ID   GATM_HUMAN              Reviewed;         423 AA.
AC   P50440; B4DH99; B4DPI3; Q53EQ4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 217.
DE   RecName: Full=Glycine amidinotransferase, mitochondrial;
DE            EC=2.1.4.1 {ECO:0000269|PubMed:16820567, ECO:0000269|PubMed:27233232, ECO:0000269|PubMed:36543883, ECO:0000269|PubMed:3800397};
DE   AltName: Full=L-arginine:glycine amidinotransferase;
DE   AltName: Full=Transamidinase;
DE   Flags: Precursor;
GN   Name=GATM; Synonyms=AGAT;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=8313955; DOI=10.1016/0014-5793(94)80394-3;
RA   Humm A., Huber R., Mann K.;
RT   "The amino acid sequences of human and pig L-arginine:glycine
RT   amidinotransferase.";
RL   FEBS Lett. 339:101-107(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
RA   Austruy E., Belley L., Millasot P., Junien C., Jeanpierre C.;
RT   "Characterization of the human cDNA with partial homology with the gamma
RT   subunit of sodium potassium ATPase of rat, mouse, rabbit and sheep.";
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Kidney;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-110.
RC   TISSUE=Kidney;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   PATHWAY.
RX   PubMed=3800397; DOI=10.1016/0003-9861(86)90385-1;
RA   Gross M.D., Eggen M.A., Simon A.M., Van Pilsum J.F.;
RT   "The purification and characterization of human kidney L-arginine:glycine
RT   amidinotransferase.";
RL   Arch. Biochem. Biophys. 251:747-755(1986).
RN   [8]
RP   ACTIVE SITE CYS-407.
RX   PubMed=9148748; DOI=10.1042/bj3220771;
RA   Humm A., Fritsche E., Mann K., Goehl U., Huber R.;
RT   "Recombinant expression and isolation of human L-arginine:glycine
RT   amidinotransferase and identification of its active-site cysteine
RT   residue.";
RL   Biochem. J. 322:771-776(1997).
RN   [9]
RP   REVIEW.
RX   PubMed=9165070;
RA   Humm A., Fritsche E., Steinbacher S.;
RT   "Structure and reaction mechanism of L-arginine:glycine
RT   amidinotransferase.";
RL   Biol. Chem. 378:193-197(1997).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16820567; DOI=10.1161/circulationaha.105.000448;
RA   Cullen M.E., Yuen A.H., Felkin L.E., Smolenski R.T., Hall J.L., Grindle S.,
RA   Miller L.W., Birks E.J., Yacoub M.H., Barton P.J.;
RT   "Myocardial expression of the arginine:glycine amidinotransferase gene is
RT   elevated in heart failure and normalized after recovery: potential
RT   implications for local creatine synthesis.";
RL   Circulation 114:I16-I20(2006).
RN   [11]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16125225; DOI=10.1016/j.placenta.2005.07.004;
RA   McMinn J., Wei M., Schupf N., Cusmai J., Johnson E.B., Smith A.C.,
RA   Weksberg R., Thaker H.M., Tycko B.;
RT   "Unbalanced placental expression of imprinted genes in human intrauterine
RT   growth restriction.";
RL   Placenta 27:540-549(2006).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=16614068; DOI=10.1073/pnas.0511031103;
RA   Monk D., Arnaud P., Apostolidou S., Hills F.A., Kelsey G., Stanier P.,
RA   Feil R., Moore G.E.;
RT   "Limited evolutionary conservation of imprinting in the human placenta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6623-6628(2006).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-385, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-49, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [16]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=36543883; DOI=10.1038/s41598-022-26655-4;
RA   Sinn M., Stanoppi M., Hauth F., Fleming J.R., Funck D., Mayans O.,
RA   Hartig J.S.;
RT   "Guanidino acid hydrolysis by the human enzyme annotated as agmatinase.";
RL   Sci. Rep. 12:22088-22088(2022).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 38-423 IN COMPLEX WITH ARGININE,
RP   AND ACTIVE SITE.
RC   TISSUE=Kidney;
RX   PubMed=9218780; DOI=10.1093/emboj/16.12.3373;
RA   Humm A., Fritsche E., Steinbacher S., Huber R.;
RT   "Crystal structure and mechanism of human L-arginine:glycine
RT   amidinotransferase: a mitochondrial enzyme involved in creatine
RT   biosynthesis.";
RL   EMBO J. 16:3373-3385(1997).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF MUTANTS ASN-170; ASN-254 AND
RP   SER-407, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   REACTION MECHANISM, MUTAGENESIS OF ASP-170; GLU-233; ASP-254; HIS-303;
RP   ASP-305; ARG-322; SER-355; CYS-407 AND CYS-410, AND PATHWAY.
