GATM_MOUSE
ID GATM_MOUSE Reviewed; 423 AA.
AC Q9D964; A2AK36; Q3U8U4; Q3UAM0; Q3UKD9; Q6IU01;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Glycine amidinotransferase, mitochondrial;
DE EC=2.1.4.1 {ECO:0000250|UniProtKB:P50440};
DE AltName: Full=L-arginine:glycine amidinotransferase;
DE AltName: Full=Transamidinase;
DE Flags: Precursor;
GN Name=Gatm;
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=Bone marrow macrophage, Pancreas, and Placenta;
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].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 120-358.
RA Zink R.M., Westberg M.C., Van Pilsum J.F.;
RT "The comparative cDNA sequences of some mammalian kidney L-arginine:glycine
RT amidinotransferase genes and their evolutionary significance.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12671064; DOI=10.1073/pnas.0230424100;
RA Sandell L.L., Guan X.J., Ingram R., Tilghman S.M.;
RT "Gatm, a creatine synthesis enzyme, is imprinted in mouse placenta.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4622-4627(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, 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).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=29654216; DOI=10.1681/asn.2017111179;
RA Reichold M., Klootwijk E.D., Reinders J., Otto E.A., Milani M., Broeker C.,
RA Laing C., Wiesner J., Devi S., Zhou W., Schmitt R., Tegtmeier I.,
RA Sterner C., Doellerer H., Renner K., Oefner P.J., Dettmer K.,
RA Simbuerger J.M., Witzgall R., Stanescu H.C., Dumitriu S., Iancu D.,
RA Patel V., Mozere M., Tekman M., Jaureguiberry G., Issler N., Kesselheim A.,
RA Walsh S.B., Gale D.P., Howie A.J., Martins J.R., Hall A.M., Kasgharian M.,
RA O'Brien K., Ferreira C.R., Atwal P.S., Jain M., Hammers A.,
RA Charles-Edwards G., Choe C.U., Isbrandt D., Cebrian-Serrano A., Davies B.,
RA Sandford R.N., Pugh C., Konecki D.S., Povey S., Bockenhauer D.,
RA Lichter-Konecki U., Gahl W.A., Unwin R.J., Warth R., Kleta R.;
RT "Glycine amidinotransferase (GATM), renal Fanconi syndrome, and kidney
RT failure.";
RL J. Am. Soc. Nephrol. 29:1849-1858(2018).
CC -!- FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate
CC precursor of creatine. Creatine plays a vital role in energy metabolism
CC in muscle tissues. May play a role in embryonic and central nervous
CC system development. {ECO:0000269|PubMed:12671064}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycine + L-arginine = guanidinoacetate + L-ornithine;
CC Xref=Rhea:RHEA:13201, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57742; EC=2.1.4.1;
CC Evidence={ECO:0000250|UniProtKB:P50440};
CC -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC creatine from L-arginine and glycine: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, brain, gonads, uterus, and
CC embryonic head, chest and abdomen. Maternally expressed in the placenta
CC and yolk sac of embryos. {ECO:0000269|PubMed:12671064}.
CC -!- DEVELOPMENTAL STAGE: Expressed in a wide range of extraembryonic and
CC embryonic tissues throughout development. Expressed at relatively low
CC levels in mid-gestation stage embryos, with expression gradually
CC increasing during embryonic development. {ECO:0000269|PubMed:12671064}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice do not manifest aminoaciduria or
CC glucosuria. {ECO:0000269|PubMed:29654216}.
CC -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000305}.
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DR EMBL; AK007325; BAB24960.1; -; mRNA.
DR EMBL; AK146052; BAE26862.1; -; mRNA.
DR EMBL; AK146111; BAE26909.1; -; mRNA.
DR EMBL; AK151313; BAE30294.1; -; mRNA.
DR EMBL; AK152069; BAE30923.1; -; mRNA.
DR EMBL; AL772253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466519; EDL28104.1; -; Genomic_DNA.
DR EMBL; BC003879; AAH03879.1; -; mRNA.
