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Protein

Hemoglobin subunit alpha-1/2

Gene

Hba1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in oxygen transport from the lung to the various peripheral tissues.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi59 – 591Iron (heme distal ligand)
Metal bindingi88 – 881Iron (heme proximal ligand)

GO - Molecular functioni

GO - Biological processi

  • negative regulation of blood pressure Source: RGD
  • regulation of sensory perception of pain Source: RGD
Complete GO annotation...

Keywords - Biological processi

Oxygen transport, Transport

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-RNO-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-RNO-2168880. Scavenging of heme from plasma.

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin subunit alpha-1/2
Alternative name(s):
Alpha-1/2-globin
Hemoglobin alpha-1/2 chain
Gene namesi
Name:Hba1
Synonyms:Hba-a1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2782. Hba1.

Subcellular locationi

GO - Cellular componenti

  • hemoglobin complex Source: InterPro
  • synapse Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 142141Hemoglobin subunit alpha-1/2PRO_0000052751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei8 – 81N6-succinyllysineBy similarity
Modified residuei9 – 91PhosphothreonineBy similarity
Modified residuei12 – 121N6-succinyllysineBy similarity
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-succinyllysine; alternateBy similarity
Modified residuei25 – 251PhosphotyrosineBy similarity
Modified residuei41 – 411N6-succinyllysineBy similarity
Modified residuei50 – 501PhosphoserineBy similarity
Modified residuei103 – 1031PhosphoserineBy similarity
Modified residuei109 – 1091PhosphothreonineBy similarity
Modified residuei125 – 1251PhosphoserineBy similarity
Modified residuei132 – 1321PhosphoserineBy similarity
Modified residuei135 – 1351PhosphothreonineBy similarity
Modified residuei138 – 1381PhosphothreonineBy similarity
Modified residuei139 – 1391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP01946.
PRIDEiP01946.

PTM databases

iPTMnetiP01946.
PhosphoSiteiP01946.

Expressioni

Tissue specificityi

Red blood cells.

Gene expression databases

ExpressionAtlasiP01946. baseline.
GenevisibleiP01946. RN.

Interactioni

Subunit structurei

Heterotetramer of two alpha chains and two beta chains.

Protein-protein interaction databases

BioGridi247661. 1 interaction.
261987. 1 interaction.
IntActiP01946. 1 interaction.
STRINGi10116.ENSRNOP00000044233.

Structurei

Secondary structure

1
142
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Helixi19 – 213Combined sources
Helixi22 – 3615Combined sources
Helixi38 – 447Combined sources
Beta strandi50 – 523Combined sources
Helixi54 – 7219Combined sources
Helixi74 – 763Combined sources
Helixi77 – 804Combined sources
Helixi82 – 898Combined sources
Helixi96 – 11318Combined sources
Turni115 – 1173Combined sources
Helixi120 – 13718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DHTX-ray2.98A2-142[»]
3HF4X-ray2.70A/E2-142[»]
ProteinModelPortaliP01946.
SMRiP01946. Positions 2-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01946.

Family & Domainsi

Sequence similaritiesi

Belongs to the globin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01946.
KOiK13822.
OMAiSKHILAH.
OrthoDBiEOG7KH9MP.
PhylomeDBiP01946.
TreeFamiTF332328.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01946-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLSADDKTN IKNCWGKIGG HGGEYGEEAL QRMFAAFPTT KTYFSHIDVS
60 70 80 90 100
PGSAQVKAHG KKVADALAKA ADHVEDLPGA LSTLSDLHAH KLRVDPVNFK
110 120 130 140
FLSHCLLVTL ACHHPGDFTP AMHASLDKFL ASVSTVLTSK YR
Length:142
Mass (Da):15,329
Last modified:January 23, 2007 - v3
Checksum:iDEF6857594C42A99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211H → S AA sequence (PubMed:8334153).Curated
Sequence conflicti71 – 799ADHVEDLPG → GAHLBBVPZ AA sequence (PubMed:1191258).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61D → A in alpha-2. 3 Publications
Natural varianti45 – 451S → N.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17083 mRNA. Translation: AAA41308.1.
X56325 Genomic DNA. Translation: CAA39764.1.
X65495 Genomic DNA. Translation: CAA46476.1.
U29528 Genomic DNA. Translation: AAA99054.1.
BC059150 mRNA. Translation: AAH59150.1.
BC091567 mRNA. Translation: AAH91567.1.
S66657 Genomic DNA. Translation: AAP13984.1.
M32510 mRNA. Translation: AAA41315.1.
PIRiI54239. HART1.
RefSeqiNP_001007723.1. NM_001007722.1.
NP_037228.1. NM_013096.1.
UniGeneiRn.107334.
Rn.203003.

