HBB_LITCT
ID HBB_LITCT Reviewed; 140 AA.
AC P02135;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX NCBI_TaxID=8400;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3487542; DOI=10.1016/s0021-9258(19)83909-1;
RA Tam L.T., Gray G.P., Riggs A.F.;
RT "The hemoglobins of the bullfrog Rana catesbeiana. The structure of the
RT beta chain of component C and the role of the alpha chain in the formation
RT of intermolecular disulfide bonds.";
RL J. Biol. Chem. 261:8290-8294(1986).
CC -!- FUNCTION: The beta chain is a component of adult hemoglobins B. And C.
CC -!- SUBUNIT: Heterotetramer of either two alpha-B chains or two alpha-C
CC chains and two beta chains.
CC -!- MISCELLANEOUS: Hemoglobin C tetramers polymerize by the formation of
CC disulfide bonds. The deoxy tetramers of hemoglobin B and C associate to
CC form molecules believed to be trimers (B+2C) of very low oxygen
CC affinity.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; A02455; HBFGC.
DR PRIDE; P02135; -.
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..140
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053086"
FT BINDING 57
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 86
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 140 AA; 15425 MW; 01963DA6056020E5 CRC64;
GGSDVSAFLA KVDKRAVGGE ALARLLIVYP WTQRYFSTFG NLGSADAISH NSKVLAHGQR
VLDSIEEGLK HPZBLKAYYA KLSERHSGEL HVDPANFYRL GNVLITVMAR HFHEEFTPEL
QCALHSSFCA VGEALAKGYH