HBB_PTEGI
ID HBB_PTEGI Reviewed; 146 AA.
AC D0VX08; P86192;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Hemoglobin subunit beta {ECO:0000250|UniProtKB:P14391};
DE AltName: Full=Beta-globin {ECO:0000250|UniProtKB:P14391};
DE AltName: Full=Hemoglobin beta chain {ECO:0000250|UniProtKB:P14391, ECO:0000312|PDB:3FH9};
GN Name=HBB {ECO:0000250|UniProtKB:P14391};
OS Pteropus giganteus (Indian flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=143291;
RN [1] {ECO:0000305, ECO:0000312|PDB:3FH9}
RP X-RAY CRYSTALLOGRAPHY (1.62 ANGSTROMS).
RA Moorthy P.S., Neelagandan K., Balasubramanian M., Thenmozhi M.,
RA Ponnuswamy M.N.;
RT "Crystal structure determination of Indian flying fox (Pteropus giganteus)
RT at 1.62 A resolution.";
RL Submitted (DEC-2008) to the PDB data bank.
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Red blood cells. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PDB; 3FH9; X-ray; 1.62 A; B=1-146.
DR PDBsum; 3FH9; -.
DR AlphaFoldDB; D0VX08; -.
DR SMR; D0VX08; -.
DR PRIDE; D0VX08; -.
DR EvolutionaryTrace; D0VX08; -.
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 CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000398146"
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 /evidence="ECO:0000305"
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 /evidence="ECO:0000305"
FT MOD_RES 1
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
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 HELIX 5..15
FT /evidence="ECO:0007829|PDB:3FH9"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:3FH9"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3FH9"
SQ SEQUENCE 146 AA; 15937 MW; FC0590DF35543643 CRC64;
VHLSGEEKAA VTGLWGKVKV DEVGGEALGR LLVVYPWTQR FFDSFGDLSS ASAVMGNPKV
KAHGKKVLDS FSEGLQHLDN LKGTFAKLSE LHCDKLHVDP ENFRLLGNVL VCVLARHFGK
EFTPQVQAAY QKVVAGVANA LAHKYH