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Glycine amidinotransferase, mitochondrial (EC 2.1.4.1) (L-arginine:glycine amidinotransferase) (Transamidinase)

 GATM_HUMAN              Reviewed;         423 AA.
P50440; B4DH99; B4DPI3; Q53EQ4;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 181.
RecName: Full=Glycine amidinotransferase, mitochondrial;
EC=2.1.4.1 {ECO:0000269|PubMed:27233232, ECO:0000269|PubMed:3800397};
AltName: Full=L-arginine:glycine amidinotransferase;
AltName: Full=Transamidinase;
Flags: Precursor;
Name=GATM; Synonyms=AGAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=8313955; DOI=10.1016/0014-5793(94)80394-3;
Humm A., Huber R., Mann K.;
"The amino acid sequences of human and pig L-arginine:glycine
amidinotransferase.";
FEBS Lett. 339:101-107(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Kidney;
Austruy E., Belley L., Millasot P., Junien C., Jeanpierre C.;
"Characterization of the human cDNA with partial homology with the
gamma subunit of sodium potassium ATPase of rat, mouse, rabbit and
sheep.";
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-110.
TISSUE=Kidney;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=3800397; DOI=10.1016/0003-9861(86)90385-1;
Gross M.D., Eggen M.A., Simon A.M., Van Pilsum J.F.;
"The purification and characterization of human kidney L-
arginine:glycine amidinotransferase.";
Arch. Biochem. Biophys. 251:747-755(1986).
[8]
ACTIVE SITE CYS-407.
PubMed=9148748; DOI=10.1042/bj3220771;
Humm A., Fritsche E., Mann K., Goehl U., Huber R.;
"Recombinant expression and isolation of human L-arginine:glycine
amidinotransferase and identification of its active-site cysteine
residue.";
Biochem. J. 322:771-776(1997).
[9]
REVIEW.
PubMed=9165070;
Humm A., Fritsche E., Steinbacher S.;
"Structure and reaction mechanism of L-arginine:glycine
amidinotransferase.";
Biol. Chem. 378:193-197(1997).
[10]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16820567; DOI=10.1161/CIRCULATIONAHA.105.000448;
Cullen M.E., Yuen A.H., Felkin L.E., Smolenski R.T., Hall J.L.,
Grindle S., Miller L.W., Birks E.J., Yacoub M.H., Barton P.J.;
"Myocardial expression of the arginine:glycine amidinotransferase gene
is elevated in heart failure and normalized after recovery: potential
implications for local creatine synthesis.";
Circulation 114:I16-I20(2006).
[11]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=16125225; DOI=10.1016/j.placenta.2005.07.004;
McMinn J., Wei M., Schupf N., Cusmai J., Johnson E.B., Smith A.C.,
Weksberg R., Thaker H.M., Tycko B.;
"Unbalanced placental expression of imprinted genes in human
intrauterine growth restriction.";
Placenta 27:540-549(2006).
[12]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16614068; DOI=10.1073/pnas.0511031103;
Monk D., Arnaud P., Apostolidou S., Hills F.A., Kelsey G., Stanier P.,
Feil R., Moore G.E.;
"Limited evolutionary conservation of imprinting in the human
placenta.";
Proc. Natl. Acad. Sci. U.S.A. 103:6623-6628(2006).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-385, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[14]
INVOLVEMENT IN CCDS3.
PubMed=20682460; DOI=10.1016/j.ymgme.2010.06.021;
Edvardson S., Korman S.H., Livne A., Shaag A., Saada A.,
Nalbandian R., Allouche-Arnon H., Gomori J.M., Katz-Brull R.;
"l-arginine:glycine amidinotransferase (AGAT) deficiency: clinical
presentation and response to treatment in two patients with a novel
mutation.";
Mol. Genet. Metab. 101:228-232(2010).
[15]
INVOLVEMENT IN CCDS3.
PubMed=22386973; DOI=10.1016/j.ymgme.2012.01.017;
Ndika J.D., Johnston K., Barkovich J.A., Wirt M.D., O'Neill P.,
Betsalel O.T., Jakobs C., Salomons G.S.;
"Developmental progress and creatine restoration upon long-term
creatine supplementation of a patient with arginine:glycine
amidinotransferase deficiency.";
Mol. Genet. Metab. 106:48-54(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-49, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-423.
TISSUE=Kidney;
PubMed=9218780; DOI=10.1093/emboj/16.12.3373;
Humm A., Fritsche E., Steinbacher S., Huber R.;
"Crystal structure and mechanism of human L-arginine:glycine
amidinotransferase: a mitochondrial enzyme involved in creatine
biosynthesis.";
EMBO J. 16:3373-3385(1997).
[19]
X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF MUTANTS ASN-170; ASN-254 AND
SER-407, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, AND
MUTAGENESIS OF ASP-170; GLU-233; ASP-254; HIS-303; ASP-305; ARG-322;
SER-355; CYS-407 AND CYS-410.
PubMed=9266688; DOI=10.1111/j.1432-1033.1997.00483.x;
Fritsche E., Humm A., Huber R.;
"Substrate binding and catalysis by L-arginine:glycine
amidinotransferase -- a mutagenesis and crystallographic study.";
Eur. J. Biochem. 247:483-490(1997).
[20]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-423.
PubMed=9915841; DOI=10.1074/jbc.274.5.3026;
Fritsche E., Humm A., Huber R.;
"The ligand-induced structural changes of human L-arginine:glycine
amidinotransferase. A mutational and crystallographic study.";
J. Biol. Chem. 274:3026-3032(1999).
[21]
INVOLVEMENT IN CCDS3.
PubMed=11555793; DOI=10.1086/323765;
Item C.B., Stockler-Ipsiroglu S., Stromberger C., Muhl A.,
Alessandri M.G., Bianchi M.C., Tosetti M., Fornai F., Cioni G.;
"Arginine:glycine amidinotransferase deficiency: the third inborn
error of creatine metabolism in humans.";
Am. J. Hum. Genet. 69:1127-1133(2001).
[22]
VARIANTS CCDS3 GLN-413 AND TRP-413.
PubMed=23660394; DOI=10.1016/j.ymgme.2013.04.006;
Comeaux M.S., Wang J., Wang G., Kleppe S., Zhang V.W., Schmitt E.S.,
Craigen W.J., Renaud D., Sun Q., Wong L.J.;
"Biochemical, molecular, and clinical diagnoses of patients with
cerebral creatine deficiency syndromes.";
Mol. Genet. Metab. 109:260-268(2013).
[23]
VARIANT CCDS3 SER-203.
PubMed=23770102; DOI=10.1016/j.nmd.2013.04.011;
Nouioua S., Cheillan D., Zaouidi S., Salomons G.S., Amedjout N.,
Kessaci F., Boulahdour N., Hamadouche T., Tazir M.;
"Creatine deficiency syndrome. A treatable myopathy due to arginine-
glycine amidinotransferase (AGAT) deficiency.";
Neuromuscul. Disord. 23:670-674(2013).
[24]
VARIANTS CCDS3 PRO-185; SER-203 AND TRP-413.
PubMed=26490222; DOI=10.1016/j.ymgme.2015.10.003;
Stockler-Ipsiroglu S., Apatean D., Battini R., DeBrosse S.,
Dessoffy K., Edvardson S., Eichler F., Johnston K., Koeller D.M.,
Nouioua S., Tazir M., Verma A., Dowling M.D., Wierenga K.J.,
Wierenga A.M., Zhang V., Wong L.J.;
"Arginine:glycine amidinotransferase (AGAT) deficiency: Clinical
features and long term outcomes in 16 patients diagnosed worldwide.";
Mol. Genet. Metab. 116:252-259(2015).
[25]
VARIANTS CCDS3 GLN-23; VAL-93; ASN-102; LEU-105; LYS-181; PRO-185;
CYS-189; SER-203; THR-208; HIS-282; VAL-329; LEU-346; TRP-413; GLN-413
AND GLN-415, CHARACTERIZATION OF VARIANTS CCDS3 GLN-23; VAL-93;
ASN-102; LEU-105; LYS-181; PRO-185; CYS-189; SER-203; THR-208;
HIS-282; VAL-329; LEU-346; TRP-413; GLN-413 AND GLN-415, VARIANTS
CYS-231 AND GLY-234, CHARACTERIZATION OF VARIANTS CYS-231 AND GLY-234,
AND CATALYTIC ACTIVITY.
PubMed=27233232; DOI=10.1002/humu.23018;
DesRoches C.L., Bruun T., Wang P., Marshall C.R.,
Mercimek-Mahmutoglu S.;
"Arginine-Glycine Amidinotransferase Deficiency and Functional
Characterization of Missense Variants in GATM.";
Hum. Mutat. 37:926-932(2016).
-!- FUNCTION: 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. May be involved in the
response to heart failure by elevating local creatine synthesis.
{ECO:0000269|PubMed:16125225, ECO:0000269|PubMed:16614068,
ECO:0000269|PubMed:16820567}.
-!- CATALYTIC ACTIVITY: L-arginine + glycine = L-ornithine +
guanidinoacetate. {ECO:0000269|PubMed:27233232,
ECO:0000269|PubMed:3800397}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.0 uM for arginine {ECO:0000269|PubMed:3800397,
ECO:0000269|PubMed:9266688};
KM=3.0 uM for glycine {ECO:0000269|PubMed:3800397,
ECO:0000269|PubMed:9266688};
Vmax=0.44 umol/min/mg enzyme {ECO:0000269|PubMed:3800397,
ECO:0000269|PubMed:9266688};
-!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
creatine from L-arginine and glycine: step 1/2.
-!- SUBUNIT: Homodimer. There is an equilibrium between the monomeric
and dimeric forms, shifted towards the side of the monomer.
{ECO:0000269|PubMed:3800397}.
-!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion inner membrane;
Peripheral membrane protein; Intermembrane side. Note=Probably
attached to the outer side of the inner membrane.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Mitochondrial;
IsoId=P50440-1; Sequence=Displayed;
Name=2; Synonyms=Cytoplasmic;
IsoId=P50440-2; Sequence=VSP_000235;
Name=3;
IsoId=P50440-3; Sequence=VSP_039871;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
lung, salivary gland and skeletal muscle tissue, with the highest
expression in kidney. Biallelically expressed in placenta and
fetal tissues. {ECO:0000269|PubMed:16125225,
ECO:0000269|PubMed:16614068, ECO:0000269|PubMed:16820567}.
-!- INDUCTION: Expression is elevated in the myocardium during heart
failure, and decreased in inter-uterine growth restriction (IUGR)-
associated placenta. {ECO:0000269|PubMed:16125225,
ECO:0000269|PubMed:16820567}.
-!- DOMAIN: One chain folds into a compact single domain composed of
repeating units, five beta-beta-alpha-beta modules, which surround
the central active site.
-!- DISEASE: Cerebral creatine deficiency syndrome 3 (CCDS3)
[MIM:612718]: An autosomal recessive disorder characterized by
developmental delay/regression, mental retardation, severe
disturbance of expressive and cognitive speech, and severe
depletion of creatine/phosphocreatine in the brain. Most patients
develop a myopathy characterized by muscle weakness and atrophy
later in life. {ECO:0000269|PubMed:11555793,
ECO:0000269|PubMed:20682460, ECO:0000269|PubMed:22386973,
ECO:0000269|PubMed:23660394, ECO:0000269|PubMed:23770102,
ECO:0000269|PubMed:26490222, ECO:0000269|PubMed:27233232}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the amidinotransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG60595.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; S68805; AAB29892.1; -; mRNA.
EMBL; X86401; CAA60153.1; -; mRNA.
EMBL; AK294995; BAG58060.1; -; mRNA.
EMBL; AK298350; BAG60595.1; ALT_INIT; mRNA.
EMBL; AK223585; BAD97305.1; -; mRNA.
EMBL; AC025580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004141; AAH04141.1; -; mRNA.
CCDS; CCDS10122.1; -. [P50440-1]
PIR; S41734; S41734.
PIR; S54161; S54161.
RefSeq; NP_001473.1; NM_001482.2. [P50440-1]
UniGene; Hs.560354; -.
UniGene; Hs.729565; -.
UniGene; Hs.75335; -.
PDB; 1JDW; X-ray; 1.90 A; A=1-423.
PDB; 1JDX; X-ray; 2.40 A; A=38-423.
PDB; 2JDW; X-ray; 2.10 A; A=1-423.
PDB; 2JDX; X-ray; 2.90 A; A=38-423.
PDB; 3JDW; X-ray; 2.40 A; A=1-423.
PDB; 4JDW; X-ray; 2.50 A; A=1-423.
PDB; 5JDW; X-ray; 2.60 A; A=38-423.
PDB; 6JDW; X-ray; 2.50 A; A=38-423.
PDB; 7JDW; X-ray; 2.37 A; A=38-423.
PDB; 8JDW; X-ray; 2.30 A; A=38-423.
PDB; 9JDW; X-ray; 2.50 A; A=38-423.
PDBsum; 1JDW; -.
PDBsum; 1JDX; -.
PDBsum; 2JDW; -.
PDBsum; 2JDX; -.
PDBsum; 3JDW; -.
PDBsum; 4JDW; -.
PDBsum; 5JDW; -.
PDBsum; 6JDW; -.
PDBsum; 7JDW; -.
PDBsum; 8JDW; -.
PDBsum; 9JDW; -.
DisProt; DP00099; -.
ProteinModelPortal; P50440; -.
SMR; P50440; -.
BioGrid; 108898; 3.
IntAct; P50440; 7.
STRING; 9606.ENSP00000379895; -.
DrugBank; DB04454; Alpha-Aminobutyric Acid.
DrugBank; DB02068; Delta-Amino Valeric Acid.
DrugBank; DB02530; Gamma(Amino)-Butyric Acid.
DrugBank; DB00145; Glycine.
DrugBank; DB00129; L-Ornithine.
DrugBank; DB04185; Norvaline.
iPTMnet; P50440; -.
PhosphoSitePlus; P50440; -.
BioMuta; GATM; -.
DMDM; 1730201; -.
REPRODUCTION-2DPAGE; IPI00032103; -.
MaxQB; P50440; -.
PaxDb; P50440; -.
PeptideAtlas; P50440; -.
PRIDE; P50440; -.
DNASU; 2628; -.
Ensembl; ENST00000396659; ENSP00000379895; ENSG00000171766. [P50440-1]
Ensembl; ENST00000558336; ENSP00000454008; ENSG00000171766. [P50440-3]
GeneID; 2628; -.
KEGG; hsa:2628; -.
UCSC; uc001zvc.4; human. [P50440-1]
CTD; 2628; -.
DisGeNET; 2628; -.
EuPathDB; HostDB:ENSG00000171766.15; -.
GeneCards; GATM; -.
GeneReviews; GATM; -.
HGNC; HGNC:4175; GATM.
HPA; HPA026077; -.
MalaCards; GATM; -.
MIM; 602360; gene.
MIM; 612718; phenotype.
neXtProt; NX_P50440; -.
OpenTargets; ENSG00000171766; -.
Orphanet; 35704; Arginine:glycine amidinotransferase deficiency.
PharmGKB; PA28590; -.
eggNOG; ENOG410IFBR; Eukaryota.
eggNOG; ENOG410Y45M; LUCA.
GeneTree; ENSGT00390000011613; -.
HOGENOM; HOG000231593; -.
HOVERGEN; HBG002492; -.
InParanoid; P50440; -.
KO; K00613; -.
OMA; RPCHQID; -.
OrthoDB; EOG091G07LX; -.
PhylomeDB; P50440; -.
TreeFam; TF300256; -.
BioCyc; MetaCyc:HS10376-MONOMER; -.
BRENDA; 2.1.4.1; 2681.
Reactome; R-HSA-71288; Creatine metabolism.
UniPathway; UPA00104; UER00579.
ChiTaRS; GATM; human.
EvolutionaryTrace; P50440; -.
GeneWiki; GATM_(gene); -.
GenomeRNAi; 2628; -.
PRO; PR:P50440; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000171766; -.
CleanEx; HS_GATM; -.
ExpressionAtlas; P50440; baseline and differential.
Genevisible; P50440; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0015068; F:glycine amidinotransferase activity; IDA:UniProtKB.
GO; GO:0006601; P:creatine biosynthetic process; IDA:MGI.
GO; GO:0006600; P:creatine metabolic process; IMP:CAFA.
GO; GO:0007611; P:learning or memory; IMP:CAFA.
GO; GO:0007275; P:multicellular organism development; IMP:CAFA.
GO; GO:0014889; P:muscle atrophy; IMP:CAFA.
InterPro; IPR033195; AmidinoTrfase.
PANTHER; PTHR10488; PTHR10488; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Disease mutation; Membrane; Mitochondrion;
Mitochondrion inner membrane; Phosphoprotein; Polymorphism;
Reference proteome; Transferase; Transit peptide.
TRANSIT 1 37 Mitochondrion. {ECO:0000250}.
CHAIN 38 423 Glycine amidinotransferase,
mitochondrial.
/FTId=PRO_0000001206.
ACT_SITE 254 254
ACT_SITE 303 303
ACT_SITE 407 407 Amidino-cysteine intermediate.
{ECO:0000269|PubMed:9148748}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 385 385 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 37 MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQ ->
MNILK (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_000235.
VAR_SEQ 388 423 ITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD -> M
YNK (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039871.
VARIANT 23 23 R -> Q (in CCDS3; unknown pathological
significance; reduces glycine
amidinotransferase activity;
dbSNP:rs370155767).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076483.
VARIANT 93 93 I -> V (in CCDS3; unknown pathological
significance; reduces glycine
amidinotransferase activity;
dbSNP:rs34991226).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076484.
VARIANT 102 102 K -> N (in CCDS3; unknown pathological
significance; reduces glycine
amidinotransferase activity;
dbSNP:rs376335787).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076485.
VARIANT 105 105 P -> L (in CCDS3; loss of glycine
amidinotransferase activity;
dbSNP:rs147804855).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076486.
VARIANT 110 110 Q -> H (in dbSNP:rs1288775).
{ECO:0000269|Ref.4}.
/FTId=VAR_020305.
VARIANT 181 181 E -> K (in CCDS3; loss of glycine
amidinotransferase activity;
dbSNP:rs376982466).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076487.
VARIANT 185 185 A -> P (in CCDS3; decreases glycine
amidinotransferase activity).
{ECO:0000269|PubMed:26490222,
ECO:0000269|PubMed:27233232}.
/FTId=VAR_076488.
VARIANT 189 189 R -> C (in CCDS3; loss of glycine
amidinotransferase activity;
dbSNP:rs377578020).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076489.
VARIANT 203 203 Y -> S (in CCDS3; loss of glycine
amidinotransferase activity;
dbSNP:rs397514709).
{ECO:0000269|PubMed:23770102,
ECO:0000269|PubMed:26490222,
ECO:0000269|PubMed:27233232}.
/FTId=VAR_069816.
VARIANT 208 208 A -> T (in CCDS3; loss of glycine
amidinotransferase activity;
dbSNP:rs374059924).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076490.
VARIANT 231 231 S -> C (decreases glycine
amidinotransferase activity;
dbSNP:rs202225656).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076491.
VARIANT 234 234 D -> G (decreases glycine
amidinotransferase activity;
dbSNP:rs146057680).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076492.
VARIANT 282 282 R -> H (in CCDS3; decreases glycine
amidinotransferase activity;
dbSNP:rs371447931).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076493.
VARIANT 329 329 L -> V (in CCDS3; decreases glycine
amidinotransferase activity;
dbSNP:rs373802463).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076494.
VARIANT 346 346 P -> L (in CCDS3; decreases glycine
amidinotransferase activity;
dbSNP:rs142814307).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076495.
VARIANT 413 413 R -> Q (in CCDS3; loss of glycine
amidinotransferase activity).
{ECO:0000269|PubMed:23660394,
ECO:0000269|PubMed:27233232}.
/FTId=VAR_071789.
VARIANT 413 413 R -> W (in CCDS3; loss of glycine
amidinotransferase activity).
{ECO:0000269|PubMed:23660394,
ECO:0000269|PubMed:26490222,
ECO:0000269|PubMed:27233232}.
/FTId=VAR_071790.
VARIANT 415 415 R -> Q (in CCDS3; unknown pathological
significance; reduces glycine
amidinotransferase activity;
dbSNP:rs374592247).
{ECO:0000269|PubMed:27233232}.
/FTId=VAR_076496.
MUTAGEN 170 170 D->N: Complete loss of activity.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 233 233 E->K: Complete loss of activity; when
associated with S-407.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 254 254 D->N: Significantly reduced activity.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 303 303 H->V: Complete loss of activity.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 305 305 D->A: Complete loss of activity.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 322 322 R->E: Significantly reduced activity.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 355 355 S->A: Significantly reduced activity.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 407 407 C->S: Complete loss of activity; when
associated with K-233.
{ECO:0000269|PubMed:9266688}.
MUTAGEN 410 410 C->A: No effect on activity.
{ECO:0000269|PubMed:9266688}.
CONFLICT 98 98 N -> I (in Ref. 3; BAG60595).
{ECO:0000305}.
CONFLICT 246 246 T -> I (in Ref. 3; BAG60595).
{ECO:0000305}.
CONFLICT 384 384 E -> G (in Ref. 3; BAG58060).
{ECO:0000305}.
CONFLICT 395 395 I -> V (in Ref. 3; BAG60595).
{ECO:0000305}.
STRAND 70 73 {ECO:0000244|PDB:1JDW}.
STRAND 75 80 {ECO:0000244|PDB:1JDW}.
HELIX 93 96 {ECO:0000244|PDB:1JDW}.
HELIX 101 103 {ECO:0000244|PDB:1JDW}.
HELIX 104 110 {ECO:0000244|PDB:1JDW}.
STRAND 113 115 {ECO:0000244|PDB:1JDW}.
HELIX 117 136 {ECO:0000244|PDB:1JDW}.
STRAND 140 142 {ECO:0000244|PDB:1JDW}.
STRAND 152 154 {ECO:0000244|PDB:1JDW}.
STRAND 159 161 {ECO:0000244|PDB:1JDW}.
HELIX 168 171 {ECO:0000244|PDB:1JDW}.
STRAND 172 176 {ECO:0000244|PDB:1JDW}.
STRAND 178 181 {ECO:0000244|PDB:1JDW}.
HELIX 187 189 {ECO:0000244|PDB:1JDW}.
HELIX 192 195 {ECO:0000244|PDB:1JDW}.
HELIX 197 205 {ECO:0000244|PDB:1JDW}.
STRAND 209 212 {ECO:0000244|PDB:1JDW}.
HELIX 220 222 {ECO:0000244|PDB:1JDW}.
HELIX 232 240 {ECO:0000244|PDB:1JDW}.
STRAND 248 250 {ECO:0000244|PDB:1JDW}.
HELIX 255 257 {ECO:0000244|PDB:1JDW}.
STRAND 258 261 {ECO:0000244|PDB:1JDW}.
STRAND 264 267 {ECO:0000244|PDB:1JDW}.
HELIX 275 285 {ECO:0000244|PDB:1JDW}.
TURN 286 288 {ECO:0000244|PDB:1JDW}.
STRAND 290 293 {ECO:0000244|PDB:1JDW}.
STRAND 296 298 {ECO:0000244|PDB:1JDW}.
TURN 305 307 {ECO:0000244|PDB:1JDW}.
STRAND 308 312 {ECO:0000244|PDB:1JDW}.
STRAND 315 318 {ECO:0000244|PDB:1JDW}.
HELIX 327 332 {ECO:0000244|PDB:1JDW}.
STRAND 336 338 {ECO:0000244|PDB:1JDW}.
STRAND 352 354 {ECO:0000244|PDB:1JDW}.
HELIX 356 360 {ECO:0000244|PDB:1JDW}.
STRAND 363 366 {ECO:0000244|PDB:1JDW}.
STRAND 369 373 {ECO:0000244|PDB:1JDW}.
HELIX 377 385 {ECO:0000244|PDB:1JDW}.
STRAND 389 393 {ECO:0000244|PDB:1JDW}.
HELIX 396 399 {ECO:0000244|PDB:1JDW}.
TURN 400 402 {ECO:0000244|PDB:1JDW}.
TURN 405 408 {ECO:0000244|PDB:1JDW}.
STRAND 409 415 {ECO:0000244|PDB:1JDW}.
SEQUENCE 423 AA; 48455 MW; 5BEF7A8A039B70FB CRC64;
MLRVRCLRGG SRGAEAVHYI GSRLGRTLTG WVQRTFQSTQ AATASSRNSC AADDKATEPL
PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTIEVKANTY EKYWPFYQKQ GGHYFPKDHL
KKAVAEIEEM CNILKTEGVT VRRPDPIDWS LKYKTPDFES TGLYSAMPRD ILIVVGNEII
EAPMAWRSRF FEYRAYRSII KDYFHRGAKW TTAPKPTMAD ELYNQDYPIH SVEDRHKLAA
QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYLGIEW MRRHLAPDYR VHIISFKDPN
PMHIDATFNI IGPGIVLSNP DRPCHQIDLF KKAGWTIITP PTPIIPDDHP LWMSSKWLSM
NVLMLDEKRV MVDANEVPIQ KMFEKLGITT IKVNIRNANS LGGGFHCWTC DVRRRGTLQS
YLD


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