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   27-MAR-2024, 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; 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,
RC   Pancreas, 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   GlyGen; P01942; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P01942; -.
DR   PhosphoSitePlus; P01942; -.
DR   SwissPalm; P01942; -.
DR   REPRODUCTION-2DPAGE; IPI00469114; -.
DR   REPRODUCTION-2DPAGE; P01942; -.
DR   CPTAC; non-CPTAC-3573; -.
DR   EPD; P01942; -.
DR   jPOST; P01942; -.
DR   MaxQB; P01942; -.
DR   PaxDb; 10090-ENSMUSP00000090895; -.
DR   PeptideAtlas; P01942; -.
DR   ProteomicsDB; 269719; -.
DR   Pumba; P01942; -.
DR   AGR; MGI:96015; -.
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: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:0001540; F:amyloid-beta binding; ISO:MGI.
DR   GO; GO:0001664; F:G protein-coupled receptor 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; IBA:GO_Central.
DR   GO; GO:0005344; F:oxygen carrier activity; IBA:GO_Central.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0015670; P:carbon dioxide transport; NAS:ComplexPortal.
DR   GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR   GO; GO:0048821; P:erythrocyte development; IGI:MGI.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0030185; P:nitric oxide transport; ISO:ComplexPortal.
DR   GO; GO:0015671; P:oxygen transport; ISO:ComplexPortal.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR   GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR   CDD; cd08927; Hb-alpha-like; 1.
DR   Gene3D; 1.10.490.10; Globins; 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   PANTHER; PTHR11442; HEMOGLOBIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR11442:SF48; HEMOGLOBIN SUBUNIT ALPHA; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00612; ALPHAHAEM.
DR   PRINTS; PR00815; PIHAEM.
DR   SUPFAM; SSF46458; Globin-like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
DR   SWISS-2DPAGE; P01942; -.
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="O2"
FT                   /ligand_id="ChEBI:CHEBI:15379"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00238"
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
//