HBA_BOVIN
ID HBA_BOVIN Reviewed; 142 AA.
AC P01966; A3KN13; Q3SZE0; Q9TTR9; Q9TTS0; Q9TTS1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Hemoglobin subunit alpha;
DE AltName: Full=Alpha-globin;
DE AltName: Full=Hemoglobin alpha chain;
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000250|UniProtKB:P01946};
GN Name=HBA;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES N; S AND Y).
RC STRAIN=Podolian;
RA Rullo R., Pieragostini E., Vincenti D., Campanile C., Di Luccia A.;
RT "Nucleotide sequence of Podolian cattle (Bos taurus primigenius) alpha
RT globin genes.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-142.
RC STRAIN=Holstein;
RX PubMed=6048714; DOI=10.1016/0003-9861(67)90591-7;
RA Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Babin D.R.;
RT "Amino acid sequence of the alpha-chain of bovine fetal hemoglobin.";
RL Arch. Biochem. Biophys. 120:1-14(1967).
RN [4]
RP PROTEIN SEQUENCE OF 2-24.
RC TISSUE=Brain capillary;
RX PubMed=2769252; DOI=10.1111/j.1471-4159.1989.tb07388.x;
RA Pardridge W.M., Nowlin D.M., Calaycay J., Shively J.E.;
RT "Predominant low-molecular-weight proteins in isolated brain capillaries
RT are histones.";
RL J. Neurochem. 53:1014-1018(1989).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=8411160; DOI=10.1006/jmbi.1993.1530;
RA Perutz M.F., Fermi G., Poyart C., Pagnier J., Kister J.;
RT "A novel allosteric mechanism in haemoglobin. Structure of bovine
RT deoxyhaemoglobin, absence of specific chloride-binding sites and origin of
RT the chloride-linked Bohr effect in bovine and human haemoglobin.";
RL J. Mol. Biol. 233:536-545(1993).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=11369847; DOI=10.1110/ps.48301;
RA Safo M.K., Abraham D.J.;
RT "The X-ray structure determination of bovine carbonmonoxy hemoglobin at 2.1
RT A resolution and its relationship to the quaternary structures of other
RT hemoglobin crystal forms.";
RL Protein Sci. 10:1091-1099(2001).
CC -!- FUNCTION: Involved in oxygen transport from the lung to the various
CC peripheral tissues.
CC -!- FUNCTION: [Hemopressin]: Hemopressin acts as an antagonist peptide of
CC the cannabinoid receptor CNR1. Hemopressin-binding efficiently blocks
CC cannabinoid receptor CNR1 and subsequent signaling.
CC {ECO:0000250|UniProtKB:P01946}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- POLYMORPHISM: There are 3 alleles in Podolian cattle; N, S and Y.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/HB/";
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DR EMBL; AJ242797; CAB56827.1; -; Genomic_DNA.
DR EMBL; AJ242798; CAB56828.1; -; Genomic_DNA.
DR EMBL; AJ242799; CAB56829.1; -; Genomic_DNA.
DR EMBL; BC102940; AAI02941.1; -; mRNA.
DR EMBL; BC133477; AAI33478.1; -; mRNA.
DR PIR; A02289; HABO.
DR RefSeq; NP_001070890.2; NM_001077422.3.
DR RefSeq; XP_001788728.1; XM_001788676.4.
DR RefSeq; XP_003585623.1; XM_003585575.2.
DR PDB; 1FSX; X-ray; 2.10 A; A/C=2-142.
DR PDB; 1G08; X-ray; 1.90 A; A/C=2-142.
DR PDB; 1G09; X-ray; 2.04 A; A/C=2-142.
DR PDB; 1G0A; X-ray; 2.04 A; A/C=2-142.
DR PDB; 1HDA; X-ray; 2.20 A; A/C=2-142.
DR PDB; 2QSP; X-ray; 1.85 A; A/C=2-142.
