HBB_MESAU
ID HBB_MESAU Reviewed; 147 AA.
AC P02094;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
DE AltName: Full=Hemoglobin beta-major chain;
GN Name=HBB;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1562610; DOI=10.1016/0167-4781(92)90451-5;
RA Lee K.M., Subar M., Li H., Boussios T.;
RT "Cloning of two adult hamster globin cDNAs (alpha and beta major).";
RL Biochim. Biophys. Acta 1130:343-344(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RA Braunitzer G., Schrank B., Stangl A., Wiesner H.;
RT "Respiration at high altitudes, phosphate-protein-interaction: sequence of
RT the hemoglobins of the hamster (Mesocricetus aureatus) and the camel
RT (Camelus ferus, Camelidae).";
RL J. Chem. Soc. Pak. 2:1-7(1980).
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; X57030; CAA40346.1; -; mRNA.
DR PIR; A02410; HBHY.
DR PIR; S22336; S22336.
DR AlphaFoldDB; P02094; -.
DR SMR; P02094; -.
DR Proteomes; UP000189706; Unplaced.
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; Reference proteome; S-nitrosylation;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086, ECO:0000269|Ref.2"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053016"
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 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 51..53
FT /note="SAS -> LPV (in Ref. 1; CAA40346)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="S -> I (in Ref. 1; CAA40346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 147 AA; 15991 MW; B398F240D6141C92 CRC64;
MVHLTDAEKA LVTGLWGKVN ADAVGAEALG RLLVVYPWTQ RFFEHFGDLS SASAVMNNPQ
VKAHGKKVIH SFADGLKHLD NLKGAFSSLS ELHCDKLHVD PENFKLLGNM IIIVLSHDLG
KDFTPSAQSA FHKVVAGVAN ALAHKYH
