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Hemoglobin subunit alpha (Alpha-globin) (Hemoglobin alpha chain)

 HBA_MOUSE               Reviewed;         142 AA.
P01942;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 148.
RecName: Full=Hemoglobin subunit alpha;
AltName: Full=Alpha-globin;
AltName: Full=Hemoglobin alpha chain;
Name=Hba; Synonyms=Hba-a1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE.
STRAIN=BALB/cJ;
PubMed=519760; DOI=10.1016/0092-8674(79)90139-9;
Nishioka Y., Leder P.;
"The complete sequence of a chromosomal mouse alpha-globin gene
reveals elements conserved throughout vertebrate evolution.";
Cell 18:875-882(1979).
[2]
PROTEIN SEQUENCE OF 2-142.
STRAIN=BALB/cJ, C57BL/6J, and NB;
PubMed=5340470; DOI=10.1016/0022-2836(67)90347-6;
Popp R.A.;
"Hemoglobins of mice: sequence and possible ambiguity at one position
of the alpha chain.";
J. Mol. Biol. 27:9-16(1967).
[3]
PROTEIN SEQUENCE OF 18-57; 94-100 AND 129-140, AND IDENTIFICATION BY
MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-99.
PubMed=282635; DOI=10.1073/pnas.75.12.6187;
Leder A., Miller H.I., Hamer D.H., Seidman J.G., Norman B.,
Sullivan M., Leder P.;
"Comparison of cloned mouse alpha- and beta-globin genes: conservation
of intervening sequence locations and extragenic homology.";
Proc. Natl. Acad. Sci. U.S.A. 75:6187-6191(1978).
[5]
NUCLEOTIDE SEQUENCE OF 84-109.
PubMed=277329;
Curtis P.J., Mantei N., Weissmann C.;
"Characterization and kinetics of synthesis of 15S beta-globin RNA, a
putative precursor of beta-globin mRNA.";
Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25; SER-103; THR-109;
SER-112; SER-125; SER-132; THR-135; THR-138 AND SER-139, VARIANT
[LARGE SCALE ANALYSIS] ASN-69, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-12; LYS-17 AND
LYS-41, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[8]
VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
PubMed=5345070; DOI=10.1093/oxfordjournals.jhered.a107953;
Popp R.A.;
"Studies on the mouse hemoglobin loci. 8. A fourth alpha-chain
phenotype.";
J. Hered. 60:126-133(1969).
[9]
VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
Popp R.A.;
(In) Altman P.A., Katz D.D. (eds.);
Inbred and genetically defined strains of laboratory animals,
pp.105-105, Federation of American Societies for Experimental Biology,
Bethesda (1979).
[10]
VARIANTS VAL-26; ILE-63; ASN-69; THR-69 AND ALA-79.
PubMed=7092800; DOI=10.1007/BF00484946;
Popp R.A., Bailiff E.G., Skow L.C., Whitney J.B. III;
"The primary structure of genetic variants of mouse hemoglobin.";
Biochem. Genet. 20:199-208(1982).
-!- FUNCTION: Involved in oxygen transport from the lung to the
various peripheral tissues.
-!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
-!- TISSUE SPECIFICITY: Red blood cells.
-!- POLYMORPHISM: In inbred mouse strains there are at least 6 alleles
that can occur at the HBA locus: A, B, C, D, F, or G. Strains
carrying the A and F alleles produce a single kind of alpha chain,
whereas those carrying B, C, D, or G each produce 2 kinds of
chains. The sequence shown is that of the B(1) and D(1) allele
chains. {ECO:0000269|PubMed:7092800}.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-----------------------------------------------------------------------
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EMBL; V00714; CAA24095.1; -; Genomic_DNA.
EMBL; M10703; AAA37782.2; -; Genomic_DNA.
EMBL; M10840; AAA37784.1; -; mRNA.
CCDS; CCDS24523.1; -.
PIR; A90791; HAMS.
UniGene; Mm.196110; -.
UniGene; Mm.459653; -.
PDB; 3HRW; X-ray; 2.80 A; A/C=2-142.
PDBsum; 3HRW; -.
ProteinModelPortal; P01942; -.
SMR; P01942; -.
DIP; DIP-34118N; -.
IntAct; P01942; 11.
MINT; MINT-1869504; -.
STRING; 10090.ENSMUSP00000090897; -.
iPTMnet; P01942; -.
PhosphoSitePlus; P01942; -.
