HBA_RAT
ID HBA_RAT Reviewed; 142 AA.
AC P01946; P33583; Q63243; Q80XV2; Q91V15;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Hemoglobin subunit alpha-1/2;
DE AltName: Full=Alpha-1/2-globin;
DE AltName: Full=Hemoglobin alpha-1/2 chain;
DE Contains:
DE RecName: Full=Hemopressin {ECO:0000303|PubMed:12500972};
GN Name=Hba1; Synonyms=Hba-a1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP PROTEIN SEQUENCE (ALPHA-1).
RX PubMed=1191258; DOI=10.1042/bj1490259;
RA Chua C.G., Carrell R.W., Howard B.H.;
RT "The amino acid sequence of the alpha chain of the major haemoglobin of the
RT rat (Rattus norvegicus).";
RL Biochem. J. 149:259-269(1975).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ALPHA-1).
RX PubMed=3619896; DOI=10.1016/0006-291x(87)90573-0;
RA Satoh H., Fujii H., Okazaki T.;
RT "Molecular cloning and sequence analysis of two rat major globin cDNAs.";
RL Biochem. Biophys. Res. Commun. 146:618-624(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-6.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=10196478; DOI=10.1016/s0378-1119(99)00055-4;
RA Satoh H., Inokuchi N., Nagae Y., Okazaki T.;
RT "Molecular cloning and characterization of two sets of alpha-theta genes in
RT the rat alpha-like globin gene cluster.";
RL Gene 230:91-99(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-2).
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RA Ma C.W., Cheng L.Y.L., Lam V.M.S.;
RT "Cloning and characterisation of a rat alpha-globin gene.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-6.
RC TISSUE=Pituitary, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL PROTEIN SEQUENCE (ALPHA-1 AND -2).
RX PubMed=242324; DOI=10.1042/bj1490245;
RA Garrick L.M., Sharma V.S., McDonald M.J., Ranney H.M.;
RT "Rat haemoglobin heterogeneity. Two structurally distinct alpha chains and
RT functional behaviour of selected components.";
RL Biochem. J. 149:245-258(1975).
RN [7]
RP PARTIAL PROTEIN SEQUENCE (ALPHA-1).
RX PubMed=4676390;
RA Brdicka R., Massa A., Carta S., Tentori L., Vivaldi G.;
RT "Partial amino acid sequence of some tryptic peptides of the alpha-1 chain
RT of Rattus norvegicus hemoglobin.";
RL Life Sci. 11:895-899(1972).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89, AND VARIANT ALPHA-2 ALA-6.
RC STRAIN=Sprague-Dawley;
RX PubMed=8226096; DOI=10.3109/03630269308997489;
RA Lam V.M., Gu Y.L., Au D.M., Wong W.M., Ma C.W., Cheng L.Y.;
RT "Two new rat alpha-globin sequences as identified by the conserved region
RT PCR.";
RL Hemoglobin 17:363-371(1993).
RN [9]
RP PROTEIN SEQUENCE OF 2-36.
RC TISSUE=Brown adipose tissue;
RX PubMed=8334153; DOI=10.1016/0005-2760(93)90084-m;
RA Dutta-Roy A.K., Huang Y., Dunbar B., Trayhurn P.;
RT "Purification and characterization of fatty acid-binding proteins from
RT brown adipose tissue of the rat.";
RL Biochim. Biophys. Acta 1169:73-79(1993).
RN [10]
RP PROTEIN SEQUENCE OF 2-12; 18-57; 70-100 AND 129-140, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 76-92 AND 95-141.
RX PubMed=6098570; DOI=10.3109/03630268408991745;
RA Crkvenjakov R., Bucan M., Konstantinovic M., Fogel M., Savic A., Glisin V.;
RT "Characterization of two rat globin cDNA clones.";
RL Hemoglobin 8:597-611(1984).
RN [12]
RP PROTEIN SEQUENCE OF 96-104 (HEMOPRESSIN).
RX PubMed=12500972; DOI=10.1074/jbc.m212030200;
RA Rioli V., Gozzo F.C., Heimann A.S., Linardi A., Krieger J.E., Shida C.S.,
RA Almeida P.C., Hyslop S., Eberlin M.N., Ferro E.S.;
RT "Novel natural peptide substrates for endopeptidase 24.15, neurolysin, and
RT angiotensin-converting enzyme.";
RL J. Biol. Chem. 278:8547-8555(2003).
RN [13]
RP FUNCTION (HEMOPRESSIN).
RX PubMed=18077343; DOI=10.1073/pnas.0706980105;
RA Heimann A.S., Gomes I., Dale C.S., Pagano R.L., Gupta A., de Souza L.L.,
RA Luchessi A.D., Castro L.M., Giorgi R., Rioli V., Ferro E.S., Devi L.A.;
RT "Hemopressin is an inverse agonist of CB1 cannabinoid receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:20588-20593(2007).
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 (PubMed:18077343). Hemopressin-binding
CC efficiently blocks cannabinoid receptor CNR1 and subsequent signaling
CC (PubMed:18077343). {ECO:0000269|PubMed:18077343}.
CC -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC -!- TISSUE SPECIFICITY: Red blood cells.
