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Protein

Guanidinoacetate N-methyltransferase

Gene

Gamt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine.PROSITE-ProRule annotation

Pathway:icreatine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes creatine from L-arginine and glycine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glycine amidinotransferase, mitochondrial (Gatm)
  2. Guanidinoacetate N-methyltransferase (Gamt)
This subpathway is part of the pathway creatine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes creatine from L-arginine and glycine, the pathway creatine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei42 – 421SubstratePROSITE-ProRule annotation
Binding sitei46 – 461SubstratePROSITE-ProRule annotation
Binding sitei50 – 501S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei135 – 1351S-adenosyl-L-methionine and substratePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • creatine biosynthetic process Source: MGI
  • embryonic liver development Source: Ensembl
  • organ morphogenesis Source: MGI
  • regulation of multicellular organism growth Source: MGI
  • S-adenosylhomocysteine metabolic process Source: Ensembl
  • S-adenosylmethionine metabolic process Source: Ensembl
  • spermatogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_307447. Creatine metabolism.
UniPathwayiUPA00104; UER00580.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanidinoacetate N-methyltransferase (EC:2.1.1.2)
Gene namesi
Name:Gamt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1098221. Gamt.

Subcellular locationi

  • Cell projectionmicrovillus 1 Publication

  • Note: Detected in microvilli of the epithelial cells lining the caput epididymis.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 236235Guanidinoacetate N-methyltransferasePRO_0000087431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO35969.
PaxDbiO35969.
PRIDEiO35969.

2D gel databases

REPRODUCTION-2DPAGEIPI00742399.
O35969.
SWISS-2DPAGEO35969.

PTM databases

PhosphoSiteiO35969.

Expressioni

Tissue specificityi

Highly expressed in testis, caput epididymis, ovary, and liver. In the testis, localized primarily in Sertoli cells. Expressed in brain with high levels in oligodendrocytes and olfactory ensheathing glia. Moderate levels of expression in astrocytes.2 Publications

Gene expression databases

BgeeiO35969.
CleanExiMM_GAMT.
GenevisibleiO35969. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiO35969. 2 interactions.
MINTiMINT-1869591.
STRINGi10090.ENSMUSP00000101002.

Structurei

3D structure databases

ProteinModelPortaliO35969.
SMRiO35969. Positions 8-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini13 – 236224RMT2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni69 – 746S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni90 – 923S-adenosyl-L-methioninePROSITE-ProRule annotation
Regioni117 – 1182S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni171 – 1722Substrate bindingPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RMT2 methyltransferase family.PROSITE-ProRule annotation
Contains 1 RMT2 (arginine N-methyltransferase 2-like) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG235457.
GeneTreeiENSGT00390000018061.
HOGENOMiHOG000010290.
HOVERGENiHBG005801.
InParanoidiO35969.
KOiK00542.
OMAiRYYAFPQ.
OrthoDBiEOG75QR4S.
PhylomeDBiO35969.
TreeFamiTF328555.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016550. GuanidinoAc_N-MeTrfase.
IPR026480. RMT2_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF009285. GAMT. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51559. SAM_RMT2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35969-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSSSAASPLF APGEDCGPAW RAAPAAYDAS DTHLQILGKP VMERWETPYM
60 70 80 90 100
HALAAAAASR GGRVLEVGFG MAIAASRVQQ APIEEHWIIE CNDGVFQRLQ
110 120 130 140 150
DWALRQPHKV VPLKGLWEEV APTLPDGHFD GILYDTYPLS EEAWHTHQFN
160 170 180 190 200
FIKNHAFRLL KTGGVLTYCN LTSWGELMKS KYTDITTMFE ETQVPALQEA
210 220 230
GFLKENICTE VMALVPPADC RYYAFPQMIT PLVTKH
Length:236
Mass (Da):26,336
Last modified:January 1, 1998 - v1
Checksum:i3D982DE5D51DF5CD
GO
Isoform 2 (identifier: O35969-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-153: K → KLSSHGPTPSCPLASLQ

Note: No experimental confirmation available.
Show »
Length:252
Mass (Da):27,913
Checksum:i2F7006B71CFA8FF1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei153 – 1531K → KLSSHGPTPSCPLASLQ in isoform 2. 1 PublicationVSP_017727

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015887 mRNA. Translation: AAB81495.1.
AF010499, AF010498 Genomic DNA. Translation: AAB81498.1.
AK140688 mRNA. Translation: BAE24443.1.
AK158087 mRNA. Translation: BAE34352.1.
BC049233 mRNA. Translation: AAH49233.1.
CCDSiCCDS35976.1. [O35969-1]
PIRiJC5664.
RefSeqiNP_034385.1. NM_010255.3. [O35969-1]
XP_006513284.1. XM_006513221.2. [O35969-2]
UniGeneiMm.7329.

