GGACT_MOUSE
ID GGACT_MOUSE Reviewed; 149 AA.
AC Q923B0; Q66JP0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Gamma-glutamylaminecyclotransferase;
DE Short=GGACT;
DE EC=4.3.2.8 {ECO:0000250|UniProtKB:Q9BVM4};
DE AltName: Full=AIG2-like domain-containing protein 1;
DE AltName: Full=Gamma-glutamylamine cyclotransferase;
GN Name=Ggact; Synonyms=A2ld1;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Liver;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RX PubMed=16224779; DOI=10.1002/prot.20610;
RA Klock H.E., Schwarzenbacher R., Xu Q., McMullan D., Abdubek P., Ambing E.,
RA Axelrod H., Biorac T., Canaves J.M., Chiu H.-J., Deacon A.M., DiDonato M.,
RA Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hale J.,
RA Hampton E., Han G.W., Haugen J., Hornsby M., Jaroszewski L., Koesema E.,
RA Kreusch A., Kuhn P., Miller M.D., Moy K., Nigoghossian E., Paulsen J.,
RA Quijano K., Reyes R., Rife C., Sims E., Spraggon G., Stevens R.C.,
RA van den Bedem H., Velasquez J., Vincent J., White A., Wolf G.,
RA Hodgson K.O., Wooley J., Lesley S.A., Wilson I.A.;
RT "Crystal structure of a conserved hypothetical protein (gi: 13879369) from
RT mouse at 1.90 A resolution reveals a new fold.";
RL Proteins 61:1132-1136(2005).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=20944236; DOI=10.1107/s1744309110033658;
RA Serrano P., Pedrini B., Geralt M., Jaudzems K., Mohanty B., Horst R.,
RA Herrmann T., Elsliger M.A., Wilson I.A., Wuthrich K.;
RT "Comparison of NMR and crystal structures highlights conformational
RT isomerism in protein active sites.";
RL Acta Crystallogr. F 66:1393-1405(2010).
CC -!- FUNCTION: Contributes to degradation of proteins cross-linked by
CC transglutaminases by degrading the cross-link between a lysine and a
CC glutamic acid residue. Catalyzes the formation of 5-oxo-L-proline from
CC L-gamma-glutamyl-L-epsilon-lysine. Inactive with L-gamma-glutamyl-
CC alpha-amino acid substrates such as L-gamma-glutamyl-L-alpha-cysteine
CC and L-gamma-glutamyl-L-alpha-alanine. {ECO:0000250|UniProtKB:Q9BVM4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=epsilon-(gamma-L-glutamyl)-L-lysine = 5-oxo-L-proline + L-
CC lysine; Xref=Rhea:RHEA:16961, ChEBI:CHEBI:32551, ChEBI:CHEBI:58402,
CC ChEBI:CHEBI:133752; EC=4.3.2.8;
CC Evidence={ECO:0000250|UniProtKB:Q9BVM4};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:16224779}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q923B0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q923B0-2; Sequence=VSP_031641, VSP_031642;
CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase 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; AK050251; BAC34147.1; -; mRNA.
DR EMBL; BC006662; AAH06662.1; -; mRNA.
DR EMBL; BC080839; AAH80839.1; -; mRNA.
DR CCDS; CCDS27351.1; -. [Q923B0-1]
DR RefSeq; NP_663441.1; NM_145466.2. [Q923B0-1]
DR RefSeq; XP_006518983.1; XM_006518920.2. [Q923B0-1]
DR PDB; 1VKB; X-ray; 1.90 A; A=1-149.
DR PDB; 2KL2; NMR; -; A=1-149.
DR PDBsum; 1VKB; -.
DR PDBsum; 2KL2; -.
DR AlphaFoldDB; Q923B0; -.
DR BMRB; Q923B0; -.
DR SMR; Q923B0; -.
DR STRING; 10090.ENSMUSP00000037278; -.
DR EPD; Q923B0; -.
DR jPOST; Q923B0; -.
DR MaxQB; Q923B0; -.
DR PaxDb; Q923B0; -.
DR PeptideAtlas; Q923B0; -.
DR PRIDE; Q923B0; -.
DR ProteomicsDB; 266798; -. [Q923B0-1]
DR ProteomicsDB; 266799; -. [Q923B0-2]
DR Antibodypedia; 57333; 83 antibodies from 16 providers.
DR DNASU; 223267; -.
DR Ensembl; ENSMUST00000038075; ENSMUSP00000037278; ENSMUSG00000041625. [Q923B0-1]
DR Ensembl; ENSMUST00000110679; ENSMUSP00000135487; ENSMUSG00000041625. [Q923B0-2]
DR GeneID; 223267; -.
DR KEGG; mmu:223267; -.
DR UCSC; uc011zqm.1; mouse. [Q923B0-1]
DR CTD; 87769; -.
DR MGI; MGI:2385008; Ggact.
DR VEuPathDB; HostDB:ENSMUSG00000041625; -.
DR eggNOG; KOG4450; Eukaryota.
DR GeneTree; ENSGT00390000010543; -.
DR HOGENOM; CLU_2605416_0_0_1; -.
DR InParanoid; Q923B0; -.
DR OMA; YQRTALR; -.
DR OrthoDB; 1389682at2759; -.
DR PhylomeDB; Q923B0; -.
DR TreeFam; TF323258; -.
DR BioGRID-ORCS; 223267; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Ggact; mouse.
DR EvolutionaryTrace; Q923B0; -.
DR PRO; PR:Q923B0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q923B0; protein.
DR Bgee; ENSMUSG00000041625; Expressed in right kidney and 198 other tissues.
DR ExpressionAtlas; Q923B0; baseline and differential.
DR Genevisible; Q923B0; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0061929; F:gamma-glutamylaminecyclotransferase activity; ISS:UniProtKB.
DR GO; GO:0042219; P:cellular modified amino acid catabolic process; ISS:UniProtKB.
DR CDD; cd06661; GGCT_like; 1.
DR InterPro; IPR009288; AIG2-like_dom.
DR InterPro; IPR039126; GGACT.
DR InterPro; IPR013024; GGCT-like.
DR InterPro; IPR036568; GGCT-like_sf.
DR PANTHER; PTHR12510; PTHR12510; 1.
DR Pfam; PF06094; GGACT; 1.
DR SUPFAM; SSF110857; SSF110857; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lyase; Reference proteome.
FT CHAIN 1..149
FT /note="Gamma-glutamylaminecyclotransferase"
FT /id="PRO_0000320204"
FT ACT_SITE 82
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 7..10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 66..79
FT /note="EIYEVDEQMLRFLD -> NWKGGHICHCRWIH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031641"
FT VAR_SEQ 80..149
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031642"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:2KL2"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1VKB"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1VKB"
FT HELIX 23..25
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 28..38
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1VKB"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:1VKB"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1VKB"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:1VKB"
FT STRAND 108..118
FT /evidence="ECO:0007829|PDB:1VKB"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:1VKB"
SQ SEQUENCE 149 AA; 17080 MW; 0FB86B86AF2AB46B CRC64;
MAHIFVYGTL KRGQPNHKVM LDHSHGLAAF RGRGCTVESF PLVIAGEHNI PWLLYLPGKG
HCVTGEIYEV DEQMLRFLDD FEDCPSMYQR TALQVQVLEW EGDGDPGDSV QCFVYTTATY
APEWLFLPYH ESYDSEGPHG LRYNPRENR
