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A6NGU5 (GGT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Putative gamma-glutamyltranspeptidase 3

Short name=GGT 3
EC=2.3.2.2
Alternative name(s):
Gamma-glutamyltransferase 3
Glutathione hydrolase 3
EC=3.4.19.13
Gene names
Name:GGT3P
Synonyms:GGT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length568 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceUncertain

General annotation (Comments)

Function

Initiates extracellular glutathione (GSH) breakdown; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors By similarity.

Catalytic activity

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.

Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Pathway

Sulfur metabolism; glutathione metabolism.

Subcellular location

Membrane; Single-pass type II membrane protein By similarity.

Post-translational modification

Cleaved by autocatalysis into a large and a small subunit By similarity.

Miscellaneous

In some epileptic patients treated with phenytoin, phenobarbital and carbamazepin, GGT3 is found, as an additional form of GGT. This group of patients has levels of ceruloplasmin and oxidase activity that were significantly higher than in the group of patients without GGT3. However, levels of ceruloplasmin and oxidase activity are significantly higher in this group of patients without GGT3 than those of the control group.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Caution

Could be the product of a pseudogene. According to Ref.3, it is not functional.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 380380Putative gamma-glutamyltranspeptidase 3 heavy chain By similarity
PRO_0000334690
Chain381 – 568188Putative gamma-glutamyltranspeptidase 3 light chain By similarity
PRO_0000334691

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2622Helical; Signal-anchor for type II membrane protein; Probable
Topological domain27 – 568542Extracellular Potential
Region450 – 4512Glutamate binding By similarity

Sites

Active site3811Nucleophile By similarity
Binding site1071Glutamate By similarity
Binding site3991Glutamate By similarity

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation2661N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3441N-linked (GlcNAc...) Potential
Glycosylation5101N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A6NGU5 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 48BF7C2A2DFEF165

FASTA56861,502
        10         20         30         40         50         60 
MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC LEIGRDTLRD 

        70         80         90        100        110        120 
GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTRK AEVINAREVA PRLAFASMFN 

       130        140        150        160        170        180 
SSEQSQKGGL SVAVPGEIRG YELAHQRHGR LPWARLFQPS IQLARQGFPV GKGLAAVLEN 

       190        200        210        220        230        240 
KRTVIEQQPV LCEVFCRDRK VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD 

       250        260        270        280        290        300 
IQAAGGIVTA EDLNNYCAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR 

       310        320        330        340        350        360 
ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF AAQLRSQISD 

       370        380        390        400        410        420 
HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI NLYFGSKVCS PVSGILFNNM 

       430        440        450        460        470        480 
DDFSSPSITN EFGAPPSPAN FIQPGKQPLL SMCPTIMVGQ DGQVRMVVGA AGGTQITTDT 

       490        500        510        520        530        540 
ALAIIYNLWF GYDVKRAVEE PRLHNKLLPN VTTVERNIDQ AVTAALETRH HHTQIASTFI 

       550        560 
AVVQAIVRTA GGWAAASDSR KGGEPAGY 

« Hide

References

« Hide 'large scale' references
[1]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Assessment of copper status in epileptic patients treated with anticonvulsant drugs by measuring the specific oxidase activity of ceruloplasmin."
Tutor-Crespo M.J., Hermida J., Tutor J.C.
Epilepsy Res. 56:147-153(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EPILEPSY.
[3]"The human gamma-glutamyltransferase gene family."
Heisterkamp N., Groffen J., Warburton D., Sneddon T.P.
Hum. Genet. 123:321-332(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, NOMENCLATURE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC008132 Genomic DNA. No translation available.
UniGeneHs.595809.

3D structure databases

ProteinModelPortalA6NGU5.
SMRA6NGU5. Positions 33-375, 381-568.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEA6NGU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GeneCardsGC22M018765.
HGNCHGNC:4252. GGT3P.
HPAHPA045635.
neXtProtNX_A6NGU5.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG005835.
InParanoidA6NGU5.
PhylomeDBA6NGU5.

Enzyme and pathway databases

UniPathwayUPA00204.

Gene expression databases

GenevestigatorA6NGU5.

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
PANTHERPTHR11686. PTHR11686. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
TIGRFAMsTIGR00066. g_glut_trans. 1 hit.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGGT3_HUMAN
AccessionPrimary (citable) accession number: A6NGU5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: March 19, 2014
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM