ID   HBB2_GOBGI              Reviewed;         146 AA.
AC   P83614;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Hemoglobin subunit beta-2;
DE   AltName: Full=Beta-2-globin;
DE   AltName: Full=Hemoglobin beta-2 chain;
GN   Name=hbb2;
OS   Gobionotothen gibberifrons (Humped rockcod) (Notothenia gibberifrons).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Notothenioidei; Nototheniidae; Gobionotothen.
OX   NCBI_TaxID=36202 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBUNIT, AND MASS SPECTROMETRY.
RC   TISSUE=Blood {ECO:0000269|PubMed:14511380};
RX   PubMed=14511380; DOI=10.1046/j.1432-1033.2003.03786.x;
RA   Marinakis P., Tamburrini M., Carratore V., di Prisco G.;
RT   "Unique features of the hemoglobin system of the Antarctic fish
RT   Gobionotothen gibberifrons.";
RL   Eur. J. Biochem. 270:3981-3987(2003).
CC   -!- FUNCTION: Involved in oxygen transport from gills to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Hb 2 is a heterotetramer of two alpha-2 and two beta-2 chains.
CC       {ECO:0000269|PubMed:14511380}.
CC   -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=16420; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:14511380};
CC   -!- MISCELLANEOUS: This fish has two hemoglobins: Hb1 (major) and Hb2
CC       (about 15-20% of the total). They display the Root effect and the
CC       alkaline Bohr effect, which is enhanced by organophosphate and to a
CC       lesser extent by chloride.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238, ECO:0000305}.
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DR   AlphaFoldDB; P83614; -.
DR   SMR; P83614; -.
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_0000052965"
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;  16399 MW;  BF3D48C6AC87BBE2 CRC64;
     VEWTDFERAT INDIFSKLEY EVVGPATLAR CLVVYPWTQR YFGNFGNLYN AAAIAENPMV
     SKHGITILHG LDRAVKNMDD IKNTYAELSV LHSEKLHVDP DNFQLLADCL TIVVAARFGN
     TFTGEVQAAF QKFLSVVVSS LGRQYH