HBA_MOUSE
ID HBA_MOUSE Reviewed; 142 AA.
AC P01942;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
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; Synonyms=Hba-a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BALB/cJ;
RX PubMed=519760; DOI=10.1016/0092-8674(79)90139-9;
RA Nishioka Y., Leder P.;
RT "The complete sequence of a chromosomal mouse alpha-globin gene reveals
RT elements conserved throughout vertebrate evolution.";
RL Cell 18:875-882(1979).
RN [2]
RP PROTEIN SEQUENCE OF 2-142.
RC STRAIN=BALB/cJ, C57BL/6J, and NB;
RX PubMed=5340470; DOI=10.1016/0022-2836(67)90347-6;
RA Popp R.A.;
RT "Hemoglobins of mice: sequence and possible ambiguity at one position of
RT the alpha chain.";
RL J. Mol. Biol. 27:9-16(1967).
RN [3]
RP PROTEIN SEQUENCE OF 18-57; 94-100 AND 129-140, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-99.
RX PubMed=282635; DOI=10.1073/pnas.75.12.6187;
RA Leder A., Miller H.I., Hamer D.H., Seidman J.G., Norman B., Sullivan M.,
RA Leder P.;
RT "Comparison of cloned mouse alpha- and beta-globin genes: conservation of
RT intervening sequence locations and extragenic homology.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:6187-6191(1978).
RN [5]
RP NUCLEOTIDE SEQUENCE OF 84-109.
RX PubMed=277329; DOI=10.1101/sqb.1978.042.01.098;
RA Curtis P.J., Mantei N., Weissmann C.;
RT "Characterization and kinetics of synthesis of 15S beta-globin RNA, a
RT putative precursor of beta-globin mRNA.";
RL Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25; SER-103; THR-109;
RP SER-112; SER-125; SER-132; THR-135; THR-138 AND SER-139, VARIANT [LARGE
RP SCALE ANALYSIS] ASN-69, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-12; LYS-17 AND LYS-41,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8]
RP VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
RX PubMed=5345070; DOI=10.1093/oxfordjournals.jhered.a107953;
RA Popp R.A.;
RT "Studies on the mouse hemoglobin loci. 8. A fourth alpha-chain phenotype.";
RL J. Hered. 60:126-133(1969).
RN [9]
RP VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
RA Popp R.A.;
RL (In) Altman P.A., Katz D.D. (eds.);
RL Inbred and genetically defined strains of laboratory animals, pp.105-105,
RL Federation of American Societies for Experimental Biology, Bethesda (1979).
RN [10]
RP VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
RX PubMed=7092800; DOI=10.1007/bf00484946;
RA Popp R.A., Bailiff E.G., Skow L.C., Whitney J.B. III;
RT "The primary structure of genetic variants of mouse hemoglobin.";
RL Biochem. Genet. 20:199-208(1982).
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: In inbred mouse strains there are at least 6 alleles that
CC can occur at the HBA locus: A, B, C, D, F, or G. Strains carrying the A
CC and F alleles produce a single kind of alpha chain, whereas those
CC carrying B, C, D, or G each produce 2 kinds of chains. The sequence
CC shown is that of the B(1) and D(1) allele chains.
CC {ECO:0000269|PubMed:7092800}.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
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DR EMBL; V00714; CAA24095.1; -; Genomic_DNA.
DR EMBL; M10703; AAA37782.2; -; Genomic_DNA.
DR EMBL; M10840; AAA37784.1; -; mRNA.
DR CCDS; CCDS24523.1; -.
DR PIR; A90791; HAMS.
DR PDB; 3HRW; X-ray; 2.80 A; A/C=2-142.
DR PDBsum; 3HRW; -.
DR AlphaFoldDB; P01942; -.
DR SMR; P01942; -.
DR ComplexPortal; CPX-2922; Hemoglobin HbA complex, variant HBB1.
DR ComplexPortal; CPX-2924; Hemoglobin HbA complex, variant HBB2.