RX   PubMed=9266688; DOI=10.1111/j.1432-1033.1997.00483.x;
RA   Fritsche E., Humm A., Huber R.;
RT   "Substrate binding and catalysis by L-arginine:glycine amidinotransferase
RT   -- a mutagenesis and crystallographic study.";
RL   Eur. J. Biochem. 247:483-490(1997).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-423.
RX   PubMed=9915841; DOI=10.1074/jbc.274.5.3026;
RA   Fritsche E., Humm A., Huber R.;
RT   "The ligand-induced structural changes of human L-arginine:glycine
RT   amidinotransferase. A mutational and crystallographic study.";
RL   J. Biol. Chem. 274:3026-3032(1999).
RN   [20]
RP   INVOLVEMENT IN CCDS3.
RX   PubMed=11555793; DOI=10.1086/323765;
RA   Item C.B., Stockler-Ipsiroglu S., Stromberger C., Muhl A., Alessandri M.G.,
RA   Bianchi M.C., Tosetti M., Fornai F., Cioni G.;
RT   "Arginine:glycine amidinotransferase deficiency: the third inborn error of
RT   creatine metabolism in humans.";
RL   Am. J. Hum. Genet. 69:1127-1133(2001).
RN   [21]
RP   INVOLVEMENT IN CCDS3.
RX   PubMed=20682460; DOI=10.1016/j.ymgme.2010.06.021;
RA   Edvardson S., Korman S.H., Livne A., Shaag A., Saada A., Nalbandian R.,
RA   Allouche-Arnon H., Gomori J.M., Katz-Brull R.;
RT   "l-arginine:glycine amidinotransferase (AGAT) deficiency: clinical
RT   presentation and response to treatment in two patients with a novel
RT   mutation.";
RL   Mol. Genet. Metab. 101:228-232(2010).
RN   [22]
RP   INVOLVEMENT IN CCDS3.
RX   PubMed=22386973; DOI=10.1016/j.ymgme.2012.01.017;
RA   Ndika J.D., Johnston K., Barkovich J.A., Wirt M.D., O'Neill P.,
RA   Betsalel O.T., Jakobs C., Salomons G.S.;
RT   "Developmental progress and creatine restoration upon long-term creatine
RT   supplementation of a patient with arginine:glycine amidinotransferase
RT   deficiency.";
RL   Mol. Genet. Metab. 106:48-54(2012).
RN   [23]
RP   VARIANTS CCDS3 GLN-413 AND TRP-413.
RX   PubMed=23660394; DOI=10.1016/j.ymgme.2013.04.006;
RA   Comeaux M.S., Wang J., Wang G., Kleppe S., Zhang V.W., Schmitt E.S.,
RA   Craigen W.J., Renaud D., Sun Q., Wong L.J.;
RT   "Biochemical, molecular, and clinical diagnoses of patients with cerebral
RT   creatine deficiency syndromes.";
RL   Mol. Genet. Metab. 109:260-268(2013).
RN   [24]
RP   VARIANT CCDS3 SER-203.
RX   PubMed=23770102; DOI=10.1016/j.nmd.2013.04.011;
RA   Nouioua S., Cheillan D., Zaouidi S., Salomons G.S., Amedjout N.,
RA   Kessaci F., Boulahdour N., Hamadouche T., Tazir M.;
RT   "Creatine deficiency syndrome. A treatable myopathy due to arginine-glycine
RT   amidinotransferase (AGAT) deficiency.";
RL   Neuromuscul. Disord. 23:670-674(2013).
RN   [25]
RP   VARIANTS CCDS3 PRO-185; SER-203 AND TRP-413.
RX   PubMed=26490222; DOI=10.1016/j.ymgme.2015.10.003;
RA   Stockler-Ipsiroglu S., Apatean D., Battini R., DeBrosse S., Dessoffy K.,
RA   Edvardson S., Eichler F., Johnston K., Koeller D.M., Nouioua S., Tazir M.,
RA   Verma A., Dowling M.D., Wierenga K.J., Wierenga A.M., Zhang V., Wong L.J.;
RT   "Arginine:glycine amidinotransferase (AGAT) deficiency: Clinical features
RT   and long term outcomes in 16 patients diagnosed worldwide.";
RL   Mol. Genet. Metab. 116:252-259(2015).
RN   [26]
RP   VARIANTS CCDS3 GLN-23; VAL-93; ASN-102; LEU-105; LYS-181; PRO-185; CYS-189;
RP   SER-203; THR-208; HIS-282; VAL-329; LEU-346; TRP-413; GLN-413 AND GLN-415,
RP   CHARACTERIZATION OF VARIANTS CCDS3 GLN-23; VAL-93; ASN-102; LEU-105;
RP   LYS-181; PRO-185; CYS-189; SER-203; THR-208; HIS-282; VAL-329; LEU-346;
RP   TRP-413; GLN-413 AND GLN-415, VARIANTS CYS-231 AND GLY-234,
RP   CHARACTERIZATION OF VARIANTS CYS-231 AND GLY-234, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=27233232; DOI=10.1002/humu.23018;
RA   DesRoches C.L., Bruun T., Wang P., Marshall C.R., Mercimek-Mahmutoglu S.;
RT   "Arginine-Glycine Amidinotransferase Deficiency and Functional
RT   Characterization of Missense Variants in GATM.";
RL   Hum. Mutat. 37:926-932(2016).