DR EMBL; AY625267; AAT39893.1; -; mRNA.
DR CCDS; CCDS16665.1; -.
DR RefSeq; NP_080237.1; NM_025961.5.
DR AlphaFoldDB; Q9D964; -.
DR SMR; Q9D964; -.
DR BioGRID; 211934; 2.
DR IntAct; Q9D964; 1.
DR STRING; 10090.ENSMUSP00000028624; -.
DR iPTMnet; Q9D964; -.
DR PhosphoSitePlus; Q9D964; -.
DR SwissPalm; Q9D964; -.
DR REPRODUCTION-2DPAGE; IPI00112129; -.
DR EPD; Q9D964; -.
DR jPOST; Q9D964; -.
DR MaxQB; Q9D964; -.
DR PaxDb; Q9D964; -.
DR PeptideAtlas; Q9D964; -.
DR PRIDE; Q9D964; -.
DR ProteomicsDB; 272934; -.
DR Antibodypedia; 11803; 337 antibodies from 28 providers.
DR DNASU; 67092; -.
DR Ensembl; ENSMUST00000028624; ENSMUSP00000028624; ENSMUSG00000027199.
DR GeneID; 67092; -.
DR KEGG; mmu:67092; -.
DR UCSC; uc008maw.2; mouse.
DR CTD; 2628; -.
DR MGI; MGI:1914342; Gatm.
DR VEuPathDB; HostDB:ENSMUSG00000027199; -.
DR eggNOG; ENOG502QVCA; Eukaryota.
DR GeneTree; ENSGT00390000011613; -.
DR HOGENOM; CLU_047415_1_0_1; -.
DR InParanoid; Q9D964; -.
DR OMA; SHNEWDP; -.
DR OrthoDB; 636718at2759; -.
DR PhylomeDB; Q9D964; -.
DR TreeFam; TF300256; -.
DR BRENDA; 2.1.4.1; 3474.
DR Reactome; R-MMU-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00579.
DR BioGRID-ORCS; 67092; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Gatm; mouse.
DR PRO; PR:Q9D964; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D964; protein.
DR Bgee; ENSMUSG00000027199; Expressed in right kidney and 75 other tissues.
DR Genevisible; Q9D964; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0015067; F:amidinotransferase activity; ISO:MGI.
DR GO; GO:0015068; F:glycine amidinotransferase activity; ISS:UniProtKB.
DR GO; GO:0006601; P:creatine biosynthetic process; ISO:MGI.
DR GO; GO:0006600; P:creatine metabolic process; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0014889; P:muscle atrophy; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0046689; P:response to mercury ion; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0043434; P:response to peptide hormone; ISO:MGI.
DR InterPro; IPR033195; AmidinoTrfase.
DR PANTHER; PTHR10488; PTHR10488; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 38..423
FT /note="Glycine amidinotransferase, mitochondrial"
FT /id="PRO_0000001207"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 303
FT /evidence="ECO:0000250"
FT ACT_SITE 407
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT MOD_RES 385
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT CONFLICT 172
FT /note="L -> M (in Ref. 1; BAE26862)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="F -> Y (in Ref. 1; BAE30294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 423 AA; 48297 MW; 0B51171DACE140B4 CRC64;
MLRVRCLRGG SRGAEAVHYI GSRLGGSLTG WVQRTFQSTQ AATASSRNSC AAEDKATHPL
PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTVEVKANTY EKYWPFYQKN GGLYFPKDHL
KKAVAEVEEM CNILSMEGVT VRRPDPIDWS LKYKTPDFES TGLYSAMPRD ILMVVGNEII
EAPMAWRSRF FEYRAYRSII KDYFHRGAKW TTAPKPTMAD ELYDQNYPIH SVEDRHKLAA
QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PTPVIPDDHP LWMSSKWLSM
NVLMLDEKRV MVDANEVPIQ KMFEKLGIST IKVNIRNANS LGGGFHCWTC DVRRRGTLQS
YFD
