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Q99JP7

- GGT7_MOUSE

UniProt

Q99JP7 - GGT7_MOUSE

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Protein
Gamma-glutamyltransferase 7
Gene
Ggt7, Ggtl3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Cleaves glutathione conjugates 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

GO - Molecular functioni

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

GO - Biological processi

  1. glutathione biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Hydrolase, Transferase

Keywords - Biological processi

Glutathione biosynthesis

Enzyme and pathway databases

SABIO-RKQ99JP7.
UniPathwayiUPA00204.

Protein family/group databases

MEROPSiT03.017.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-glutamyltransferase 7 (EC:2.3.2.2)
Short name:
GGT 7
Alternative name(s):
Gamma-glutamyltransferase-like 3
Gamma-glutamyltranspeptidase 7
Glutathione hydrolase 7 (EC:3.4.19.13)
Cleaved into the following 2 chains:
Gene namesi
Name:Ggt7
Synonyms:Ggtl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1913385. Ggt7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 106106Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei107 – 12721Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini128 – 662535Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. 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 – 472472Gamma-glutamyltransferase 7 heavy chain By similarity
PRO_0000011068Add
BLAST
Chaini473 – 662190Gamma-glutamyltransferase 7 light chain By similarity
PRO_0000011069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi198 – 1981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi267 – 2671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi283 – 2831N-linked (GlcNAc...) Reviewed prediction
Glycosylationi330 – 3301N-linked (GlcNAc...) Reviewed prediction
Glycosylationi353 – 3531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi394 – 3941N-linked (GlcNAc...) Reviewed prediction
Glycosylationi519 – 5191N-linked (GlcNAc...) Reviewed prediction
Glycosylationi523 – 5231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi586 – 5861N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ99JP7.
PaxDbiQ99JP7.
PRIDEiQ99JP7.

PTM databases

PhosphoSiteiQ99JP7.

Expressioni

Gene expression databases

BgeeiQ99JP7.
CleanExiMM_GGT7.
GenevestigatoriQ99JP7.

Interactioni

Subunit structurei

Heterodimer composed of the light and heavy chains. The active site is located in the light chain. Interacts with FAM57A By similarity.

Protein-protein interaction databases

IntActiQ99JP7. 1 interaction.
MINTiMINT-4096072.

Structurei

3D structure databases

ProteinModelPortaliQ99JP7.
SMRiQ99JP7. Positions 133-655.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0405.
GeneTreeiENSGT00550000074591.
HOGENOMiHOG000231793.
HOVERGENiHBG039468.
InParanoidiA2AQN1.
KOiK00681.
OMAiMLVHDIR.
OrthoDBiEOG7DNNTR.
TreeFamiTF333329.

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.

Sequencei

Sequence statusi: Complete.

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

Q99JP7-1 [UniParc]FASTAAdd to Basket

« Hide

MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF    50
LGDPDTDPDS FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC 100
SCRQDGLTVI VTACLTFATG VTVALVMQIY FGDPQIFQQG AVVTDASSCT 150
ALGMEVLSKQ GSSVDAAVAA ALCLGIVAPH SSGLGGGGVM LVHDIRRNES 200
HLIDFRESAP GALREEALQR SWDTKPGLLV GVPGMVKGLH EAHQLYGRLP 250
WSQVLAFAAA VAQDGFNVTH DLAHALAEQL PPNASDRFLD TFLPLGHPPL 300
PGSLLRRPDL AEVLDILGTS GPAAFYNGGN LTLEMVAEAQ HAGGVITEED 350
FSNYSALTEK PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS 400
REQALHWVAE TLKIALALAS RLGDPVYDST ITESMDDMLS KVEAANFRGH 450
ISDSQAAPAP LLPVYELDGA PTAAQVLVMG PDDFIVAMVS SLNRPFGSGL 500
LTPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL SFLLPTVVRP 550
AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL 600
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNTFIIGVKD 650
PRSPDAAGAT IL 662
Length:662
Mass (Da):70,251
Last modified:July 27, 2011 - v2
Checksum:iBA7F3413D694F381
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481S → H in AAH05772. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK032051 mRNA. Translation: BAC27672.1.
AL844852 Genomic DNA. Translation: CAM18929.1.
BC005772 mRNA. Translation: AAH05772.1.
AF332053 mRNA. Translation: AAK56082.1.
AF332054 mRNA. Translation: AAK56083.1.
CCDSiCCDS16949.1.
RefSeqiNP_659035.2. NM_144786.2.
UniGeneiMm.41757.

Genome annotation databases

EnsembliENSMUST00000029131; ENSMUSP00000029131; ENSMUSG00000027603.
GeneIDi207182.
KEGGimmu:207182.
UCSCiuc012chc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK032051 mRNA. Translation: BAC27672.1 .
AL844852 Genomic DNA. Translation: CAM18929.1 .
BC005772 mRNA. Translation: AAH05772.1 .
AF332053 mRNA. Translation: AAK56082.1 .
AF332054 mRNA. Translation: AAK56083.1 .
CCDSi CCDS16949.1.
RefSeqi NP_659035.2. NM_144786.2.
UniGenei Mm.41757.

3D structure databases

ProteinModelPortali Q99JP7.
SMRi Q99JP7. Positions 133-655.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q99JP7. 1 interaction.
MINTi MINT-4096072.

Protein family/group databases

MEROPSi T03.017.

PTM databases

PhosphoSitei Q99JP7.

Proteomic databases

MaxQBi Q99JP7.
PaxDbi Q99JP7.
PRIDEi Q99JP7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029131 ; ENSMUSP00000029131 ; ENSMUSG00000027603 .
GeneIDi 207182.
KEGGi mmu:207182.
UCSCi uc012chc.1. mouse.

Organism-specific databases

CTDi 2686.
MGIi MGI:1913385. Ggt7.

Phylogenomic databases

eggNOGi COG0405.
GeneTreei ENSGT00550000074591.
HOGENOMi HOG000231793.
HOVERGENi HBG039468.
InParanoidi A2AQN1.
KOi K00681.
OMAi MLVHDIR.
OrthoDBi EOG7DNNTR.
TreeFami TF333329.

Enzyme and pathway databases

UniPathwayi UPA00204 .
SABIO-RK Q99JP7.

Miscellaneous databases

NextBioi 371879.
PROi Q99JP7.
SOURCEi Search...

Gene expression databases

Bgeei Q99JP7.
CleanExi MM_GGT7.
Genevestigatori Q99JP7.

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.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary cancer.
  4. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-662.
    Strain: ILS and ISS.

Entry informationi

Entry nameiGGT7_MOUSE
AccessioniPrimary (citable) accession number: Q99JP7
Secondary accession number(s): A2AQN1, Q91V91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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