位置:首页 > 蛋白库 > GGT5_RAT
GGT5_RAT
ID   GGT5_RAT                Reviewed;         572 AA.
AC   Q9QWE9; Q5PQV0;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Glutathione hydrolase 5 proenzyme;
DE            EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE   AltName: Full=Gamma-glutamyl leukotrienase;
DE            Short=GGL;
DE   AltName: Full=Gamma-glutamyl transpeptidase-related enzyme;
DE            Short=GGT-rel;
DE   AltName: Full=Gamma-glutamyltransferase 5;
DE            Short=GGT 5;
DE            EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE   AltName: Full=Gamma-glutamyltransferase-like activity 1;
DE   AltName: Full=Gamma-glutamyltranspeptidase 5;
DE   AltName: Full=Leukotriene-C4 hydrolase;
DE            EC=3.4.19.14 {ECO:0000250|UniProtKB:P19440};
DE   Contains:
DE     RecName: Full=Glutathione hydrolase 5 heavy chain;
DE   Contains:
DE     RecName: Full=Glutathione hydrolase 5 light chain;
DE   Flags: Precursor;
GN   Name=Ggt5; Synonyms=Ggtla1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Fischer 344/N; TISSUE=Trachea;
RX   PubMed=9374738; DOI=10.1152/ajplung.1997.273.5.l1082;
RA   Potdar P.D., Andrews K.L., Nettesheim P., Ostrowski L.E.;
RT   "Expression and regulation of gamma-glutamyl transpeptidase-related enzyme
RT   in tracheal cells.";
RL   Am. J. Physiol. 273:L1082-L1089(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC       glutathione-S-conjugate. Converts leukotriene C4 (LTC4), a glutathione-
CC       S-conjugate, to leukotriene D4 (LTD4). Does not cleave gamma-glutamyl
CC       compounds such as gamma-glutamyl leucine. May also catalyze a
CC       transpeptidation reaction in addition to the hydrolysis reaction,
CC       transferring the gamma-glutamyl moiety to an acceptor amino acid to
CC       form a new gamma-glutamyl compound. Acts as a negative regulator of
CC       geranylgeranyl glutathione bioactivity by cleaving off its gamma-
CC       glutamyl group, playing a role in adaptive immune responses.
CC       {ECO:0000250|UniProtKB:P36269}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC         5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC         Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC         ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC         ChEBI:CHEBI:78608; EC=2.3.2.2;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC         Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC         cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC         ChEBI:CHEBI:143103; EC=3.4.19.13;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4;
CC         Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-[(2E,6E,10E)-geranylgeranyl]-L-glutathione = L-
CC         glutamate + S-[(2E,6E,10E)-geranylgeranyl]-L-cysteinylglycine;
CC         Xref=Rhea:RHEA:65120, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:156326, ChEBI:CHEBI:156330;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65121;
CC         Evidence={ECO:0000250|UniProtKB:P36269};
CC   -!- ACTIVITY REGULATION: Inhibited by serine-borate.
CC       {ECO:0000250|UniProtKB:P36269}.
CC   -!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9Z2A9}.
CC   -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC       {ECO:0000250|UniProtKB:P36269}.
CC   -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC       site is located in the light chain. {ECO:0000250|UniProtKB:Q9Z2A9}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z2A9}; Single-
CC       pass type II membrane protein {ECO:0000250|UniProtKB:Q9Z2A9}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, but at low level, except in the
CC       airway epithelial cells. Detected in brain, heart, kidney, liver, lung,
CC       spleen, testis and trachea. {ECO:0000269|PubMed:9374738}.
CC   -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC       {ECO:0000250|UniProtKB:P19440}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9Z2A9}.
CC   -!- MISCELLANEOUS: A previous study reported that GSH and oxidized
CC       glutathione (GSSG) are not substrates for murine GGT5 (By similarity).
CC       However, this result contrasts with two studies reported that GSH is
CC       indeed a substrate for GGT5 (By similarity).
CC       {ECO:0000250|UniProtKB:P36269, ECO:0000250|UniProtKB:Q9Z2A9}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U76252; AAC23546.1; -; mRNA.
DR   EMBL; BC087018; AAH87018.1; -; mRNA.
