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P13264 (GLSK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glutaminase kidney isoform, mitochondrial
Short name=GLS
EC=3.5.1.2
Alternative name(s):
K-glutaminase
L-glutamine amidohydrolase

Cleaved into the following 2 chains:

  1. Glutaminase kidney isoform 68 kDa chain
  2. Glutaminase kidney isoform 65 kDa chain
Gene names
Name:Gls
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length674 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 first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate in the brain.

Catalytic activity

L-glutamine + H2O = L-glutamate + NH3.

Subunit structure

Homotetramer. Tetramer composed of 68 and 65 kDa peptides in a 1:3 ratio. Interacts with ATCAY; the interaction is direct and may control GLS localization, negatively regulating its activity. Ref.6

Subcellular location

Isoform 1: Cytoplasm › cytosol By similarity.

Isoform 2: Mitochondrion.

Tissue specificity

Kidney, brain, and intestine.

Sequence similarities

Belongs to the glutaminase family.

Contains 2 ANK repeats.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P13264-1)

Also known as: KGA;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P13264-2)

Also known as: GAC;

The sequence of this isoform differs from the canonical sequence as follows:
     556-674: VKSVINLLFA...TVHKNLDGLL → HSFGPLDYES...YRMESLGERS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1616Mitochondrion
Chain17 – 674658Glutaminase kidney isoform 68 kDa chain
PRO_0000011623
Chain73 – 674602Glutaminase kidney isoform 65 kDa chain
PRO_0000011624

Regions

Repeat590 – 61930ANK 1
Repeat624 – 65330ANK 2
Compositional bias91 – 999Poly-Gln

Sites

Binding site2911Substrate By similarity
Binding site3401Substrate By similarity
Binding site3861Substrate By similarity
Binding site3931Substrate By similarity
Binding site4191Substrate By similarity
Binding site4711Substrate By similarity
Binding site4891Substrate; via amide nitrogen By similarity

Amino acid modifications

Modified residue3161N6-acetyllysine By similarity

Natural variations

Alternative sequence556 – 674119VKSVI…LDGLL → HSFGPLDYESLQQELALKDT VWKKVSPESSDDTSTTIVYR MESLGERS in isoform 2.
VSP_041992

Experimental info

Sequence conflict281T → A in AAG30873. Ref.2
Sequence conflict349 – 3513LIK → EFG in AAA41234. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (KGA) [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: 4B2524A45D3678CA

FASTA67474,024
        10         20         30         40         50         60 
MMRLRGSAML RELLLRPPAA VGGVLRRTQP LGTLCRRPRG GSRPAAGLVA AARLHPWWGG 

        70         80         90        100        110        120 
GGRAKGPGSG GLSSSPSEIL QELGKGGTPP QQQQQQQQQP GASPPAAPGP KDSPGETDAF 

       130        140        150        160        170        180 
GNSEGKEMVA AGDNKVKQGL LPSLEDLLFY TIAEGQEKIP VHKFITALKS TGLRTSDPRL 

       190        200        210        220        230        240 
KECMDMLRLT LQTTSDGVML DKDLFKKCVQ SNIVLLTQAF RRKFVIPDFM SFTSHIDELY 

       250        260        270        280        290        300 
ESAKKQSGGK VADYIPQLAK FSPDLWGVSV CTVDGQRHSI GDTKVPFCLQ SCVKPLKYAI 

       310        320        330        340        350        360 
AVNDLGTEYV HRYVGKEPSG LRFNKLFLNE DDKPHNPMVN AGAIVVTSLI KQGVNNAEKF 

       370        380        390        400        410        420 
DYVMQFLNKM AGNEYVGFSN ATFQSERESG DRNFAIGYYL KEKKCFPEGT DMVGILDFYF 

       430        440        450        460        470        480 
QLCSIEVTCE SASVMAATLA NGGFCPITGE RVLSPEAVRN TLSLMHSCGM YDFSGQFAFH 

       490        500        510        520        530        540 
VGLPAKSGVA GGILLVVPNV MGMMCWSPPL DKMGNSVKGI HFCHDLVSLC NFHNYDNLRH 

       550        560        570        580        590        600 
FAKKLDPRRE GGDQRVKSVI NLLFAAYTGD VSALRRFALS AMDMEQRDYD SRTALHVAAA 

       610        620        630        640        650        660 
EGHVEVVKFL LEACKVNPFP KDRWNNTPMD EALHFGHHDV FKILQEYQVQ YTPQGDSDDG 

       670 
KENQTVHKNL DGLL

« Hide

Isoform 2 (GAC) [UniParc].

