HBB_PIG
ID HBB_PIG Reviewed; 147 AA.
AC P02067; Q29025;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hemoglobin subunit beta;
DE AltName: Full=Beta-globin;
DE AltName: Full=Hemoglobin beta chain;
GN Name=HBB;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sharma A., Parson C.T., Midha S., Okabe J., Yerle M., Pinton P., Logan J.,
RA Kumar L.R.;
RT "Molecular characterization of porcine beta globin locus.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-147.
RX PubMed=565742;
RA Braunitzer G., Schrank B., Stangl A., Scheithauer U.;
RT "Hemoglobins, XXI. Sequence analysis of porcine hemoglobin.";
RL Hoppe-Seyler's Z. Physiol. Chem. 359:137-146(1978).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME.
RX PubMed=7990139; DOI=10.1006/jmbi.1994.1751;
RA Katz D.S., White S.P., Huang W., Kumar R., Christianson D.W.;
RT "Structure determination of aquomet porcine hemoglobin at 2.8-A
RT resolution.";
RL J. Mol. Biol. 244:541-553(1994).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-147 IN COMPLEX WITH HEME.
RX PubMed=10713517; DOI=10.1107/s0907444900000093;
RA Lu T.-H., Panneerselvam K., Liaw Y.-C., Kan P., Lee C.-J.;
RT "Structure determination of porcine haemoglobin.";
RL Acta Crystallogr. D 56:304-312(2000).
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 -!- INTERACTION:
CC P02067; Q5U8X5; Xeno; NbExp=6; IntAct=EBI-9014782, EBI-12557210;
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; X86791; CAA60490.1; -; Genomic_DNA.
DR PIR; S54269; HBPG.
DR RefSeq; NP_001138313.1; NM_001144841.1.
DR PDB; 1QPW; X-ray; 1.80 A; B/D=2-147.
DR PDB; 2PGH; X-ray; 2.80 A; B/D=2-147.
DR PDB; 4F4O; X-ray; 2.90 A; B/E/H/K=2-147.
DR PDBsum; 1QPW; -.
DR PDBsum; 2PGH; -.
DR PDBsum; 4F4O; -.
DR AlphaFoldDB; P02067; -.
DR SMR; P02067; -.
DR DIP; DIP-59910N; -.
DR IntAct; P02067; 2.
DR STRING; 9823.ENSSSCP00000015647; -.
DR ChEMBL; CHEMBL4006; -.
DR PaxDb; P02067; -.
DR PeptideAtlas; P02067; -.
DR PRIDE; P02067; -.
DR GeneID; 407066; -.
DR KEGG; ssc:407066; -.
DR CTD; 3043; -.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P02067; -.
DR OrthoDB; 1370439at2759; -.
DR EvolutionaryTrace; P02067; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02086,
FT ECO:0000269|PubMed:565742"
FT CHAIN 2..147
FT /note="Hemoglobin subunit beta"
FT /id="PRO_0000053071"
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 /evidence="ECO:0000250|UniProtKB:P80044"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00238,
FT ECO:0000269|PubMed:10713517, ECO:0000269|PubMed:7990139,
FT ECO:0007744|PDB:1QPW, ECO:0007744|PDB:2PGH,
FT ECO:0007744|PDB:4F4O"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0000250|UniProtKB:P02086"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P68871"
FT MOD_RES 60
FT /note="N6-acetyllysine"
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 126
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 59..75
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1QPW"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:1QPW"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:1QPW"
SQ SEQUENCE 147 AA; 16166 MW; FC96A95FE14CEC93 CRC64;
MVHLSAEEKE AVLGLWGKVN VDEVGGEALG RLLVVYPWTQ RFFESFGDLS NADAVMGNPK
VKAHGKKVLQ SFSDGLKHLD NLKGTFAKLS ELHCDQLHVD PENFRLLGNV IVVVLARRLG
HDFNPNVQAA FQKVVAGVAN ALAHKYH
