HBB_COTGO
ID HBB_COTGO Reviewed; 147 AA.
AC P84652;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=hbb;
OS Cottoperca gobio (Frogmouth) (Aphritis gobio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Bovichtidae; Cottoperca.
OX NCBI_TaxID=56716;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-147, AND SUBUNIT.
RC TISSUE=Blood {ECO:0000269|Ref.1};
RA Giordano D., Grassi L., Parisi E., Bargelloni L., di Prisco G., Verde C.;
RT "Embryonic beta-globin in the non-Antartic notothenioid fish Cottoperca
RT gobio (Bovichtidae).";
RL Polar Biol. 30:75-82(2006).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-147, AND SUBUNIT.
RC TISSUE=Blood {ECO:0000269|PubMed:19292863};
RX PubMed=19292863; DOI=10.1111/j.1742-4658.2009.06954.x;
RA Giordano D., Boechi L., Vergara A., Marti M.A., Samuni U., Dantsker D.,
RA Grassi L., Estrin D.A., Friedman J.M., Mazzarella L., di Prisco G.,
RA Verde C.;
RT "The hemoglobins of the sub-Antarctic fish Cottoperca gobio, a phyletically
RT basal species--oxygen-binding equilibria, kinetics and molecular
RT dynamics.";
RL FEBS J. 276:2266-2277(2009).
CC -!- FUNCTION: Involved in oxygen transport from gills to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- SUBUNIT: Hb 1 is a heterotetramer of two alpha-1 and two beta chains.
CC Hb 2 is a heterotetramer of two alpha-2 and two beta chains.
CC {ECO:0000269|PubMed:19292863, ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 and Hb2. They display
CC the Bohr and root effects. {ECO:0000269|PubMed:19292863}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR AlphaFoldDB; P84652; -.
DR SMR; P84652; -.
DR Proteomes; UP000504630; Genome assembly.
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 Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /evidence="ECO:0000269|PubMed:19292863"
FT /id="PRO_0000250612"
FT BINDING 64
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:P80044,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
FT BINDING 93
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:P80044,
FT ECO:0000255|PROSITE-ProRule:PRU00238"
SQ SEQUENCE 147 AA; 16377 MW; 195FA707691297BD CRC64;
MVEWTDFERA TIKDVFSKIE YEVVGPAALA RCLVVYPWTQ RYFGNFGNLY NAAAITGNPK
VAKHGITILH GLDKAVKNMD DIRNTYAELS VLHSEKLHVD PDNFKLLADC LTIVVAAQMG
KAFTGEIQAA FQKFLAVVVS SLGRQYH
