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Hemoglobin subunit alpha-1/2 (Alpha-1/2-globin) (Hemoglobin alpha-1/2 chain)

 HBA_RAT                 Reviewed;         142 AA.
P01946; P33583; Q63243; Q80XV2; Q91V15;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 152.
RecName: Full=Hemoglobin subunit alpha-1/2;
AltName: Full=Alpha-1/2-globin;
AltName: Full=Hemoglobin alpha-1/2 chain;
Name=Hba1; Synonyms=Hba-a1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
PROTEIN SEQUENCE (ALPHA-1).
PubMed=1191258; DOI=10.1042/bj1490259;
Chua C.G., Carrell R.W., Howard B.H.;
"The amino acid sequence of the alpha chain of the major haemoglobin
of the rat (Rattus norvegicus).";
Biochem. J. 149:259-269(1975).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ALPHA-1).
PubMed=3619896; DOI=10.1016/0006-291X(87)90573-0;
Satoh H., Fujii H., Okazaki T.;
"Molecular cloning and sequence analysis of two rat major globin
cDNAs.";
Biochem. Biophys. Res. Commun. 146:618-624(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-6.
STRAIN=Wistar; TISSUE=Liver;
PubMed=10196478; DOI=10.1016/S0378-1119(99)00055-4;
Satoh H., Inokuchi N., Nagae Y., Okazaki T.;
"Molecular cloning and characterization of two sets of alpha-theta
genes in the rat alpha-like globin gene cluster.";
Gene 230:91-99(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-2).
STRAIN=Sprague-Dawley; TISSUE=Liver;
Ma C.W., Cheng L.Y.L., Lam V.M.S.;
"Cloning and characterisation of a rat alpha-globin gene.";
Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-6.
TISSUE=Pituitary, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PARTIAL PROTEIN SEQUENCE (ALPHA-1 AND -2).
PubMed=242324; DOI=10.1042/bj1490245;
Garrick L.M., Sharma V.S., McDonald M.J., Ranney H.M.;
"Rat haemoglobin heterogeneity. Two structurally distinct alpha chains
and functional behaviour of selected components.";
Biochem. J. 149:245-258(1975).
[7]
PARTIAL PROTEIN SEQUENCE (ALPHA-1).
PubMed=4676390;
Brdicka R., Massa A., Carta S., Tentori L., Vivaldi G.;
"Partial amino acid sequence of some tryptic peptides of the alpha-1
chain of Rattus norvegicus hemoglobin.";
Life Sci. 11:895-899(1972).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89, AND VARIANT ALPHA-2 ALA-6.
STRAIN=Sprague-Dawley;
PubMed=8226096; DOI=10.3109/03630269308997489;
Lam V.M., Gu Y.L., Au D.M., Wong W.M., Ma C.W., Cheng L.Y.;
"Two new rat alpha-globin sequences as identified by the conserved
region PCR.";
Hemoglobin 17:363-371(1993).
[9]
PROTEIN SEQUENCE OF 2-36.
TISSUE=Brown adipose tissue;
PubMed=8334153; DOI=10.1016/0005-2760(93)90084-M;
Dutta-Roy A.K., Huang Y., Dunbar B., Trayhurn P.;
"Purification and characterization of fatty acid-binding proteins from
brown adipose tissue of the rat.";
Biochim. Biophys. Acta 1169:73-79(1993).
[10]
PROTEIN SEQUENCE OF 2-12; 18-57; 70-100 AND 129-140, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-92 AND 95-141.
PubMed=6098570; DOI=10.3109/03630268408991745;
Crkvenjakov R., Bucan M., Konstantinovic M., Fogel M., Savic A.,
Glisin V.;
"Characterization of two rat globin cDNA clones.";
Hemoglobin 8:597-611(1984).
-!- 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.
-!- MISCELLANEOUS: In rats there are two non-allelic alpha chains and
two non-allelic beta chains. The alpha-1 chain sequence is shown.
-!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
ProRule:PRU00238}.
-!- CAUTION: PubMed:8334153 incorrectly assigned their sequence
fragment as a fatty acid-binding protein. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M17083; AAA41308.1; -; mRNA.
EMBL; X56325; CAA39764.1; -; Genomic_DNA.
EMBL; X65495; CAA46476.1; -; Genomic_DNA.
EMBL; U29528; AAA99054.1; -; Genomic_DNA.
EMBL; BC059150; AAH59150.1; -; mRNA.
EMBL; BC091567; AAH91567.1; -; mRNA.
EMBL; S66657; AAP13984.1; -; Genomic_DNA.
EMBL; M32510; AAA41315.1; -; mRNA.
PIR; I54239; HART1.
RefSeq; NP_001007723.1; NM_001007722.1.
RefSeq; NP_037228.1; NM_013096.1.
UniGene; Rn.107334; -.
