A6NGU5 (GGT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative gamma-glutamyltranspeptidase 3
Short name=GGT 3
EC=2.3.2.2

Alternative name(s):
Gamma-glutamyltransferase 3

Cleaved into the following 2 chains:

1. Putative gamma-glutamyltranspeptidase 3 heavy chain
2. Putative gamma-glutamyltranspeptidase 3 light chain

Gene names

Name:	GGT3P
Synonyms:	GGT3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Uncertain

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

Ontologies

Keywords
Biological process	Glutathione biosynthesis
Cellular component	Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW leukotriene biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	anchored to external side of plasma membrane Traceable author statement Ref.3. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	gamma-glutamyltransferase activity Traceable author statement Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	Putative gamma-glutamyltranspeptidase 3 heavy chain By similarity		PRO_0000334690
	Chain	381 – 568	188	Putative gamma-glutamyltranspeptidase 3 light chain By similarity		PRO_0000334691
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 26	22	Helical; Signal-anchor for type II membrane protein; Probable
	Topological domain	27 – 568	542	Extracellular Potential
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Glycosylation	230	1	N-linked (GlcNAc...) Potential
	Glycosylation	266	1	N-linked (GlcNAc...) Potential
	Glycosylation	297	1	N-linked (GlcNAc...) Potential
	Glycosylation	344	1	N-linked (GlcNAc...) Potential
	Glycosylation	510	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	A6NGU5 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 48BF7C2A2DFEF165	FASTA	568	61,502
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 10591208] [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: 14642999] [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: 18357469] [Abstract] Cited for: IDENTIFICATION, NOMENCLATURE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC008132 Genomic DNA. No translation available.
IPI	IPI00788054.
UniGene	Hs.595809.
3D structure databases
ProteinModelPortal	A6NGU5.
SMR	A6NGU5. Positions 35-568.
ModBase	Search...
Protein-protein interaction databases
STRING	A6NGU5.
Proteomic databases
PRIDE	A6NGU5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000401924; ENSP00000385721; ENSG00000133475. ENST00000402582; ENSP00000384349; ENSG00000133475. ENST00000424627; ENSP00000402035; ENSG00000133475.
Organism-specific databases
GeneCards	GC22M018765.
H-InvDB	HIX0041197.
HGNC	HGNC:4252. GGT3P.
neXtProt	NX_A6NGU5.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG005835.
InParanoid	A6NGU5.
PhylomeDB	A6NGU5.
Gene expression databases
Bgee	A6NGU5.
Genevestigator	A6NGU5.
Family and domain databases
InterPro	IPR000101. GGT_peptidase. [Graphical view]
PANTHER	PTHR11686. GGT_peptidase. 1 hit.
Pfam	PF01019. G_glu_transpept. 1 hit. [Graphical view]
PRINTS	PR01210. GGTRANSPTASE.
TIGRFAMs	TIGR00066. G_glut_trans. 1 hit.
PROSITE	PS00462. G_GLU_TRANSPEPTIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GGT3_HUMAN

Accession

Primary (citable) accession number: A6NGU5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	January 15, 2008
Last modified:	November 16, 2011
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.