CC -!- MISCELLANEOUS: In rats there are two non-allelic alpha chains and two
CC non-allelic beta chains. The alpha-1 chain sequence is shown.
CC -!- SIMILARITY: Belongs to the globin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00238}.
CC -!- CAUTION: PubMed:8334153 incorrectly assigned their sequence fragment as
CC a fatty acid-binding protein. {ECO:0000305}.
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DR EMBL; M17083; AAA41308.1; -; mRNA.
DR EMBL; X56325; CAA39764.1; -; Genomic_DNA.
DR EMBL; X65495; CAA46476.1; -; Genomic_DNA.
DR EMBL; U29528; AAA99054.1; -; Genomic_DNA.
DR EMBL; BC059150; AAH59150.1; -; mRNA.
DR EMBL; BC091567; AAH91567.1; -; mRNA.
DR EMBL; S66657; AAP13984.1; -; Genomic_DNA.
DR EMBL; M32510; AAA41315.1; -; mRNA.
DR PIR; I54239; HART1.
DR RefSeq; NP_001007723.1; NM_001007722.1.
DR RefSeq; NP_037228.1; NM_013096.1.
DR PDB; 3DHT; X-ray; 2.98 A; A=2-142.
DR PDB; 3HF4; X-ray; 2.70 A; A/E=2-142.
DR PDBsum; 3DHT; -.
DR PDBsum; 3HF4; -.
DR AlphaFoldDB; P01946; -.
DR SMR; P01946; -.
DR BioGRID; 247661; 3.
DR BioGRID; 261987; 2.
DR ComplexPortal; CPX-2925; Hemoglobin HbA complex, variant HBB1.
DR ComplexPortal; CPX-2926; Hemoglobin HbA complex, variant HBB2.
DR IntAct; P01946; 2.
DR STRING; 10116.ENSRNOP00000044233; -.
DR CarbonylDB; P01946; -.
DR iPTMnet; P01946; -.
DR PhosphoSitePlus; P01946; -.
DR jPOST; P01946; -.
DR PaxDb; P01946; -.
DR PRIDE; P01946; -.
DR GeneID; 25632; -.
DR GeneID; 360504; -.
DR KEGG; rno:25632; -.
DR KEGG; rno:360504; -.
DR UCSC; RGD:2782; rat.
DR CTD; 110257; -.
DR CTD; 15122; -.
DR RGD; 2782; Hba1.
DR VEuPathDB; HostDB:ENSRNOG00000029886; -.
DR eggNOG; KOG3378; Eukaryota.
DR HOGENOM; CLU_003827_10_2_1; -.
DR InParanoid; P01946; -.
DR OMA; MYFPAEF; -.
DR OrthoDB; 1398217at2759; -.
DR PhylomeDB; P01946; -.
DR TreeFam; TF332328; -.
DR Reactome; R-RNO-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-RNO-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-RNO-2168880; Scavenging of heme from plasma.
DR Reactome; R-RNO-9707564; Cytoprotection by HMOX1.
DR Reactome; R-RNO-9707616; Heme signaling.
DR EvolutionaryTrace; P01946; -.
DR PRO; PR:P01946; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000029886; Expressed in spleen and 18 other tissues.
DR ExpressionAtlas; P01946; baseline and differential.
DR Genevisible; P01946; RN.
DR GO; GO:0031838; C:haptoglobin-hemoglobin complex; IBA:GO_Central.
DR GO; GO:0005833; C:hemoglobin complex; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:UniProtKB.
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:0015670; P:carbon dioxide transport; IC:ComplexPortal.
DR GO; GO:0098869; P:cellular oxidant detoxification; IEA:GOC.
DR GO; GO:0048821; P:erythrocyte development; ISO:RGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IDA:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR GO; GO:0035634; P:response to stilbenoid; ISO:RGD.
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:8334153, ECO:0000269|Ref.10"
FT CHAIN 2..142
FT /note="Hemoglobin subunit alpha-1/2"
FT /id="PRO_0000052751"
FT PEPTIDE 96..104
FT /note="Hemopressin"
FT /evidence="ECO:0000269|PubMed:12500972"
FT /id="PRO_0000455938"
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 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P69905"
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 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 132
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 6
FT /note="D -> A (in alpha-2)"
FT /evidence="ECO:0000269|PubMed:10196478,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8226096"
FT VARIANT 45
FT /note="S -> N"
FT CONFLICT 21
FT /note="H -> S (in Ref. 9; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 71..79
FT /note="ADHVEDLPG -> GAHLBBVPZ (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:3HF4"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 96..113
FT /evidence="ECO:0007829|PDB:3HF4"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3HF4"
FT HELIX 120..137
FT /evidence="ECO:0007829|PDB:3HF4"
SQ SEQUENCE 142 AA; 15329 MW; DEF6857594C42A99 CRC64;
MVLSADDKTN IKNCWGKIGG HGGEYGEEAL QRMFAAFPTT KTYFSHIDVS PGSAQVKAHG
KKVADALAKA ADHVEDLPGA LSTLSDLHAH KLRVDPVNFK FLSHCLLVTL ACHHPGDFTP
AMHASLDKFL ASVSTVLTSK YR