DR   RefSeq; NP_062108.2; NM_019235.2.
DR   AlphaFoldDB; Q9QWE9; -.
DR   SMR; Q9QWE9; -.
DR   MEROPS; T03.002; -.
DR   GlyGen; Q9QWE9; 8 sites.
DR   iPTMnet; Q5PQV0; -.
DR   Ensembl; ENSRNOT00000093720; ENSRNOP00000076334; ENSRNOG00000062276.
DR   GeneID; 29566; -.
DR   KEGG; rno:29566; -.
DR   CTD; 2687; -.
DR   RGD; 2684; Ggt5.
DR   GeneTree; ENSGT00940000155794; -.
DR   InParanoid; Q9QWE9; -.
DR   OrthoDB; 1419292at2759; -.
DR   PhylomeDB; Q9QWE9; -.
DR   Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR   Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-RNO-9753281; Paracetamol ADME.
DR   UniPathway; UPA00204; -.
DR   UniPathway; UPA00880; -.
DR   PRO; PR:Q9QWE9; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0036374; F:glutathione hydrolase activity; ISO:RGD.
DR   GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0002951; F:leukotriene-C(4) hydrolase; ISS:UniProtKB.
DR   GO; GO:0000048; F:peptidyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; ISO:RGD.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006751; P:glutathione catabolic process; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR   GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISO:RGD.
DR   GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; TAS:RGD.
DR   Gene3D; 1.10.246.130; -; 1.
DR   Gene3D; 3.60.20.40; -; 1.
DR   InterPro; IPR043138; GGT_lsub_C.
DR   InterPro; IPR000101; GGT_peptidase.
DR   InterPro; IPR043137; GGT_ssub.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR11686; PTHR11686; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Glutathione biosynthesis; Glycoprotein; Hydrolase;
KW   Leukotriene biosynthesis; Membrane; Protease; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix; Zymogen.
FT   CHAIN           1..387
FT                   /note="Glutathione hydrolase 5 heavy chain"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT                   /id="PRO_0000011076"
FT   CHAIN           388..572
FT                   /note="Glutathione hydrolase 5 light chain"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT                   /id="PRO_0000011077"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2A9"
FT   TRANSMEM        7..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2A9"
FT   TOPO_DOM        30..572
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z2A9"
FT   ACT_SITE        388
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         110
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         406
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         427
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   BINDING         453..454
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250|UniProtKB:P19440"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        185
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        377
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        200
FT                   /note="Q -> H (in Ref. 1; AAC23546)"
FT   CONFLICT        325
FT                   /note="A -> T (in Ref. 1; AAC23546)"
SQ   SEQUENCE   572 AA;  61569 MW;  72CE9CCEB1FEB645 CRC64;
     MAWGHRTTVC LVLLGVSLGL AIIVLAVVLP HHQASCRPDA FTRAAVAADS KICSDIGRVI
     LQQQGSPVDA AIAALICTGV VNPQSMGLGG GVVFTIYNAS TGKVEVINAR ETVPASHDQR
     LLDQCTNALP LCTGAQWIGV PGELRGYAEA HRRYGRLPWA QLFQPTIALL REGFRVPPIL
     SQFLNTSFLQ PCLNSSTLRQ LFFNGTETLR SQDPLPWPAL ANTLETVAKE GAEVLYTGKL
     GQTLVEDIAW QGSQLTVQDL AAFRPKVVEP LEMALGNYTL YSPPPPAGGA ILSFILNVLK
     GFNFSAETVA GPEGKVNMYH HLVEALKFAV GQRWRLWDPY SHPGIQNISQ DLLRETLAQH
     IRQQIDGRGD HQLSHYNLSG VRGNSMGTSH VSVLGEDGSA VAATSTINTP FGAMVYSPRT
     GILLNNELLD LCWRHKPGST VTPPPVPGEQ PPSSMVPSIL INEVQGSKLV IGGAGGELII
     SAVTQAIVNK LWLGFSLTDA IAAPILHVNS KGHVEYEPKF NQEVRKGLQD RGQSQSQSQR
     PVFLNSVQAV FQEGPCVYAA SDLRKAGKAS GY
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024