HBB_CAVPO
ID HBB_CAVPO Reviewed; 146 AA.
AC P02095;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=527943;
RA Braunitzer G., Schrank B., Stangl A., Wiesner H.;
RT "Respiration at high altitudes, phosphate-protein interaction: the sequence
RT of hemoglobins from guinea pig and dromedary.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:1941-1946(1979).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS), AND SUBUNIT.
RX PubMed=20811494; DOI=10.1371/journal.pone.0012389;
RA Pairet B., Jaenicke E.;
RT "Structure of the altitude adapted hemoglobin of guinea pig in the R2-
RT state.";
RL PLoS ONE 5:E12389-E12389(2010).
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:20811494}.
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; A02411; HBGP.
DR PDB; 3A0G; X-ray; 2.50 A; B=1-146.
DR PDB; 3HYU; X-ray; 1.67 A; B=1-146.
DR PDBsum; 3A0G; -.
DR PDBsum; 3HYU; -.
DR AlphaFoldDB; P02095; -.
DR SMR; P02095; -.
DR STRING; 10141.ENSCPOP00000001378; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P02095; -.
DR EvolutionaryTrace; P02095; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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; Reference proteome; S-nitrosylation;
KW Transport.
FT CHAIN 1..146
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000052915"
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 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:3HYU"
FT HELIX 20..34
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 51..56
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 58..74
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:3A0G"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:3HYU"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 124..141
FT /evidence="ECO:0007829|PDB:3HYU"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3HYU"
SQ SEQUENCE 146 AA; 15921 MW; E880DAC410019685 CRC64;
VHLTAAEKSA ILDLWGKVNV GEIGAEALGR LLVVYPWTQR FFEKFGDLSS ASAIMSNAHV
KSHGAKVLAS FSEGLKHLQD LKGTFAKLSE LHCDKLHVDP ENFRLLGNMI VIALAHHHPS
EFTPCTQAAF QKVTAGVANA LAHKYH