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GGCT_MOUSE
ID   GGCT_MOUSE              Reviewed;         188 AA.
AC   Q9D7X8; Q3URJ2; Q66JQ5;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Gamma-glutamylcyclotransferase;
DE            EC=4.3.2.9 {ECO:0000250|UniProtKB:O75223};
GN   Name=Ggct;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, Skin, Spinal cord, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-glutamyl
CC       dipeptides and may play a significant role in glutathione homeostasis.
CC       Induces release of cytochrome c from mitochondria with resultant
CC       induction of apoptosis. {ECO:0000250|UniProtKB:O75223}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an alpha-(gamma-L-glutamyl)-L-amino acid = 5-oxo-L-proline +
CC         an L-alpha-amino acid; Xref=Rhea:RHEA:20505, ChEBI:CHEBI:58402,
CC         ChEBI:CHEBI:59869, ChEBI:CHEBI:71304; EC=4.3.2.9;
CC         Evidence={ECO:0000250|UniProtKB:O75223};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20506;
CC         Evidence={ECO:0000250|UniProtKB:O75223};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O75223}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK008719; BAB25854.1; -; mRNA.
DR   EMBL; AK050049; BAC34049.1; -; mRNA.
DR   EMBL; AK079465; BAC37656.1; -; mRNA.
DR   EMBL; AK141474; BAE24696.1; -; mRNA.
DR   EMBL; CH466597; EDK98717.1; -; Genomic_DNA.
DR   EMBL; BC080818; AAH80818.1; -; mRNA.
DR   CCDS; CCDS20161.1; -.
DR   RefSeq; NP_080913.1; NM_026637.3.
DR   AlphaFoldDB; Q9D7X8; -.
DR   SMR; Q9D7X8; -.
DR   BioGRID; 225358; 6.
DR   STRING; 10090.ENSMUSP00000120154; -.
DR   iPTMnet; Q9D7X8; -.
DR   PhosphoSitePlus; Q9D7X8; -.
DR   REPRODUCTION-2DPAGE; Q66JQ5; -.
DR   REPRODUCTION-2DPAGE; Q9D7X8; -.
DR   EPD; Q9D7X8; -.
DR   jPOST; Q9D7X8; -.
DR   MaxQB; Q9D7X8; -.
DR   PaxDb; Q9D7X8; -.
DR   PeptideAtlas; Q9D7X8; -.
DR   PRIDE; Q9D7X8; -.
DR   ProteomicsDB; 268873; -.
DR   Ensembl; ENSMUST00000131475; ENSMUSP00000120154; ENSMUSG00000002797.
DR   GeneID; 110175; -.
DR   KEGG; mmu:110175; -.
DR   UCSC; uc009cah.1; mouse.
DR   CTD; 79017; -.
DR   MGI; MGI:95700; Ggct.
DR   VEuPathDB; HostDB:ENSMUSG00000002797; -.
DR   eggNOG; KOG4059; Eukaryota.
DR   GeneTree; ENSGT00500000044921; -.
DR   HOGENOM; CLU_048475_2_1_1; -.
DR   InParanoid; Q9D7X8; -.
DR   OMA; APHDYVM; -.
DR   OrthoDB; 1484710at2759; -.
DR   PhylomeDB; Q9D7X8; -.
DR   TreeFam; TF314378; -.
DR   Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR   BioGRID-ORCS; 110175; 6 hits in 73 CRISPR screens.
DR   ChiTaRS; Ggct; mouse.
DR   PRO; PR:Q9D7X8; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9D7X8; protein.
DR   Bgee; ENSMUSG00000002797; Expressed in animal zygote and 261 other tissues.
DR   ExpressionAtlas; Q9D7X8; baseline and differential.
DR   Genevisible; Q9D7X8; MM.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   CDD; cd06661; GGCT_like; 1.
DR   InterPro; IPR017939; G-Glutamylcylcotransferase.
DR   InterPro; IPR013024; GGCT-like.
DR   InterPro; IPR036568; GGCT-like_sf.
DR   PANTHER; PTHR12935; PTHR12935; 1.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   1: Evidence at protein level;
KW   Lyase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..188
FT                   /note="Gamma-glutamylcyclotransferase"
FT                   /id="PRO_0000089581"
FT   ACT_SITE        98
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
FT   BINDING         19..22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250, ECO:0000250|UniProtKB:O75223"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   CONFLICT        45
FT                   /note="R -> C (in Ref. 2; EDK98717 and 3; AAH80818)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   188 AA;  21166 MW;  E03657B103BA7421 CRC64;
     MASSDCEGHA GQEGETFLYF AYGSNLLTER IHLRNPSAVF CCVARLQDFK LDFGNFQGKM
     SERWHGGIAT IFQSPGDEVW GVVWRMNKSN ISSLDEQEGV KSGVYVVIEI KVSTREGKEI
     TCRSYLMTNY ESAPPSPQYK KVICMGAKEN GLPQEYQEKL KAIEPNEYKG KISDEMEDII
     KKGESKLS
 
 
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