DR PDB; 2QSS; X-ray; 1.75 A; A/C=2-142.
DR PDB; 3CIU; X-ray; 3.50 A; A/C=2-142.
DR PDB; 3PI8; X-ray; 2.20 A; A/C=2-142.
DR PDB; 3PI9; X-ray; 2.90 A; A/C=2-142.
DR PDB; 3PIA; X-ray; 2.10 A; A/C=2-142.
DR PDB; 6IHX; X-ray; 1.46 A; A/C=2-141.
DR PDB; 6II1; X-ray; 1.34 A; A/C=2-139.
DR PDBsum; 1FSX; -.
DR PDBsum; 1G08; -.
DR PDBsum; 1G09; -.
DR PDBsum; 1G0A; -.
DR PDBsum; 1HDA; -.
DR PDBsum; 2QSP; -.
DR PDBsum; 2QSS; -.
DR PDBsum; 3CIU; -.
DR PDBsum; 3PI8; -.
DR PDBsum; 3PI9; -.
DR PDBsum; 3PIA; -.
DR PDBsum; 6IHX; -.
DR PDBsum; 6II1; -.
DR AlphaFoldDB; P01966; -.
DR BMRB; P01966; -.
DR SMR; P01966; -.
DR BioGRID; 169070; 1.
DR STRING; 9913.ENSBTAP00000037374; -.
DR Allergome; 8242; Bos d HG.
DR PaxDb; P01966; -.
DR PeptideAtlas; P01966; -.
DR PRIDE; P01966; -.
DR Ensembl; ENSBTAT00000037545; ENSBTAP00000037374; ENSBTAG00000051412.
DR GeneID; 100140149; -.
DR GeneID; 512439; -.
DR KEGG; bta:100140149; -.
DR KEGG; bta:512439; -.
DR CTD; 15121; -.
DR CTD; 3039; -.
DR VEuPathDB; HostDB:ENSBTAG00000051412; -.
DR eggNOG; KOG3378; Eukaryota.
DR GeneTree; ENSGT00940000154590; -.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P01966; -.
DR OMA; ARMFIAY; -.
DR OrthoDB; 1398217at2759; -.
DR TreeFam; TF332328; -.
DR Reactome; R-BTA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-BTA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-BTA-2168880; Scavenging of heme from plasma.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-BTA-9707616; Heme signaling.
DR EvolutionaryTrace; P01966; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000051412; Expressed in floor plate of diencephalon and 104 other tissues.
DR ExpressionAtlas; P01966; baseline and differential.
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:0005506; F:iron ion binding; IEA:InterPro.
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; cd08927; Hb-alpha-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; IPR002338; Hemoglobin_a-typ.
DR InterPro; IPR002339; Hemoglobin_pi.
DR Pfam; PF00042; Globin; 1.
DR PRINTS; PR00612; ALPHAHAEM.
DR PRINTS; PR00815; PIHAEM.
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 Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2769252,
FT ECO:0000269|PubMed:6048714"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052568"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455842"
FT BINDING 59
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 88
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 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 8
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 12
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 17
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 41
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01942"
FT VARIANT 90
FT /note="H -> Y (in allele Y)"
FT /evidence="ECO:0000269|Ref.1"
FT VARIANT 132
FT /note="N -> S (in allele S)"
FT /evidence="ECO:0000269|Ref.1"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:6II1"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3CIU"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:6II1"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:6II1"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:6II1"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:6IHX"
SQ SEQUENCE 142 AA; 15184 MW; 6D20CADDA05C0DC5 CRC64;
MVLSAADKGN VKAAWGKVGG HAAEYGAEAL ERMFLSFPTT KTYFPHFDLS HGSAQVKGHG
AKVAAALTKA VEHLDDLPGA LSELSDLHAH KLRVDPVNFK LLSHSLLVTL ASHLPSDFTP
AVHASLDKFL ANVSTVLTSK YR
