| Tag | Content |
|---|
| CPLM ID | CPLM-002487 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Gamma-glutamyltranspeptidase 1 |
Protein Synonyms/Alias | GGT 1; Gamma-glutamyltransferase 1; Glutathione hydrolase 1; Leukotriene-C4 hydrolase; CD224; Gamma-glutamyltranspeptidase 1 heavy chain; Gamma-glutamyltranspeptidase 1 light chain |
Gene Name | Ggt1 |
Gene Synonyms/Alias | Ggt |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 99 | IYNSTTRKAEVINAR | acetylation | [1] | | 527 | QVVTAGLKTRHHHTE | acetylation | [2] |
|
Reference | [1] Chemical modification of active site residues in gamma-glutamyl transpeptidase. Aspartate 422 and cysteine 453. Smith TK, Meister A. J Biol Chem. 1995 May 26;270(21):12476-80. [ PMID: 7759491] [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. |
Sequence Annotation | CARBOHYD 94 94 N-linked (GlcNAc...) (Potential).
CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
CARBOHYD 119 119 N-linked (GlcNAc...) (Potential).
CARBOHYD 229 229 N-linked (GlcNAc...) (Potential).
CARBOHYD 343 343 N-linked (GlcNAc...) (Potential).
CARBOHYD 427 427 N-linked (GlcNAc...) (Potential).
CARBOHYD 510 510 N-linked (GlcNAc...) (Potential). |
Keyword | Acyltransferase; Complete proteome; Direct protein sequencing; Glutathione biosynthesis; Glycoprotein; Hydrolase; Membrane; Reference proteome; Sialic acid; Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Zymogen. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 568 AA |
Protein Sequence | MKNRFLVLGL VAVVLVFVII GLCIWLPTTS GKPDHVYSRA AVATDAKRCS EIGRDMLQEG 60
GSVVDAAIAS LLCMGLINAH SMGIGGGLFF TIYNSTTRKA EVINAREMAP RLANTSMFNN 120
SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI QLARHGFPVG KGLARALDKK 180
RDIIEKTPAL CEVFCRQGKV LQEGETVTMP KLADTLQILA QEGARAFYNG SLTAQIVKDI 240
QEAGGIMTVE DLNNYRAEVI EHPMSIGLGD STLYVPSAPL SGPVLILILN ILKGYNFSPK 300
SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA TQLRARITDE 360
TTHPTAYYEP EFYLPDDGGT AHLSVVSEDG SAVAATSTIN LYFGSKVLSR VSGILFNDEM 420
DDFSSPNFTN QFGVAPSPAN FIKPGKQPLS SMCPSIIVDK DGKVRMVVGA SGGTQITTSV 480
ALAIINSLWF GYDVKRAVEE PRLHNQLLPN TTTVEKNIDQ VVTAGLKTRH HHTEVTPDFI 540
AVVQAVVRTS GGWAAASDSR KGGEPAGY 568 |
Gene Ontology | GO:0005615; C:extracellular space; IDA:RGD. GO:0005887; C:integral to plasma membrane; TAS:RGD. GO:0003840; F:gamma-glutamyltransferase activity; IDA:RGD. GO:0036374; F:glutathione hydrolase activity; IEA:EC. GO:0007568; P:aging; IEP:RGD. GO:0034599; P:cellular response to oxidative stress; IEP:RGD. GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW. GO:0031179; P:peptide modification; IDA:RGD. GO:0032355; P:response to estradiol stimulus; IEP:RGD. GO:0032496; P:response to lipopolysaccharide; IEP:RGD. GO:0034612; P:response to tumor necrosis factor; IEP:RGD. |
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PRINTS | |