HBB_BUBBU
ID HBB_BUBBU Reviewed; 145 AA.
AC P67820; P02071;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1499282; DOI=10.1016/0305-0491(92)90163-l;
RA Ferranti P., di Luccia A., Malorni A., Pucci P., Ruoppolo M., Marino G.,
RA Ferrara L.;
RT "River buffalo (Bubalus bubalis L.) AA phenotype haemoglobins:
RT characterization by immobiline polyacrylamide gel electrophoresis and high
RT performance liquid chromatography and determination of the primary
RT structure of the constitutive chains by mass spectrometry.";
RL Comp. Biochem. Physiol. 101B:91-98(1992).
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 PIR; B58794; B58794.
DR PDB; 3CY5; X-ray; 2.00 A; B/D=1-145.
DR PDBsum; 3CY5; -.
DR AlphaFoldDB; P67820; -.
DR SMR; P67820; -.
DR EvolutionaryTrace; P67820; -.
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; Direct protein sequencing; Heme; Iron;
KW Metal-binding; Oxygen transport; Phosphoprotein; S-nitrosylation;
KW Transport.
FT CHAIN 1..145
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052898"
FT BINDING 62
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 91
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 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 58
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 81
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 92
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 35..40
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 57..75
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 100..117
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:3CY5"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3CY5"
SQ SEQUENCE 145 AA; 15986 MW; 5260F17E84737FB3 CRC64;
MLTAEEKAAV TAFWGKVHVD EVGGEALGRL LVVYPWTQRF FESFGDLSTA DAVMNNPKVK
AHGKKVLDSF SNGMKHLDDL KGTFAALSEL HCDKLHVDPE NFKLLGNVLV VVLARHFGKE
FTPVLQADFQ KVVAGVANAL AHRYH
