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Protein

Glycine amidinotransferase, mitochondrial

Gene

Gatm

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the biosynthesis of guanidinoacetate, the immediate precursor of creatine. Creatine plays a vital role in energy metabolism in muscle tissues. May play a role in embryonic and central nervous system development.1 Publication

Catalytic activityi

L-arginine + glycine = L-ornithine + guanidinoacetate.

Pathwayi: creatine biosynthesis

This protein is involved in step 1 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
Active sitei254 – 2541By similarity
Active sitei303 – 3031By similarity
Active sitei407 – 4071Amidino-cysteine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiR-MMU-71288. Creatine metabolism.
UniPathwayiUPA00104; UER00579.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine amidinotransferase, mitochondrial (EC:2.1.4.1)
Alternative name(s):
L-arginine:glycine amidinotransferase
Transamidinase
Gene namesi
Name:Gatm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914342. Gatm.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionBy similarityAdd
BLAST
Chaini38 – 423386Glycine amidinotransferase, mitochondrialPRO_0000001207Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei49 – 491PhosphoserineBy similarity
Modified residuei385 – 3851N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D964.
MaxQBiQ9D964.
PaxDbiQ9D964.
PRIDEiQ9D964.

2D gel databases

REPRODUCTION-2DPAGEIPI00112129.

PTM databases

iPTMnetiQ9D964.
PhosphoSiteiQ9D964.
SwissPalmiQ9D964.

Expressioni

Tissue specificityi

Expressed in kidney, brain, gonads, uterus, and embryonic head, chest and abdomen. Maternally expressed in the placenta and yolk sac of embryos.1 Publication

Developmental stagei

Expressed in a wide range of extraembryonic and embryonic tissues throughout development. Expressed at relatively low levels in mid-gestation stage embryos, with expression gradually increasing during embryonic development.1 Publication

Gene expression databases

BgeeiQ9D964.
GenevisibleiQ9D964. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
GATMP504401EBI-2552599,EBI-2552594From a different organism.

Protein-protein interaction databases

BioGridi211934. 1 interaction.
IntActiQ9D964. 3 interactions.
MINTiMINT-4095670.
STRINGi10090.ENSMUSP00000028624.

Structurei

3D structure databases

ProteinModelPortaliQ9D964.
SMRiQ9D964. Positions 64-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the amidinotransferase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IFBR. Eukaryota.
ENOG410Y45M. LUCA.
GeneTreeiENSGT00390000011613.
HOGENOMiHOG000231593.
HOVERGENiHBG002492.
InParanoidiQ9D964.
KOiK00613.
OMAiRPCHQID.
OrthoDBiEOG712TW4.
PhylomeDBiQ9D964.
TreeFamiTF300256.

Family and domain databases

InterProiIPR033195. AmidinoTrfase.
[Graphical view]
PANTHERiPTHR10488. PTHR10488. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9D964-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRVRCLRGG SRGAEAVHYI GSRLGGSLTG WVQRTFQSTQ AATASSRNSC
60 70 80 90 100
AAEDKATHPL PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTVEVKANTY
110 120 130 140 150
EKYWPFYQKN GGLYFPKDHL KKAVAEVEEM CNILSMEGVT VRRPDPIDWS
160 170 180 190 200
LKYKTPDFES TGLYSAMPRD ILMVVGNEII EAPMAWRSRF FEYRAYRSII
210 220 230 240 250
KDYFHRGAKW TTAPKPTMAD ELYDQNYPIH SVEDRHKLAA QGKFVTTEFE
260 270 280 290 300
PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
310 320 330 340 350
PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PTPVIPDDHP
360 370 380 390 400
LWMSSKWLSM NVLMLDEKRV MVDANEVPIQ KMFEKLGIST IKVNIRNANS
410 420
LGGGFHCWTC DVRRRGTLQS YFD
Length:423
Mass (Da):48,297
Last modified:June 1, 2001 - v1
Checksum:i0B51171DACE140B4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti172 – 1721L → M in BAE26862 (PubMed:16141072).Curated
Sequence conflicti258 – 2581F → Y in BAE30294 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007325 mRNA. Translation: BAB24960.1.
AK146052 mRNA. Translation: BAE26862.1.
AK146111 mRNA. Translation: BAE26909.1.
AK151313 mRNA. Translation: BAE30294.1.
AK152069 mRNA. Translation: BAE30923.1.
AL772253 Genomic DNA. Translation: CAM13305.1.
CH466519 Genomic DNA. Translation: EDL28104.1.
BC003879 mRNA. Translation: AAH03879.1.
AY625267 mRNA. Translation: AAT39893.1.
CCDSiCCDS16665.1.
RefSeqiNP_080237.1. NM_025961.5.
UniGeneiMm.29975.