Checksum: F4DD80AA26873041
Show »

FASTA60365,997

References

[1]"Isolation, characterization, and in vitro expression of a cDNA that encodes the kidney isoenzyme of the mitochondrial glutaminase."
Shapiro R.A., Farrell L., Srinivasan M., Curthoys N.P.
J. Biol. Chem. 266:18792-18796(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 73-90.
Strain: Sprague-Dawley.
Tissue: Kidney.
[2]"Isolation and characterization of the promoter region of the rat kidney-type glutaminase gene."
Taylor L., Liu X., Newsome W., Shapiro R.A., Srinivasan M., Curthoys N.P.
Biochim. Biophys. Acta 1518:132-136(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-133.
Strain: Sprague-Dawley.
[3]"Complexity and species variation of the kidney-type glutaminase gene."
Porter L.D., Ibrahim H., Taylor L., Curthoys N.P.
Physiol. Genomics 9:157-166(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-674 (ISOFORM 2).
[4]"Isolation of a cDNA for rat brain glutaminase."
Banner C., Hwang J.-J., Shapiro R.A., Wenthold R.J., Nakatani Y., Lample K.A., Thomas J.W., Huie D., Curthoys N.P.
Brain Res. 427:247-254(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 349-651 (ISOFORM 1).
Tissue: Brain.
[5]"Biosynthesis and processing of mitochondrial glutaminase in HTC hepatoma cells."
Perera S.Y., Voith D.M., Curthoys N.P.
Biochem. J. 273:265-270(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[6]"Brain-specific BNIP-2-homology protein Caytaxin relocalises glutaminase to neurite terminals and reduces glutamate levels."
Buschdorf J.P., Li Chew L., Zhang B., Cao Q., Liang F.Y., Liou Y.C., Zhou Y.T., Low B.C.
J. Cell Sci. 119:3337-3350(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ATCAY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M65150 mRNA. Translation: AAA41247.1.
AF302091 Genomic DNA. Translation: AAG30873.1.
AY083459 mRNA. Translation: AAM00020.1.
M22586 mRNA. Translation: AAA41234.1.
IPIIPI00199465.
PIRA41009.
RefSeqNP_001103438.1. NM_001109968.1.
NP_036701.2. NM_012569.2.
UniGeneRn.5762.

3D structure databases

ProteinModelPortalP13264.
SMRP13264. Positions 227-536.
ModBaseSearch...

Protein-protein interaction databases

IntActP13264. 1 interaction.
STRING10116.ENSRNOP00000063176.

PTM databases

PhosphoSiteP13264.

Proteomic databases

PaxDbP13264.
PRIDEP13264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24398.
KEGGrno:24398.
UCSCRGD:2707. rat.

Organism-specific databases

CTD2744.
RGD2707. Gls.

Phylogenomic databases

eggNOGCOG2066.
HOGENOMHOG000216891.
HOVERGENHBG005856.
InParanoidQ8R421.
KOK01425.
OrthoDBEOG4ZS92W.

Enzyme and pathway databases

SABIO-RKP13264.

Gene expression databases

ArrayExpressP13264.
GenevestigatorP13264.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
3.40.710.10. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR012338. Beta-lactam/transpept-like.
IPR015868. Glutaminase.
[Graphical view]
PANTHERPTHR12544. PTHR12544. 1 hit.
PfamPF00023. Ank. 1 hit.
PF04960. Glutaminase. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
SSF56601. PBP_transp_fold. 1 hit.
TIGRFAMsTIGR03814. Gln_ase. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603191.

Entry information

Entry nameGLSK_RAT
AccessionPrimary (citable) accession number: P13264
Secondary accession number(s): Q8R421
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: December 1, 1992
Last modified: April 3, 2013
This is version 113 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

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