ID   HBB2_ANAMI              Reviewed;         146 AA.
AC   P83273;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Hemoglobin subunit beta-2;
DE   AltName: Full=Beta-2-globin;
DE   AltName: Full=Hemoglobin beta-2 chain;
GN   Name=hbb2;
OS   Anarhichas minor (Arctic spotted wolffish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Zoarcales; Anarhichadidae; Anarhichas.
OX   NCBI_TaxID=65739;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12118003; DOI=10.1074/jbc.m202474200;
RA   Verde C., Carratore V., Riccio A., Tamburrini M., Parisi E., Di Prisco G.;
RT   "The functionally distinct hemoglobins of the Arctic spotted wolffish
RT   Anarhichas minor.";
RL   J. Biol. Chem. 277:36312-36320(2002).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues. {ECO:0000269|PubMed:12118003}.
CC   -!- SUBUNIT: Hb3 is a heterotetramer of two alpha-2 chains and two beta-2
CC       chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000269|PubMed:12118003}.
CC   -!- MISCELLANEOUS: Hb3 displays pronounced Bohr and root effects,
CC       accompanied by strong organophosphate regulation.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   AlphaFoldDB; P83273; -.
DR   SMR; P83273; -.
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 subunit beta-2"
FT                   /id="PRO_0000052867"
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;  16289 MW;  139B6730B659B800 CRC64;
     VEWTDFERAT IQDIFSKMDY EVVGPAALSR CLIVYPWTQR YFGSFGNLYN AAAIMGNPNV
     AKHGTIILHG LDRGVKNMDN IKETYAELSV LHSEKLHVDP DNFKLISDCL TVVVAAQFGK
     AFTGEVQAAF QKFMAVVVSA LGRQYH