HBB_LEPEU
ID HBB_LEPEU Reviewed; 147 AA.
AC P08535;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Lepus europaeus (European hare).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Lepus.
OX NCBI_TaxID=9983;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3615213; DOI=10.1093/nar/15.14.5899;
RA Pauplin Y., Rech J.;
RT "Nucleotide sequence of hare adult beta-globin gene with flanking
RT regions.";
RL Nucleic Acids Res. 15:5899-5899(1987).
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; Y00347; CAA68429.1; -; Genomic_DNA.
DR PIR; A27101; A27101.
DR PDB; 3LQD; X-ray; 2.80 A; B/D=2-147.
DR PDBsum; 3LQD; -.
DR AlphaFoldDB; P08535; -.
DR SMR; P08535; -.
DR EvolutionaryTrace; P08535; -.
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 3D-structure; Acetylation; Heme; Iron; Metal-binding; Oxygen transport;
KW Phosphoprotein; S-nitrosylation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052990"
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 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"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:3LQD"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 24..35
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3LQD"
FT HELIX 125..143
FT /evidence="ECO:0007829|PDB:3LQD"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3LQD"
SQ SEQUENCE 147 AA; 16062 MW; 9047D46AB5992FDB CRC64;
MVHLSGEEKS AVTALWGKVN VEEVGGETLG RLLVVYPWTQ RFFESFGDLS TASAVMGNPK
VKAHGKKVLA AFSEGLSHLD NLKGTFAKLS ELHCDKLHVD PENFRLLGNV LVIVLSHHFG
KEFTPQVQAA YQKVVAGVAN ALAHKYH