995).
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}.
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; P80727; -.
DR SMR; P80727; -.
DR OMA; SQLHCEK; -.
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_0000052871"
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 146 AA; 15892 MW; 3C9DF56756252C58 CRC64;
VEWSASERST ITSLWGKINV AEIGPQALAR VLIVYPWTQR YFGKFGDLSN AAAIQGNAKV
AAHGKVVLGA LEKAVKNMDD VKGTYSKLSQ LHNEKLNVDP DNFRLLGDCL TIVLATKLGA
GFPAEIQAVW QKFVAVVVSA LSKQYF