GAMT_MOUSE
ID GAMT_MOUSE Reviewed; 236 AA.
AC O35969; Q3TZ58; Q3US90;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Guanidinoacetate N-methyltransferase;
DE EC=2.1.1.2;
GN Name=Gamt;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=9325156; DOI=10.1006/bbrc.1997.9992;
RA Jenne D.E., Olsen A.S., Zimmer M.;
RT "The human guanidinoacetate methyltransferase (GAMT) gene maps to a
RT syntenic region on 19p13.3, homologous to band C of mouse chromosome 10,
RT but GAMT is not mutated in jittery mice.";
RL Biochem. Biophys. Res. Commun. 238:723-727(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Inner ear;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=8312439; DOI=10.1095/biolreprod50.1.152;
RA Lee H., Ogawa H., Fujioka M., Gerton G.L.;
RT "Guanidinoacetate methyltransferase in the mouse: extensive expression in
RT Sertoli cells of testis and in microvilli of caput epididymis.";
RL Biol. Reprod. 50:152-162(1994).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=15245487; DOI=10.1111/j.1460-9568.2004.03478.x;
RA Tachikawa M., Fukaya M., Terasaki T., Ohtsuki S., Watanabe M.;
RT "Distinct cellular expressions of creatine synthetic enzyme GAMT and
RT creatine kinases uCK-Mi and CK-B suggest a novel neuron-glial relationship
RT for brain energy homeostasis.";
RL Eur. J. Neurosci. 20:144-160(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Converts guanidinoacetate to creatine, using S-
CC adenosylmethionine as the methyl donor. Important in nervous system
CC development. {ECO:0000250|UniProtKB:Q14353}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanidinoacetate + S-adenosyl-L-methionine = creatine + H(+) +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:10656, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57742, ChEBI:CHEBI:57856, ChEBI:CHEBI:57947,
CC ChEBI:CHEBI:59789; EC=2.1.1.2; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00892};
CC -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC creatine from L-arginine and glycine: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, microvillus
CC {ECO:0000269|PubMed:8312439}. Note=Detected in microvilli of the
CC epithelial cells lining the caput epididymis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35969-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35969-2; Sequence=VSP_017727;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, caput epididymis,
CC ovary, and liver. In the testis, localized primarily in Sertoli cells.
CC Expressed in brain with high levels in oligodendrocytes and olfactory
CC ensheathing glia. Moderate levels of expression in astrocytes.
CC {ECO:0000269|PubMed:15245487, ECO:0000269|PubMed:8312439}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RMT2 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00892}.
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; AF015887; AAB81495.1; -; mRNA.
DR EMBL; AF010499; AAB81498.1; -; Genomic_DNA.
DR EMBL; AF010498; AAB81498.1; JOINED; Genomic_DNA.
DR EMBL; AK140688; BAE24443.1; -; mRNA.
DR EMBL; AK158087; BAE34352.1; -; mRNA.
DR EMBL; BC049233; AAH49233.1; -; mRNA.
DR CCDS; CCDS35976.1; -. [O35969-1]
DR CCDS; CCDS83728.1; -. [O35969-2]
DR PIR; JC5664; JC5664.
DR RefSeq; NP_001334048.1; NM_001347119.1. [O35969-2]
DR RefSeq; NP_034385.1; NM_010255.4. [O35969-1]
DR AlphaFoldDB; O35969; -.
DR SMR; O35969; -.
DR STRING; 10090.ENSMUSP00000101002; -.
DR iPTMnet; O35969; -.
DR PhosphoSitePlus; O35969; -.
DR SwissPalm; O35969; -.
DR REPRODUCTION-2DPAGE; IPI00742399; -.
DR REPRODUCTION-2DPAGE; O35969; -.
DR SWISS-2DPAGE; O35969; -.
DR jPOST; O35969; -.
DR MaxQB; O35969; -.
DR PaxDb; O35969; -.
DR PeptideAtlas; O35969; -.
DR PRIDE; O35969; -.
DR ProteomicsDB; 267764; -. [O35969-1]
DR ProteomicsDB; 267765; -. [O35969-2]
DR Antibodypedia; 22677; 235 antibodies from 29 providers.
DR DNASU; 14431; -.
DR Ensembl; ENSMUST00000020359; ENSMUSP00000020359; ENSMUSG00000020150. [O35969-2]
DR Ensembl; ENSMUST00000105363; ENSMUSP00000101002; ENSMUSG00000020150. [O35969-1]
DR GeneID; 14431; -.
DR KEGG; mmu:14431; -.
DR UCSC; uc007gcj.2; mouse. [O35969-1]
DR UCSC; uc011xio.1; mouse. [O35969-2]
DR CTD; 2593; -.
DR MGI; MGI:1098221; Gamt.
DR VEuPathDB; HostDB:ENSMUSG00000020150; -.
DR eggNOG; KOG1709; Eukaryota.
DR GeneTree; ENSGT00390000018061; -.
DR HOGENOM; CLU_102800_0_0_1; -.
DR InParanoid; O35969; -.
DR OMA; FRRENIH; -.
DR OrthoDB; 1297303at2759; -.
DR PhylomeDB; O35969; -.
DR TreeFam; TF328555; -.
DR BRENDA; 2.1.1.2; 3474.
DR Reactome; R-MMU-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00580.
DR BioGRID-ORCS; 14431; 0 hits in 71 CRISPR screens.
DR PRO; PR:O35969; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; O35969; protein.
DR Bgee; ENSMUSG00000020150; Expressed in left lobe of liver and 172 other tissues.
DR Genevisible; O35969; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030731; F:guanidinoacetate N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006601; P:creatine biosynthetic process; IMP:MGI.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0046498; P:S-adenosylhomocysteine metabolic process; ISO:MGI.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016550; GuanidinoAc_N-MeTrfase.
DR InterPro; IPR026480; RMT2_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF009285; GAMT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51559; SAM_RMT2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Methyltransferase;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q14353"
FT CHAIN 2..236
FT /note="Guanidinoacetate N-methyltransferase"
FT /id="PRO_0000087431"
FT DOMAIN 13..236
FT /note="RMT2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT REGION 90..92
FT /note="S-adenosyl-L-methionine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 20
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 42
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 46
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868,
FT ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 50
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 69..74
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 117..118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 135
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00892"
FT BINDING 171..172
FT /ligand="guanidinoacetate"
FT /ligand_id="ChEBI:CHEBI:57742"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q14353"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10868"
FT VAR_SEQ 153
FT /note="K -> KLSSHGPTPSCPLASLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017727"
SQ SEQUENCE 236 AA; 26336 MW; 3D982DE5D51DF5CD CRC64;
MSSSAASPLF APGEDCGPAW RAAPAAYDAS DTHLQILGKP VMERWETPYM HALAAAAASR
GGRVLEVGFG MAIAASRVQQ APIEEHWIIE CNDGVFQRLQ DWALRQPHKV VPLKGLWEEV
APTLPDGHFD GILYDTYPLS EEAWHTHQFN FIKNHAFRLL KTGGVLTYCN LTSWGELMKS
KYTDITTMFE ETQVPALQEA GFLKENICTE VMALVPPADC RYYAFPQMIT PLVTKH
