HBB_CERSI
ID HBB_CERSI Reviewed; 146 AA.
AC P02066;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Ceratotherium simum (White rhinoceros) (Square-lipped rhinoceros).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Rhinocerotidae; Ceratotherium.
OX NCBI_TaxID=9807;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=7141412;
RA Mazur G., Braunitzer G., Wright P.G.;
RT "The primary structure of the hemoglobin from a white rhinoceros
RT (Ceratotherium simum, perissodactyla): beta 2 Glu.";
RL Hoppe-Seyler's Z. Physiol. Chem. 363:1077-1085(1982).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- MISCELLANEOUS: The variants found in this sample from a single animal
CC suggest the presence of at least two beta chain loci.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02384; HBRNW.
DR AlphaFoldDB; P02066; -.
DR SMR; P02066; -.
DR PRIDE; P02066; -.
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_0000052920"
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 44
FT /note="Phosphoserine"
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 62
FT /note="A -> S"
FT VARIANT 62
FT /note="A -> T"
FT VARIANT 116
FT /note="K -> Q"
SQ SEQUENCE 146 AA; 15967 MW; E591654D27827FDC CRC64;
VELTAEEKAA VLALWDKVKE DEVGGEALGR LLVVYPWTQR FFDSFGDLST PAAVMGNAKV
KAHGKKVLHS FGDGVHHLDN LKGTFAALSE LHCDKLHVDP ENFRLLGNVL VVVLAKHFGK
QFTPELQAAY QKVVAGVANA LAHKYH
