ID   HBB2_SPHPU              Reviewed;         146 AA.
AC   P10061;
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;
GN   Name=HBB2;
OS   Sphenodon punctatus (Tuatara) (Hatteria punctata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Sphenodontia; Sphenodontidae; Sphenodon.
OX   NCBI_TaxID=8508;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=3214555; DOI=10.1515/bchm3.1988.369.2.755;
RA   Abbasi A., Wells R.M.G., Brittain T., Braunitzer G.;
RT   "Primary structure of the hemoglobins from Sphenodon (Sphenodon punctatus,
RT   Tuatara, Rynchocephalia). Evidence for the expression of alpha D-gene.";
RL   Biol. Chem. Hoppe-Seyler 369:755-764(1988).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: There are three forms of hemoglobin in Sphenodon: A, A' and D.
CC       Hb A is a tetramer of two alpha-A and two beta-1, Hb A' is a tetramer
CC       of two alpha-a and two beta-2, Hb D is a tetramer of two alpha-D and
CC       two beta-2.
CC   -!- MISCELLANEOUS: Sphenodon Hbs have properties not found in other
CC       reptiles: poor cooperativity, high affinity for oxygen, small Bohr and
CC       haldane effects, appreciable phosphate effects (those properties are
CC       also found in the Hbs of primitive urodele and caecilian amphibians).
CC   -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00238}.
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DR   PIR; S01139; HBTJ2.
DR   AlphaFoldDB; P10061; -.
DR   SMR; P10061; -.
DR   Proteomes; UP000694392; Unplaced.
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   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta-2"
FT                   /id="PRO_0000053114"
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   146 AA;  16342 MW;  1090F7074756ACBA CRC64;
     VHWTAEEKQL VTSLWTKVNV DECGGEALGR LLIVYPWTQR FFSSFGNLSS STAICGNPRV
     KAHGKKVFTS FGEAVKNLDN IKATYAKLSE LHCEKLHVDP QNFNLLGDIF IIVLAAHFGK
     DFTPACQAAW QKLVRVVAHA LAYHYH