HBB_CANLF
ID HBB_CANLF Reviewed; 146 AA.
AC P60524; P02056;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=864726; DOI=10.1007/bf01796112;
RA Brimhall B., Duerst M., Jones R.T.;
RT "The amino acid sequence of dog (Canis familiaris) hemoglobin.";
RL J. Mol. Evol. 9:231-235(1977).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=21543841; DOI=10.1107/s0907444911006044;
RA Bhatt V.S., Zaldivar-Lopez S., Harris D.R., Couto C.G., Wang P.G.,
RA Palmer A.F.;
RT "Structure of Greyhound hemoglobin: origin of high oxygen affinity.";
RL Acta Crystallogr. D 67:395-402(2011).
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 {ECO:0000269|PubMed:21543841}.
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; A02374; HBDG.
DR PDB; 2QLS; X-ray; 3.50 A; B/D=1-146.
DR PDB; 3GOU; X-ray; 3.00 A; B/D=1-146.
DR PDB; 3PEL; X-ray; 1.90 A; B=1-146.
DR PDBsum; 2QLS; -.
DR PDBsum; 3GOU; -.
DR PDBsum; 3PEL; -.
DR AlphaFoldDB; P60524; -.
DR SMR; P60524; -.
DR STRING; 9612.ENSCAFP00000009258; -.
DR PaxDb; P60524; -.
DR PRIDE; P60524; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P60524; -.
DR EvolutionaryTrace; P60524; -.
DR Proteomes; UP000002254; 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"
FT /id="PRO_0000052907"
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 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:3PEL"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 58..75
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:3PEL"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3PEL"
SQ SEQUENCE 146 AA; 15996 MW; ECD68B81D53608F1 CRC64;
VHLTAEEKSL VSGLWGKVNV DEVGGEALGR LLIVYPWTQR FFDSFGDLST PDAVMSNAKV
KAHGKKVLNS FSDGLKNLDN LKGTFAKLSE LHCDKLHVDP ENFKLLGNVL VCVLAHHFGK
EFTPQVQAAY QKVVAGVANA LAHKYH