DR DIP; DIP-34118N; -.
DR IntAct; P01942; 12.
DR MINT; P01942; -.
DR STRING; 10090.ENSMUSP00000090895; -.
DR iPTMnet; P01942; -.
DR PhosphoSitePlus; P01942; -.
DR SwissPalm; P01942; -.
DR REPRODUCTION-2DPAGE; IPI00469114; -.
DR REPRODUCTION-2DPAGE; P01942; -.
DR SWISS-2DPAGE; P01942; -.
DR CPTAC; non-CPTAC-3573; -.
DR EPD; P01942; -.
DR jPOST; P01942; -.
DR MaxQB; P01942; -.
DR PaxDb; P01942; -.
DR PeptideAtlas; P01942; -.
DR PRIDE; P01942; -.
DR ProteomicsDB; 269719; -.
DR MGI; MGI:96015; Hba-a1.
DR eggNOG; KOG3378; Eukaryota.
DR InParanoid; P01942; -.
DR PhylomeDB; P01942; -.
DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-MMU-2168880; Scavenging of heme from plasma.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR Reactome; R-MMU-9707616; Heme signaling.
DR ChiTaRS; Hba-a1; mouse.
DR EvolutionaryTrace; P01942; -.
DR PRO; PR:P01942; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P01942; protein.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:MGI.
DR GO; GO:0005833; C:hemoglobin complex; IPI:ComplexPortal.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0031720; F:haptoglobin binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0043177; F:organic acid binding; ISO:MGI.
DR GO; GO:0019825; F:oxygen binding; ISO:MGI.
DR GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0048821; P:erythrocyte development; IGI:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR GO; GO:0030185; P:nitric oxide transport; ISO:MGI.
DR GO; GO:0015671; P:oxygen transport; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
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:5340470"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha"
FT /id="PRO_0000052694"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000250|UniProtKB:P01946"
FT /id="PRO_0000455906"
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:0007744|PubMed:23806337"
FT MOD_RES 12
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:23806337"
FT MOD_RES 25
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 41
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VARIANT 26
FT /note="G -> V (in allele chain C(1) and in strain: NB)"
FT /evidence="ECO:0000269|PubMed:5345070,
FT ECO:0000269|PubMed:7092800, ECO:0000269|Ref.9"
FT VARIANT 63
FT /note="V -> I (in allele chain C(1) and in strain: NB)"
FT /evidence="ECO:0000269|PubMed:5345070,
FT ECO:0000269|PubMed:7092800, ECO:0000269|Ref.9"
FT VARIANT 69
FT /note="S -> N (in allele chains A, C(2), D(2), F, G(1) and
FT G(2) and in strain: C57BL)"
FT /evidence="ECO:0000269|PubMed:5345070,
FT ECO:0000269|PubMed:7092800, ECO:0000269|Ref.9,
FT ECO:0007744|PubMed:21183079"
FT VARIANT 69
FT /note="S -> T (in allele chain B(2) and in 1 BALB/C strain
FT sequence)"
FT /evidence="ECO:0000269|PubMed:5345070,
FT ECO:0000269|PubMed:7092800, ECO:0000269|Ref.9"
FT VARIANT 79
FT /note="G -> A (in allele chains F and G(2))"
FT /evidence="ECO:0000269|PubMed:5345070,
FT ECO:0000269|PubMed:7092800, ECO:0000269|Ref.9"
FT HELIX 6..17
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:3HRW"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:3HRW"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:3HRW"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:3HRW"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:3HRW"
SQ SEQUENCE 142 AA; 15085 MW; 2F70043BFF66E24A CRC64;
MVLSGEDKSN IKAAWGKIGG HGAEYGAEAL ERMFASFPTT KTYFPHFDVS HGSAQVKGHG
KKVADALASA AGHLDDLPGA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL ASHHPADFTP
AVHASLDKFL ASVSTVLTSK YR