SwissPalm; P01942; -.
REPRODUCTION-2DPAGE; IPI00469114; -.
REPRODUCTION-2DPAGE; P01942; -.
SWISS-2DPAGE; P01942; -.
EPD; P01942; -.
MaxQB; P01942; -.
PaxDb; P01942; -.
PeptideAtlas; P01942; -.
PRIDE; P01942; -.
MGI; MGI:96015; Hba-a1.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
HOGENOM; HOG000036867; -.
HOVERGEN; HBG009709; -.
InParanoid; P01942; -.
PhylomeDB; P01942; -.
EvolutionaryTrace; P01942; -.
PRO; PR:P01942; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_HBA-A1; -.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:MGI.
GO; GO:0005833; C:hemoglobin complex; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0019825; F:oxygen binding; IEA:InterPro.
GO; GO:0005344; F:oxygen carrier activity; IEA:UniProtKB-KW.
GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
GO; GO:0048821; P:erythrocyte development; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
CDD; cd08927; Hb-alpha_like; 1.
InterPro; IPR000971; Globin.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR002338; Haemoglobin_a-typ.
InterPro; IPR002339; Haemoglobin_pi.
Pfam; PF00042; Globin; 1.
PRINTS; PR00612; ALPHAHAEM.
PRINTS; PR00815; PIHAEM.
SUPFAM; SSF46458; SSF46458; 1.
PROSITE; PS01033; GLOBIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Heme; Iron; Metal-binding;
Oxygen transport; Phosphoprotein; Polymorphism; Reference proteome;
Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:5340470}.
CHAIN 2 142 Hemoglobin subunit alpha.
/FTId=PRO_0000052694.
METAL 59 59 Iron (heme distal ligand).
METAL 88 88 Iron (heme proximal ligand).
MOD_RES 4 4 Phosphoserine.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 8 8 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 12 12 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 17 17 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 17 17 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 25 25 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 36 36 Phosphoserine.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 41 41 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 109 109 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 135 135 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 138 138 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VARIANT 26 26 G -> V (in allele chain C(1) and in
strain NB). {ECO:0000269|PubMed:5345070,
ECO:0000269|PubMed:7092800,
ECO:0000269|Ref.9}.
VARIANT 63 63 V -> I (in allele chain C(1) and in
strain NB). {ECO:0000269|PubMed:5345070,
ECO:0000269|PubMed:7092800,
ECO:0000269|Ref.9}.
VARIANT 69 69 S -> N (in allele chains A, C(2), D(2),
F, G(1) and G(2) and in strain C57BL).
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:5345070,
ECO:0000269|PubMed:7092800,
ECO:0000269|Ref.9}.
VARIANT 69 69 S -> T (in allele chain B(2) and in 1
BALB/C strain sequence).
{ECO:0000269|PubMed:5345070,
ECO:0000269|PubMed:7092800,
ECO:0000269|Ref.9}.
VARIANT 79 79 G -> A (in allele chains F and G(2)).
{ECO:0000269|PubMed:5345070,
ECO:0000269|PubMed:7092800,
ECO:0000269|Ref.9}.
HELIX 6 17 {ECO:0000244|PDB:3HRW}.
HELIX 19 21 {ECO:0000244|PDB:3HRW}.
HELIX 22 36 {ECO:0000244|PDB:3HRW}.
HELIX 39 43 {ECO:0000244|PDB:3HRW}.
STRAND 45 47 {ECO:0000244|PDB:3HRW}.
HELIX 54 70 {ECO:0000244|PDB:3HRW}.
TURN 78 80 {ECO:0000244|PDB:3HRW}.
HELIX 84 89 {ECO:0000244|PDB:3HRW}.
HELIX 97 113 {ECO:0000244|PDB:3HRW}.
TURN 115 117 {ECO:0000244|PDB:3HRW}.
HELIX 120 137 {ECO:0000244|PDB:3HRW}.
HELIX 138 141 {ECO:0000244|PDB:3HRW}.
SEQUENCE 142 AA; 15085 MW; 2F70043BFF66E24A CRC64;
MVLSGEDKSN IKAAWGKIGG HGAEYGAEAL ERMFASFPTT KTYFPHFDVS HGSAQVKGHG
KKVADALASA AGHLDDLPGA LSALSDLHAH KLRVDPVNFK LLSHCLLVTL ASHHPADFTP
AVHASLDKFL ASVSTVLTSK YR


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