Genome annotation databases

EnsembliENSMUST00000028624; ENSMUSP00000028624; ENSMUSG00000027199.
GeneIDi67092.
KEGGimmu:67092.
UCSCiuc008maw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007325 mRNA. Translation: BAB24960.1.
AK146052 mRNA. Translation: BAE26862.1.
AK146111 mRNA. Translation: BAE26909.1.
AK151313 mRNA. Translation: BAE30294.1.
AK152069 mRNA. Translation: BAE30923.1.
AL772253 Genomic DNA. Translation: CAM13305.1.
CH466519 Genomic DNA. Translation: EDL28104.1.
BC003879 mRNA. Translation: AAH03879.1.
AY625267 mRNA. Translation: AAT39893.1.
CCDSiCCDS16665.1.
RefSeqiNP_080237.1. NM_025961.5.
UniGeneiMm.29975.

3D structure databases

ProteinModelPortaliQ9D964.
SMRiQ9D964. Positions 64-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211934. 1 interaction.
IntActiQ9D964. 3 interactions.
MINTiMINT-4095670.
STRINGi10090.ENSMUSP00000028624.

PTM databases

iPTMnetiQ9D964.
PhosphoSiteiQ9D964.
SwissPalmiQ9D964.

2D gel databases

REPRODUCTION-2DPAGEIPI00112129.

Proteomic databases

EPDiQ9D964.
MaxQBiQ9D964.
PaxDbiQ9D964.
PRIDEiQ9D964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028624; ENSMUSP00000028624; ENSMUSG00000027199.
GeneIDi67092.
KEGGimmu:67092.
UCSCiuc008maw.2. mouse.

Organism-specific databases

CTDi2628.
MGIiMGI:1914342. Gatm.

Phylogenomic databases

eggNOGiENOG410IFBR. Eukaryota.
ENOG410Y45M. LUCA.
GeneTreeiENSGT00390000011613.
HOGENOMiHOG000231593.
HOVERGENiHBG002492.
InParanoidiQ9D964.
KOiK00613.
OMAiRPCHQID.
OrthoDBiEOG712TW4.
PhylomeDBiQ9D964.
TreeFamiTF300256.

Enzyme and pathway databases

UniPathwayiUPA00104; UER00579.
ReactomeiR-MMU-71288. Creatine metabolism.

Miscellaneous databases

PROiQ9D964.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D964.
GenevisibleiQ9D964. MM.

Family and domain databases

InterProiIPR033195. AmidinoTrfase.
[Graphical view]
PANTHERiPTHR10488. PTHR10488. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Strain: C57BL/6J.
    Tissue: Bone marrow macrophage, Pancreas and Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Mammary tumor.
  5. "The comparative cDNA sequences of some mammalian kidney L-arginine:glycine amidinotransferase genes and their evolutionary significance."
    Zink R.M., Westberg M.C., Van Pilsum J.F.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 120-358.
  6. "Gatm, a creatine synthesis enzyme, is imprinted in mouse placenta."
    Sandell L.L., Guan X.J., Ingram R., Tilghman S.M.
    Proc. Natl. Acad. Sci. U.S.A. 100:4622-4627(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiGATM_MOUSE
AccessioniPrimary (citable) accession number: Q9D964
Secondary accession number(s): A2AK36
, Q3U8U4, Q3UAM0, Q3UKD9, Q6IU01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 125 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

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 one 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.