ID   HBB2_ARCGL              Reviewed;         147 AA.
AC   P84604;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Hemoglobin subunit beta-2;
DE   AltName: Full=Beta-2-globin;
DE   AltName: Full=Hemoglobin beta-2 chain;
GN   Name=hbb2;
OS   Arctogadus glacialis (Arctic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Arctogadus.
OX   NCBI_TaxID=185735;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-147, FUNCTION, AND SUBUNIT.
RC   TISSUE=Blood {ECO:0000269|PubMed:16717098};
RX   PubMed=16717098; DOI=10.1074/jbc.m513080200;
RA   Verde C., Balestrieri M., de Pascale D., Pagnozzi D., Lecointre G.,
RA   di Prisco G.;
RT   "The oxygen transport system in three species of the boreal fish family
RT   Gadidae. Molecular phylogeny of hemoglobin.";
RL   J. Biol. Chem. 281:22073-22084(2006).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:16717098, ECO:0000305}.
CC   -!- SUBUNIT: Hb 3 is a heterotetramer of two alpha-2 and two beta-2 chains.
CC       {ECO:0000269|PubMed:16717098}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MISCELLANEOUS: Hb 3 displays a Bohr effect, which is enhanced by
CC       organophosphates, and a Root effect.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P84604; -.
DR   SMR; P84604; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:16717098"
FT   CHAIN           2..147
FT                   /note="Hemoglobin subunit beta-2"
FT                   /id="PRO_0000247581"
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: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:0000255|PROSITE-ProRule:PRU00238"
SQ   SEQUENCE   147 AA;  16548 MW;  3C604F9F830CBC33 CRC64;
     MVEWTDSERA IINDIFATLD YEEIGRKSLT RCLIVYPWTQ RYFGAFGNLY NAATIMANPL
     IAAHGTKILH GLDRALKNMD DIKNTYAELS LLHSDKLHVD PDNFRLLADC LTVVIAAKMG
     AAFTVDTQVA WQKFLSVVVS ALGRQYH