HBB_FELCA
ID HBB_FELCA Reviewed; 146 AA.
AC P07412;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Hemoglobin subunit beta-A/B;
DE AltName: Full=Beta-A/B-globin;
DE AltName: Full=Hemoglobin beta-A/B chain;
GN Name=HBB;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP PROTEIN SEQUENCE, AND ACETYLATION AT SER-1 (VARIANT BETA-B).
RX PubMed=4063071; DOI=10.1515/bchm3.1985.366.2.699;
RA Abbasi A., Braunitzer G.;
RT "The primary structure of hemoglobins from the domestic cat (Felis catus,
RT Felidae).";
RL Biol. Chem. Hoppe-Seyler 366:699-704(1985).
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-A. {ECO:0000269|PubMed:4063071}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR PIR; B25203; B25203.
DR PDB; 3D4X; X-ray; 2.20 A; B/D=2-146.
DR PDB; 3GQP; X-ray; 2.00 A; B/D=2-146.
DR PDB; 3GQR; X-ray; 2.40 A; B/D/F/H=2-146.
DR PDB; 3GYS; X-ray; 2.90 A; B/D/F/H=2-146.
DR PDBsum; 3D4X; -.
DR PDBsum; 3GQP; -.
DR PDBsum; 3GQR; -.
DR PDBsum; 3GYS; -.
DR AlphaFoldDB; P07412; -.
DR SMR; P07412; -.
DR STRING; 9685.ENSFCAP00000015261; -.
DR iPTMnet; P07412; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P07412; -.
DR EvolutionaryTrace; P07412; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0031721; F:hemoglobin alpha binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043177; F:organic acid binding; IBA:GO_Central.
DR GO; GO:0019825; F:oxygen binding; IBA:GO_Central.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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; Reference proteome;
KW S-nitrosylation; Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta-A/B"
FT /id="PRO_0000052958"
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-acetylserine; in variant beta-B"
FT /evidence="ECO:0000269|PubMed:4063071"
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 VARIANT 1
FT /note="G -> S (in beta-B)"
FT /evidence="ECO:0000269|PubMed:4063071"
FT VARIANT 4
FT /note="T -> S (in beta-B)"
FT /evidence="ECO:0000269|PubMed:4063071"
FT VARIANT 139
FT /note="N -> S (in beta-B)"
FT /evidence="ECO:0000269|PubMed:4063071"
FT VARIANT 144
FT /note="K -> R (in beta-B)"
FT /evidence="ECO:0000269|PubMed:4063071"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:3GQP"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3GQP"
FT HELIX 124..142
FT /evidence="ECO:0007829|PDB:3GQP"
SQ SEQUENCE 146 AA; 15926 MW; FB227B1E903CDAFB CRC64;
GFLTAEEKGL VNGLWGKVNV DEVGGEALGR LLVVYPWTQR FFESFGDLSS ADAIMSNAKV
KAHGKKVLNS FSDGLKNIDD LKGAFAKLSE LHCDKLHVDP ENFRLLGNVL VCVLAHHFGH
DFNPQVQAAF QKVVAGVANA LAHKYH
