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A6NGU5

- GGT3_HUMAN

UniProt

A6NGU5 - GGT3_HUMAN

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Protein

Putative gamma-glutamyltranspeptidase 3

Gene

GGT3P

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. gamma-glutamyltransferase activity Source: UniProtKB
  2. glutathione hydrolase activity Source: UniProtKB-EC

GO - Biological processi

  1. glutathione biosynthetic process Source: UniProtKB-KW
  2. glutathione metabolic process Source: UniProtKB
  3. leukotriene biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Protease, Transferase

Keywords - Biological processi

Glutathione biosynthesis

Enzyme and pathway databases

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: Unplaced

Organism-specific databases

HGNCiHGNC:4252. GGT3P.

Subcellular locationi

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

GO - Cellular componenti

  1. anchored component of external side of plasma membrane Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. 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.

Structurei

3D structure databases

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

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Topological domaini27 – 568542ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei5 – 2622Helical; Signal-anchor for type II membrane proteinCuratedAdd
BLAST

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:
EMBL
GenBank
DDBJ
Links Updated
AC008132 Genomic DNA. No translation available.
UniGeneiHs.595809.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC008132 Genomic DNA. No translation available.
UniGenei Hs.595809.

3D structure databases

ProteinModelPortali A6NGU5.
SMRi A6NGU5. Positions 33-375, 381-568.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi A6NGU5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

GeneCardsi GC22M018765.
HGNCi HGNC:4252. GGT3P.
HPAi HPA045635.
neXtProti NX_A6NGU5.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG005835.
InParanoidi A6NGU5.

Enzyme and pathway databases

UniPathwayi UPA00204 .

Gene expression databases

Genevestigatori A6NGU5.

Family and domain databases

InterProi IPR000101. GGT_peptidase.
IPR029055. Ntn_hydrolases_N.
[Graphical view ]
PANTHERi PTHR11686. PTHR11686. 1 hit.
Pfami PF01019. G_glu_transpept. 1 hit.
[Graphical view ]
PRINTSi PR01210. GGTRANSPTASE.
SUPFAMi SSF56235. SSF56235. 1 hit.
TIGRFAMsi TIGR00066. g_glut_trans. 1 hit.
PROSITEi PS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 61 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