HBB_PHYMC
ID HBB_PHYMC Reviewed; 146 AA.
AC P09905;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Hemoglobin subunit beta-1/2;
DE AltName: Full=Beta-1/2-globin;
DE AltName: Full=Hemoglobin beta-1/2 chain;
DE AltName: Full=Hemoglobin beta-I/II chain;
GN Name=HBB;
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3718676; DOI=10.1515/bchm3.1986.367.1.355;
RA Abbasi A., Braunitzer G., Matsuda G., Maita T.;
RT "The primary structure of sperm whale hemoglobin (Physeter catodon,
RT cetacea).";
RL Biol. Chem. Hoppe-Seyler 367:355-361(1986).
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 -!- POLYMORPHISM: There are two alleles. The sequence shown is that of
CC beta-II. {ECO:0000269|PubMed:3718676}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; B25728; B25728.
DR AlphaFoldDB; P09905; -.
DR SMR; P09905; -.
DR STRING; 9755.ENSPCTP00005030320; -.
DR PRIDE; P09905; -.
DR Proteomes; UP000248484; Genome assembly.
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 CHAIN 1..146
FT /note="Hemoglobin subunit beta-1/2"
FT /id="PRO_0000053070"
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 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 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 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 VARIANT 2
FT /note="H -> Q (in beta-1)"
FT /evidence="ECO:0000269|PubMed:3718676"
FT VARIANT 5
FT /note="G -> A (in beta-1)"
FT /evidence="ECO:0000269|PubMed:3718676"
FT VARIANT 11
FT /note="L -> V (in beta-1)"
FT /evidence="ECO:0000269|PubMed:3718676"
SQ SEQUENCE 146 AA; 16184 MW; 6C65A28ADEAEE656 CRC64;
VHLTGEEKSG LTALWAKVNV EEIGGEALGR LLVVYPWTQR FFEHFGDLST ADAVMKNPKV
KKHGQKVLAS FGEGLKHLDN LKGTFATLSE LHCDKLHVDP ENFRLLGNVL VVVLARHFGK
EFTPELQTAY QKVVAGVANA LAHKYH