UniGene; Rn.203003; -.
PDB; 3DHT; X-ray; 2.98 A; A=2-142.
PDB; 3HF4; X-ray; 2.70 A; A/E=2-142.
PDBsum; 3DHT; -.
PDBsum; 3HF4; -.
ProteinModelPortal; P01946; -.
SMR; P01946; -.
BioGrid; 247661; 1.
BioGrid; 261987; 1.
IntAct; P01946; 1.
STRING; 10116.ENSRNOP00000044233; -.
iPTMnet; P01946; -.
PhosphoSitePlus; P01946; -.
PaxDb; P01946; -.
PRIDE; P01946; -.
Ensembl; ENSRNOT00000051483; ENSRNOP00000044233; ENSRNOG00000029886.
GeneID; 25632; -.
GeneID; 360504; -.
KEGG; rno:25632; -.
KEGG; rno:360504; -.
UCSC; RGD:2782; rat.
CTD; 3039; -.
CTD; 3040; -.
RGD; 2782; Hba1.
eggNOG; KOG3378; Eukaryota.
eggNOG; COG1018; LUCA.
GeneTree; ENSGT00760000119197; -.
HOGENOM; HOG000036867; -.
HOVERGEN; HBG009709; -.
InParanoid; P01946; -.
KO; K13822; -.
OMA; SKHILAH; -.
OrthoDB; EOG091G0S0X; -.
PhylomeDB; P01946; -.
TreeFam; TF332328; -.
Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-RNO-2168880; Scavenging of heme from plasma.
EvolutionaryTrace; P01946; -.
PRO; PR:P01946; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000029886; -.
ExpressionAtlas; P01946; baseline.
Genevisible; P01946; RN.
GO; GO:0072562; C:blood microparticle; ISO:RGD.
GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; ISO:RGD.
GO; GO:0031838; C:haptoglobin-hemoglobin complex; ISO:RGD.
GO; GO:0005833; C:hemoglobin complex; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043209; C:myelin sheath; ISO:RGD.
GO; GO:0045202; C:synapse; IDA:RGD.
GO; GO:0001540; F:amyloid-beta binding; IDA:RGD.
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; ISO:RGD.
GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0045776; P:negative regulation of blood pressure; IDA:RGD.
GO; GO:0010942; P:positive regulation of cell death; ISO:RGD.
GO; GO:0051291; P:protein heterooligomerization; ISO:RGD.
GO; GO:0051930; P:regulation of sensory perception of pain; IDA:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:RGD.
GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
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:8334153,
ECO:0000269|Ref.10}.
CHAIN 2 142 Hemoglobin subunit alpha-1/2.
/FTId=PRO_0000052751.
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:0000250|UniProtKB:P01942}.
MOD_RES 9 9 Phosphothreonine.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 12 12 N6-succinyllysine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 17 17 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 17 17 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 25 25 Phosphotyrosine.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 41 41 N6-succinyllysine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000250|UniProtKB:P69905}.
MOD_RES 103 103 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 109 109 Phosphothreonine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 132 132 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 135 135 Phosphothreonine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 138 138 Phosphothreonine.
{ECO:0000250|UniProtKB:P01942}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P01942}.
VARIANT 6 6 D -> A (in alpha-2).
{ECO:0000269|PubMed:10196478,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8226096}.
VARIANT 45 45 S -> N.
CONFLICT 21 21 H -> S (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 71 79 ADHVEDLPG -> GAHLBBVPZ (in Ref. 1; AA
sequence). {ECO:0000305}.
HELIX 5 18 {ECO:0000244|PDB:3HF4}.
HELIX 19 21 {ECO:0000244|PDB:3HF4}.
HELIX 22 36 {ECO:0000244|PDB:3HF4}.
HELIX 38 44 {ECO:0000244|PDB:3HF4}.
STRAND 50 52 {ECO:0000244|PDB:3HF4}.
HELIX 54 72 {ECO:0000244|PDB:3HF4}.
HELIX 74 76 {ECO:0000244|PDB:3HF4}.
HELIX 77 80 {ECO:0000244|PDB:3HF4}.
HELIX 82 89 {ECO:0000244|PDB:3HF4}.
HELIX 96 113 {ECO:0000244|PDB:3HF4}.
TURN 115 117 {ECO:0000244|PDB:3HF4}.
HELIX 120 137 {ECO:0000244|PDB:3HF4}.
SEQUENCE 142 AA; 15329 MW; DEF6857594C42A99 CRC64;
MVLSADDKTN IKNCWGKIGG HGGEYGEEAL QRMFAAFPTT KTYFSHIDVS PGSAQVKAHG
KKVADALAKA ADHVEDLPGA LSTLSDLHAH KLRVDPVNFK FLSHCLLVTL ACHHPGDFTP
AMHASLDKFL ASVSTVLTSK YR


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