HBB_BRATR
ID HBB_BRATR Reviewed; 147 AA.
AC P14526; Q45XH9;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Bradypus tridactylus (Pale-throated three-toed sloth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Pilosa; Folivora; Bradypodidae; Bradypus.
OX NCBI_TaxID=9354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sloan A.M., Campbell K.L.;
RT "Atypical molecular evolution of afrotherian and xenarthran beta-globin
RT cluster genes.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=2757790; DOI=10.1515/bchm3.1989.370.1.303;
RA Kleinschmidt T., Marz J., Braunitzer G.;
RT "The primary structure of pale-throated three-toed sloth (Bradypus
RT tridactylus, Xenarthra) hemoglobin.";
RL Biol. Chem. Hoppe-Seyler 370:303-308(1989).
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 -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; DQ091214; AAZ22685.1; -; Genomic_DNA.
DR PIR; S03999; HBOWP.
DR AlphaFoldDB; P14526; -.
DR SMR; P14526; -.
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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:2757790"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052897"
FT BINDING 64
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 93
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 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 83
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 94
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 145
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT CONFLICT 17
FT /note="H -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 16282 MW; 6D6E1A7149CBB3D5 CRC64;
MVHLADDEKA AVSALWHKVH VEEFGGEALG RLLVVYPWTS RFFESFGDLS SADAVFSNAK
VKAHGKKVLT SFGEGLKHLD DLKGTYAHLS ELHCDKLHVD PENFKLLGNV LVIVLARHFG
KEFTPQLQAA YQKVTTGVST ALAHKYH
