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Q5PQT3 (GLYAT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Glycine N-acyltransferase

EC=2.3.1.13
EC=2.3.1.71
Alternative name(s):
Acyl-CoA:glycine N-acyltransferase
Short name=AAc
Aralkyl acyl-CoA N-acyltransferase
Aralkyl acyl-CoA:amino acid N-acyltransferase
Benzoyl-coenzyme A:glycine N-acyltransferase
Glycine N-benzoyltransferase
Liver regeneration-related protein LRRG067
Gene names
Name:Glyat
ORF Names:Ab2-132
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Mitochondrial acyltransferase which transfers an acyl group to the N-terminus of glycine and glutamine, although much less efficiently. Can conjugate a multitude of substrates to form a variety of N-acylglycines, thereby detoxify xenobiotics, such as benzoic acid or salicylic acid, and endogenous organic acids, such as isovaleric acid By similarity.

Catalytic activity

Acyl-CoA + glycine = CoA + N-acylglycine.

Benzoyl-CoA + glycine = CoA + hippurate.

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the glycine N-acyltransferase family.

Sequence caution

The sequence AAP92593.1 differs from that shown. Reason: Intron retention.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 296296Glycine N-acyltransferase
PRO_0000281872

Amino acid modifications

Modified residue161N6-acetyllysine; alternate By similarity
Modified residue161N6-succinyllysine; alternate By similarity
Modified residue1131N6-acetyllysine By similarity
Modified residue1271N6-acetyllysine; alternate By similarity
Modified residue1271N6-succinyllysine; alternate By similarity
Modified residue1421N6-acetyllysine; alternate By similarity
Modified residue1421N6-succinyllysine; alternate By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue1691N6-succinyllysine By similarity
Modified residue1831N6-acetyllysine; alternate By similarity
Modified residue1831N6-succinyllysine; alternate By similarity
Modified residue2561N6-acetyllysine; alternate By similarity
Modified residue2561N6-succinyllysine; alternate By similarity
Modified residue2671N6-succinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5PQT3 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: A559056779671ABB

FASTA29633,899
        10         20         30         40         50         60 
MIVPLQGAQM LQMLEKSLKK YLPESLKVYG TIYHVNHGNP FNLKALVDKW PDFNTVVVRP 

        70         80         90        100        110        120 
QEQEMKDDLD FYTNTYQIYS KDPENCQEFL GSSEVINWKQ HLQIQSSQSH LNKAIQNLAS 

       130        140        150        160        170        180 
IHSLQVKHSE NILYVVSETV RKLFPSLLDT KNLSPGSGKP KAINQEMFKL SSLDVTHAAL 

       190        200        210        220        230        240 
VNKFWLFGGN ERSQRFIERC IKNFPSSCVL GPEGTPASWT LMDQTGEMRM GGTVPQYRAQ 

       250        260        270        280        290 
GLVSFVIYSQ DQIMKKRGFP VYSHTDKSNT VMQKMSYSLQ HLPMPCAWNQ WICVPM 

« Hide

References

[1]"Liver regeneration after PH."
Xu C.S., Chang C.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J., Zhao L.F., Ma H., Wang L., Wang S.F., Xing X.K., Shen G.M., Shi J.B., Rahman S., Wang Q.N., Zhang J.B.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE 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: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY325192 mRNA. Translation: AAP92593.1. Sequence problems.
BC087043 mRNA. Translation: AAH87043.1.
RefSeqNP_001009648.1. NM_001009648.2.
XP_006231183.1. XM_006231121.1.
XP_006231184.1. XM_006231122.1.
XP_006231185.1. XM_006231123.1.
UniGeneRn.21872.

3D structure databases

ProteinModelPortalQ5PQT3.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ5PQT3.

Proteomic databases

PaxDbQ5PQT3.
PRIDEQ5PQT3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016454; ENSRNOP00000016454; ENSRNOG00000012142.
GeneID293779.
KEGGrno:293779.
UCSCRGD:1307163. rat.

Organism-specific databases

CTD10249.
RGD1307163. Glyat.

Phylogenomic databases

eggNOGNOG48018.
GeneTreeENSGT00390000004997.
HOGENOMHOG000263599.
HOVERGENHBG107953.
KOK00628.
OMAFPVYSHV.
OrthoDBEOG7MKW6X.
PhylomeDBQ5PQT3.
TreeFamTF353258.

Gene expression databases

GenevestigatorQ5PQT3.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR010313. Glycine_N-acyltransferase.
IPR013652. Glycine_N-acyltransferase_C.
IPR015938. Glycine_N-acyltransferase_N.
[Graphical view]
PANTHERPTHR15298. PTHR15298. 1 hit.
PfamPF08444. Gly_acyl_tr_C. 1 hit.
PF06021. Gly_acyl_tr_N. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

NextBio636988.
PROQ5PQT3.

Entry information

Entry nameGLYAT_RAT
AccessionPrimary (citable) accession number: Q5PQT3
Secondary accession number(s): Q7TP56
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 70 of the entry and version 1 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