Genome annotation databases

EnsembliENSRNOT00000051483; ENSRNOP00000044233; ENSRNOG00000029886.
GeneIDi25632.
360504.
KEGGirno:25632.
rno:360504.
UCSCiRGD:2782. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17083 mRNA. Translation: AAA41308.1.
X56325 Genomic DNA. Translation: CAA39764.1.
X65495 Genomic DNA. Translation: CAA46476.1.
U29528 Genomic DNA. Translation: AAA99054.1.
BC059150 mRNA. Translation: AAH59150.1.
BC091567 mRNA. Translation: AAH91567.1.
S66657 Genomic DNA. Translation: AAP13984.1.
M32510 mRNA. Translation: AAA41315.1.
PIRiI54239. HART1.
RefSeqiNP_001007723.1. NM_001007722.1.
NP_037228.1. NM_013096.1.
UniGeneiRn.107334.
Rn.203003.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DHTX-ray2.98A2-142[»]
3HF4X-ray2.70A/E2-142[»]
ProteinModelPortaliP01946.
SMRiP01946. Positions 2-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247661. 1 interaction.
261987. 1 interaction.
IntActiP01946. 1 interaction.
STRINGi10116.ENSRNOP00000044233.

PTM databases

iPTMnetiP01946.
PhosphoSiteiP01946.

Proteomic databases

PaxDbiP01946.
PRIDEiP01946.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000051483; ENSRNOP00000044233; ENSRNOG00000029886.
GeneIDi25632.
360504.
KEGGirno:25632.
rno:360504.
UCSCiRGD:2782. rat.

Organism-specific databases

CTDi3039.
3040.
RGDi2782. Hba1.

Phylogenomic databases

eggNOGiKOG3378. Eukaryota.
COG1018. LUCA.
GeneTreeiENSGT00760000119197.
HOGENOMiHOG000036867.
HOVERGENiHBG009709.
InParanoidiP01946.
KOiK13822.
OMAiSKHILAH.
OrthoDBiEOG7KH9MP.
PhylomeDBiP01946.
TreeFamiTF332328.

Enzyme and pathway databases

ReactomeiR-RNO-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-RNO-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-RNO-2168880. Scavenging of heme from plasma.

Miscellaneous databases

EvolutionaryTraceiP01946.
PROiP01946.

Gene expression databases

ExpressionAtlasiP01946. baseline.
GenevisibleiP01946. RN.

Family and domain databases

Gene3Di1.10.490.10. 1 hit.
InterProiIPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin/Proto.
IPR002338. Haemoglobin_a.
IPR002339. Haemoglobin_pi.
[Graphical view]
PfamiPF00042. Globin. 1 hit.
[Graphical view]
PRINTSiPR00612. ALPHAHAEM.
PR00815. PIHAEM.
SUPFAMiSSF46458. SSF46458. 1 hit.
PROSITEiPS01033. GLOBIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The amino acid sequence of the alpha chain of the major haemoglobin of the rat (Rattus norvegicus)."
    Chua C.G., Carrell R.W., Howard B.H.
    Biochem. J. 149:259-269(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE (ALPHA-1).
  2. "Molecular cloning and sequence analysis of two rat major globin cDNAs."
    Satoh H., Fujii H., Okazaki T.
    Biochem. Biophys. Res. Commun. 146:618-624(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALPHA-1).
  3. "Molecular cloning and characterization of two sets of alpha-theta genes in the rat alpha-like globin gene cluster."
    Satoh H., Inokuchi N., Nagae Y., Okazaki T.
    Gene 230:91-99(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ALA-6.
    Strain: Wistar.
    Tissue: Liver.
  4. "Cloning and characterisation of a rat alpha-globin gene."
    Ma C.W., Cheng L.Y.L., Lam V.M.S.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALPHA-2).
    Strain: Sprague-Dawley.
    Tissue: Liver.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-6.
    Tissue: Pituitary and Placenta.
  6. "Rat haemoglobin heterogeneity. Two structurally distinct alpha chains and functional behaviour of selected components."
    Garrick L.M., Sharma V.S., McDonald M.J., Ranney H.M.
    Biochem. J. 149:245-258(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE (ALPHA-1 AND -2).
  7. "Partial amino acid sequence of some tryptic peptides of the alpha-1 chain of Rattus norvegicus hemoglobin."
    Brdicka R., Massa A., Carta S., Tentori L., Vivaldi G.
    Life Sci. 11:895-899(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE (ALPHA-1).
  8. "Two new rat alpha-globin sequences as identified by the conserved region PCR."
    Lam V.M., Gu Y.L., Au D.M., Wong W.M., Ma C.W., Cheng L.Y.
    Hemoglobin 17:363-371(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89, VARIANT ALPHA-2 ALA-6.
    Strain: Sprague-Dawley.
  9. "Purification and characterization of fatty acid-binding proteins from brown adipose tissue of the rat."
    Dutta-Roy A.K., Huang Y., Dunbar B., Trayhurn P.
    Biochim. Biophys. Acta 1169:73-79(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-36.
    Tissue: Brown adipose tissue.
  10. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 18-57; 70-100 AND 129-140, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  11. "Characterization of two rat globin cDNA clones."
    Crkvenjakov R., Bucan M., Konstantinovic M., Fogel M., Savic A., Glisin V.
    Hemoglobin 8:597-611(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-92 AND 95-141.

Entry informationi

Entry nameiHBA_RAT
AccessioniPrimary (citable) accession number: P01946
Secondary accession number(s): P33583
, Q63243, Q80XV2, Q91V15
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In rats there are two non-allelic alpha chains and two non-allelic beta chains. The alpha-1 chain sequence is shown.

Caution

PubMed:8334153 incorrectly assigned their sequence fragment as a fatty acid-binding protein.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.