ID   HBB2_TRICR              Reviewed;         145 AA.
AC   P10786;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Hemoglobin subunit beta-2;
DE   AltName: Full=Beta-2-globin;
DE   AltName: Full=Hemoglobin beta-2 chain;
DE   AltName: Full=Hemoglobin beta-minor chain;
GN   Name=HBB2;
OS   Triturus cristatus (Great crested newt) (Warty newt).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Triturus.
OX   NCBI_TaxID=8323;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3242554; DOI=10.1515/bchm3.1988.369.2.1343;
RA   Kleinschmidt T., Sgouros J.G., Braunitzer G.;
RT   "The first sequenced normal hemoglobin lacking histidine in position 146 of
RT   the beta-chains. The primary structures of the major and minor hemoglobin
RT   components of the great crested newt (Triturus cristatus, Urodela,
RT   Amphibia).";
RL   Biol. Chem. Hoppe-Seyler 369:1343-1360(1988).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Minor hemoglobin is a tetramer of two alpha-2 chains and two
CC       beta-2 chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S02027; S02027.
DR   AlphaFoldDB; P10786; -.
DR   SMR; P10786; -.
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..145
FT                   /note="Hemoglobin subunit beta-2"
FT                   /id="PRO_0000053139"
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   145 AA;  16218 MW;  04C8F25E427BAAC5 CRC64;
     VHLTAEDRKE IAAILGKVNV DSLGGQCLAR LIVVNPWSRR YFHDFGDLSS CDAICRNPKV
     LAHGAKVMRS IVEATKHLDN LREYYADLSV THSLKFYVDP ENFKLFSGIV IVCLALTLQT
     DFSCHKQLAF EKLMKGVSHA LGHGY