Genome annotation databases

EnsembliENSMUST00000020359; ENSMUSP00000020359; ENSMUSG00000020150. [O35969-2]
ENSMUST00000105363; ENSMUSP00000101002; ENSMUSG00000020150. [O35969-1]
GeneIDi14431.
KEGGimmu:14431.
UCSCiuc007gcj.2. mouse. [O35969-1]
uc011xio.1. mouse. [O35969-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF015887 mRNA. Translation: AAB81495.1.
AF010499, AF010498 Genomic DNA. Translation: AAB81498.1.
AK140688 mRNA. Translation: BAE24443.1.
AK158087 mRNA. Translation: BAE34352.1.
BC049233 mRNA. Translation: AAH49233.1.
CCDSiCCDS35976.1. [O35969-1]
PIRiJC5664.
RefSeqiNP_034385.1. NM_010255.3. [O35969-1]
XP_006513284.1. XM_006513221.2. [O35969-2]
UniGeneiMm.7329.

3D structure databases

ProteinModelPortaliO35969.
SMRiO35969. Positions 8-236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35969. 2 interactions.
MINTiMINT-1869591.
STRINGi10090.ENSMUSP00000101002.

PTM databases

PhosphoSiteiO35969.

2D gel databases

REPRODUCTION-2DPAGEIPI00742399.
O35969.
SWISS-2DPAGEO35969.

Proteomic databases

MaxQBiO35969.
PaxDbiO35969.
PRIDEiO35969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020359; ENSMUSP00000020359; ENSMUSG00000020150. [O35969-2]
ENSMUST00000105363; ENSMUSP00000101002; ENSMUSG00000020150. [O35969-1]
GeneIDi14431.
KEGGimmu:14431.
UCSCiuc007gcj.2. mouse. [O35969-1]
uc011xio.1. mouse. [O35969-2]

Organism-specific databases

CTDi2593.
MGIiMGI:1098221. Gamt.

Phylogenomic databases

eggNOGiNOG235457.
GeneTreeiENSGT00390000018061.
HOGENOMiHOG000010290.
HOVERGENiHBG005801.
InParanoidiO35969.
KOiK00542.
OMAiRYYAFPQ.
OrthoDBiEOG75QR4S.
PhylomeDBiO35969.
TreeFamiTF328555.

Enzyme and pathway databases

UniPathwayiUPA00104; UER00580.
ReactomeiREACT_307447. Creatine metabolism.

Miscellaneous databases

NextBioi286049.
PROiO35969.
SOURCEiSearch...

Gene expression databases

BgeeiO35969.
CleanExiMM_GAMT.
GenevisibleiO35969. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR016550. GuanidinoAc_N-MeTrfase.
IPR026480. RMT2_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PIRSFiPIRSF009285. GAMT. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51559. SAM_RMT2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human guanidinoacetate methyltransferase (GAMT) gene maps to a syntenic region on 19p13.3, homologous to band C of mouse chromosome 10, but GAMT is not mutated in jittery mice."
    Jenne D.E., Olsen A.S., Zimmer M.
    Biochem. Biophys. Res. Commun. 238:723-727(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    Strain: C57BL/6.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum and Inner ear.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Liver.
  4. "Guanidinoacetate methyltransferase in the mouse: extensive expression in Sertoli cells of testis and in microvilli of caput epididymis."
    Lee H., Ogawa H., Fujioka M., Gerton G.L.
    Biol. Reprod. 50:152-162(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  5. "Distinct cellular expressions of creatine synthetic enzyme GAMT and creatine kinases uCK-Mi and CK-B suggest a novel neuron-glial relationship for brain energy homeostasis."
    Tachikawa M., Fukaya M., Terasaki T., Ohtsuki S., Watanabe M.
    Eur. J. Neurosci. 20:144-160(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiGAMT_MOUSE
AccessioniPrimary (citable) accession number: O35969
Secondary accession number(s): Q3TZ58, Q3US90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.