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P25409 (ALAT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine aminotransferase 1

Short name=ALT1
EC=2.6.1.2
Alternative name(s):
Glutamate pyruvate transaminase 1
Short name=GPT 1
Glutamic--alanine transaminase 1
Glutamic--pyruvic transaminase 1
Gene names
Name:Gpt
Synonyms:Aat1, Gpt1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles By similarity.

Catalytic activity

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Pathway

Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Tissue specificity

Liver, heart, skeletal muscle, etc.

Induction

By glucocorticoids.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. Alanine aminotransferase subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 496495Alanine aminotransferase 1
PRO_0000123936

Amino acid modifications

Modified residue21N-acetylalanine Ref.3
Modified residue3141N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P25409 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7A4714E94146ABF8

FASTA49655,110
        10         20         30         40         50         60 
MASRVNDQSQ ASRNGLKGKV LTLDTMNPCV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF 

        70         80         90        100        110        120 
TEVIRANIGD AQAMGQRPIT FFRQVLALCV YPNLLSSPDF PEDAKRRAER ILQACGGHSL 

       130        140        150        160        170        180 
GAYSISSGIQ PIREDVAQYI ERRDGGIPAD PNNIFLSTGA SDAIVTMLKL LVSGEGRART 

       190        200        210        220        230        240 
GVLIPIPQYP LYSAALAELD AVQVDYYLDE ERAWALDIAE LRRALCQARD RCCPRVLCVI 

       250        260        270        280        290        300 
NPGNPTGQVQ TRECIEAVIR FAFKEGLFLM ADEVYQDNVY AEGSQFHSFK KVLMEMGPPY 

       310        320        330        340        350        360 
STQQELASFH SVSKGYMGEC GFRGGYVEVV NMDAEVQKQM GKLMSVRLCP PVPGQALMDM 

       370        380        390        400        410        420 
VVSPPTPSEP SFKQFQAERQ EVLAELAAKA KLTEQVFNEA PGIRCNPVQG AMYSFPQVQL 

       430        440        450        460        470        480 
PLKAVQRAQE LGLAPDMFFC LCLLEETGIC VVPGSGFGQQ EGTYHFRMTI LPPMEKLRLL 

       490 
LEKLSHFHAK FTHEYS 

« Hide

References

« Hide 'large scale' references
[1]Tanase S.
Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[2]"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].
Tissue: Liver.
[3]"Complete amino acid sequence of rat liver cytosolic alanine aminotransferase."
Ishiguro M., Suzuki M., Takio K., Matsuzawa T., Titani K.
Biochemistry 30:6048-6053(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-496, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10354 mRNA. Translation: BAA01185.1.
BC097937 mRNA. Translation: AAH97937.1.
PIRA39900.
RefSeqNP_112301.1. NM_031039.1.
UniGeneRn.6318.

3D structure databases

ProteinModelPortalP25409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000044411.

Chemistry

ChEMBLCHEMBL3260.

PTM databases

PhosphoSiteP25409.

Proteomic databases

PaxDbP25409.
PRIDEP25409.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000050556; ENSRNOP00000044411; ENSRNOG00000033915.
GeneID81670.
KEGGrno:81670.
UCSCRGD:621720. rat.

Organism-specific databases

CTD2875.
RGD621720. Gpt.

Phylogenomic databases

eggNOGCOG0436.
GeneTreeENSGT00650000093331.
HOGENOMHOG000215020.
HOVERGENHBG026148.
InParanoidP25409.
KOK00814.
OMAHAKFTLE.
OrthoDBEOG76HQ18.
PhylomeDBP25409.
TreeFamTF300839.

Enzyme and pathway databases

SABIO-RKP25409.
UniPathwayUPA00528; UER00586.

Gene expression databases

GenevestigatorP25409.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

NextBio615260.
PROP25409.

Entry information

Entry nameALAT1_RAT
AccessionPrimary (citable) accession number: P25409
Secondary accession number(s): Q4V7F7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways