HBB_EULFU
ID HBB_EULFU Reviewed; 147 AA.
AC P02053;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
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 Eulemur fulvus fulvus (Brown lemur).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Lemuridae; Eulemur.
OX NCBI_TaxID=40322;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3444413; DOI=10.1093/oxfordjournals.molbev.a040415;
RA Harris S., Thackeray J.R., Jeffreys A.J., Weiss M.L.;
RT "Nucleotide sequence analysis of the lemur beta-globin gene family:
RT evidence for major rate fluctuations in globin polypeptide evolution.";
RL Mol. Biol. Evol. 3:465-484(1986).
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=107155;
RA Maita T., Setoguchi M., Matsuda G., Goodman M.;
RT "Amino acid sequences of the alpha and beta chains of adult hemoglobin of
RT the brown lemur, Lemur fulvus fulvus.";
RL J. Biochem. 85:755-764(1979).
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; M15734; AAA36822.1; -; Genomic_DNA.
DR PIR; A02370; HBLEF.
DR AlphaFoldDB; P02053; -.
DR SMR; P02053; -.
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:0000269|PubMed:107155"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052987"
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 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
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"
SQ SEQUENCE 147 AA; 15901 MW; 690C1F6EAEDEFEFD CRC64;
MTLLSAEENA HVTSLWGKVD VEKVGGEALG RLLVVYPWTQ RFFESFGDLS SPSAVMGNPK
VKAHGKKVLS AFSEGLHHLD NLKGTFAQLS ELHCDKLHVD PQNFTLLGNV LVVVLAEHFG
NAFSPAVQAA FQKVVAGVAN ALAHKYH
