ID   HBB_ECHTE               Reviewed;         146 AA.
AC   P24292;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Hemoglobin subunit beta;
DE   AltName: Full=Beta-globin;
DE   AltName: Full=Hemoglobin beta chain;
GN   Name=HBB;
OS   Echinops telfairi (Lesser hedgehog tenrec).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Tenrecidae; Tenrecinae; Echinops.
OX   NCBI_TaxID=9371;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1793518; DOI=10.1515/bchm3.1991.372.2.975;
RA   Piccinini M., Kleinschmidt T., Gorr T., Weber R.E., Kuenzle H.,
RA   Braunitzer G.;
RT   "Primary structure and oxygen-binding properties of the hemoglobin from the
RT   lesser hedgehog tenrec (Echinops telfairi, Zalambdodonta). Evidence for
RT   phylogenetic isolation.";
RL   Biol. Chem. Hoppe-Seyler 372:975-989(1991).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC       peripheral tissues.
CC   -!- SUBUNIT: Tetramer of two alpha and two different beta chains. Two
CC       external cysteine residues at beta-16 and beta-52 cause reversible
CC       polymerization to octamers and most likely irreversible formation of
CC       higher polymers.
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; S18398; S18398.
DR   AlphaFoldDB; P24292; -.
DR   SMR; P24292; -.
DR   PRIDE; P24292; -.
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   Acetylation; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Phosphoprotein; S-nitrosylation; Transport.
FT   CHAIN           1..146
FT                   /note="Hemoglobin subunit beta"
FT                   /id="PRO_0000052951"
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"
FT   MOD_RES         1
FT                   /note="N-acetylvaline"
FT                   /evidence="ECO:0000250|UniProtKB:P02086"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         59
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         82
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         93
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   MOD_RES         144
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P68871"
FT   VARIANT         16
FT                   /note="G -> C"
FT   VARIANT         118
FT                   /note="F -> L"
SQ   SEQUENCE   146 AA;  16135 MW;  43FFAED7AD7EBC9D CRC64;
     VHMTDAEKKL VTTMWGKLDV DAAGAETLGR VLVVYPWTQR FFGHFGDLSS ACAVMDNPKV
     QAHGKKVLHS LGDGLNHLDD LKHFYAALSE LHCDKLHVDP ENFRLLGNVL VCVMSRHFGA
     EFTPQVQAAY QKVVAGVANA LAHKYH