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Protein

Putative gamma-glutamyltranspeptidase 3

Gene

GGT3P

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein uncertaini

Functioni

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

Catalytic activityi

A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid.
Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071GlutamateBy similarity
Active sitei381 – 3811NucleophileBy similarity
Binding sitei399 – 3991GlutamateBy similarity

GO - Molecular functioni

  • gamma-glutamyltransferase activity Source: UniProtKB
  • glutathione hydrolase activity Source: UniProtKB-EC

GO - Biological processi

  • glutathione biosynthetic process Source: UniProtKB-KW
  • glutathione metabolic process Source: UniProtKB
  • leukotriene biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis

Enzyme and pathway databases

ReactomeiREACT_264461. Aflatoxin activation and detoxification.
REACT_6960. Glutathione synthesis and recycling.
UniPathwayiUPA00204.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative gamma-glutamyltranspeptidase 3 (EC:2.3.2.2)
Short name:
GGT 3
Alternative name(s):
Gamma-glutamyltransferase 3
Glutathione hydrolase 3 (EC:3.4.19.13)
Cleaved into the following 2 chains:
Gene namesi
Name:GGT3P
Synonyms:GGT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:4252. GGT3P.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2622Helical; Signal-anchor for type II membrane proteinCuratedAdd
BLAST
Topological domaini27 – 568542ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • anchored component of external side of plasma membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380Putative gamma-glutamyltranspeptidase 3 heavy chainBy similarityPRO_0000334690Add
BLAST
Chaini381 – 568188Putative gamma-glutamyltranspeptidase 3 light chainBy similarityPRO_0000334691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

PRIDEiA6NGU5.

Expressioni

Gene expression databases

GenevestigatoriA6NGU5.

Organism-specific databases

HPAiHPA045635.
HPA047534.

Structurei

3D structure databases

ProteinModelPortaliA6NGU5.
SMRiA6NGU5. Positions 33-375, 381-568.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni450 – 4512Glutamate bindingBy similarity

Sequence similaritiesi

Belongs to the gamma-glutamyltransferase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG005835.
InParanoidiA6NGU5.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A6NGU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC
60 70 80 90 100
LEIGRDTLRD GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTRK
110 120 130 140 150
AEVINAREVA PRLAFASMFN SSEQSQKGGL SVAVPGEIRG YELAHQRHGR
160 170 180 190 200
LPWARLFQPS IQLARQGFPV GKGLAAVLEN KRTVIEQQPV LCEVFCRDRK
210 220 230 240 250
VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD IQAAGGIVTA
260 270 280 290 300
EDLNNYCAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR
310 320 330 340 350
ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF
360 370 380 390 400
AAQLRSQISD HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI
410 420 430 440 450
NLYFGSKVCS PVSGILFNNM DDFSSPSITN EFGAPPSPAN FIQPGKQPLL
460 470 480 490 500
SMCPTIMVGQ DGQVRMVVGA AGGTQITTDT ALAIIYNLWF GYDVKRAVEE
510 520 530 540 550
PRLHNKLLPN VTTVERNIDQ AVTAALETRH HHTQIASTFI AVVQAIVRTA
560
GGWAAASDSR KGGEPAGY
Length:568
Mass (Da):61,502
Last modified:January 15, 2008 - v2
Checksum:i48BF7C2A2DFEF165
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008132 Genomic DNA. No translation available.
UniGeneiHs.595809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC008132 Genomic DNA. No translation available.
UniGeneiHs.595809.

3D structure databases

ProteinModelPortaliA6NGU5.
SMRiA6NGU5. Positions 33-375, 381-568.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiA6NGU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiGC22M018765.
HGNCiHGNC:4252. GGT3P.
HPAiHPA045635.
HPA047534.
neXtProtiNX_A6NGU5.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG005835.
InParanoidiA6NGU5.

Enzyme and pathway databases

UniPathwayiUPA00204.
ReactomeiREACT_264461. Aflatoxin activation and detoxification.
REACT_6960. Glutathione synthesis and recycling.

Gene expression databases

GenevestigatoriA6NGU5.

Family and domain databases

InterProiIPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view]
PANTHERiPTHR11686. PTHR11686. 1 hit.
PfamiPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSiPR01210. GGTRANSPTASE.
SUPFAMiSSF56235. SSF56235. 1 hit.
TIGRFAMsiTIGR00066. g_glut_trans. 1 hit.
PROSITEiPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [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. Cited for: IDENTIFICATION, NOMENCLATURE.

Entry informationi

Entry nameiGGT3_HUMAN
AccessioniPrimary (citable) accession number: A6NGU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 15, 2008
Last modified: May 27, 2015
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Caution

Could be the product of a pseudogene. According to PubMed:18357469, it is not functional.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.