RN   [27]
RP   VARIANTS FRTS1 SER-320; ALA-336; ILE-336 AND LEU-341, INVOLVEMENT IN FRTS1,
RP   AND CHARACTERIZATION OF VARIANTS FRTS1 SER-320; ALA-336; ILE-336 AND
RP   LEU-341.
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: Transamidinase that catalyzes the transfer of the amidino
CC       group of L-arginine onto the amino moiety of acceptor metabolites such
CC       as glycine, beta-alanine, gamma-aminobutyric acid (GABA) and taurine
CC       yielding the corresponding guanidine derivatives (PubMed:3800397,
CC       PubMed:16820567, PubMed:36543883, PubMed:27233232). Catalyzes the rate-
CC       limiting step of creatine biosynthesis, namely the transfer of the
CC       amidino group from L-arginine to glycine to generate guanidinoacetate,
CC       which is then methylated by GAMT to form creatine. Provides creatine as
CC       a source for ATP generation in tissues with high energy demands, in
CC       particular skeletal muscle, heart and brain (PubMed:3800397,
CC       PubMed:36543883, PubMed:9266688, PubMed:27233232) (Probable).
CC       {ECO:0000269|PubMed:16820567, ECO:0000269|PubMed:27233232,
CC       ECO:0000269|PubMed:36543883, ECO:0000269|PubMed:3800397,
CC       ECO:0000269|PubMed:9266688, ECO:0000305|PubMed:16820567}.
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:0000269|PubMed:27233232, ECO:0000269|PubMed:36543883,
CC         ECO:0000269|PubMed:3800397, ECO:0000269|PubMed:9266688,
CC         ECO:0000305|PubMed:16820567};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13202;
CC         Evidence={ECO:0000305|PubMed:16820567, ECO:0000305|PubMed:27233232,
CC         ECO:0000305|PubMed:36543883, ECO:0000305|PubMed:3800397,
CC         ECO:0000305|PubMed:9266688};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate + L-arginine = 4-guanidinobutanoate + L-
CC         ornithine; Xref=Rhea:RHEA:75939, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57486, ChEBI:CHEBI:59888;
CC         Evidence={ECO:0000269|PubMed:36543883};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75940;
CC         Evidence={ECO:0000305|PubMed:36543883};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-alanine + L-arginine = 3-guanidinopropanoate + L-
CC         ornithine; Xref=Rhea:RHEA:75943, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57593, ChEBI:CHEBI:57966;
CC         Evidence={ECO:0000269|PubMed:36543883};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75944;
CC         Evidence={ECO:0000305|PubMed:36543883};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine + taurine = L-ornithine + taurocyamine;
CC         Xref=Rhea:RHEA:75947, ChEBI:CHEBI:32682, ChEBI:CHEBI:46911,
CC         ChEBI:CHEBI:58064, ChEBI:CHEBI:507393;
CC         Evidence={ECO:0000269|PubMed:36543883};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75948;
CC         Evidence={ECO:0000305|PubMed:36543883};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 uM for L-arginine {ECO:0000269|PubMed:3800397,
CC         ECO:0000269|PubMed:9266688};
CC         KM=3 uM for glycine {ECO:0000269|PubMed:3800397,
CC         ECO:0000269|PubMed:9266688};
CC         Vmax=0.44 umol/min/mg enzyme {ECO:0000269|PubMed:3800397,
CC         ECO:0000269|PubMed:9266688};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC       creatine from L-arginine and glycine: step 1/2.
CC       {ECO:0000305|PubMed:16820567, ECO:0000305|PubMed:36543883,
CC       ECO:0000305|PubMed:3800397, ECO:0000305|PubMed:9266688}.
CC   -!- SUBUNIT: Homodimer. There is an equilibrium between the monomeric and
CC       dimeric forms, shifted towards the side of the monomer.
CC       {ECO:0000269|PubMed:3800397}.
CC   -!- INTERACTION:
CC       P50440; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2552594, EBI-10173507;
CC       P50440; Q14457: BECN1; NbExp=3; IntAct=EBI-2552594, EBI-949378;
CC       P50440; Q9Y6G5: COMMD10; NbExp=3; IntAct=EBI-2552594, EBI-1550310;
CC       P50440; Q9UI10: EIF2B4; NbExp=3; IntAct=EBI-2552594, EBI-2340132;
CC       P50440; Q13322-4: GRB10; NbExp=3; IntAct=EBI-2552594, EBI-12353035;
CC       P50440; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-2552594, EBI-712105;
CC       P50440; Q14693: LPIN1; NbExp=3; IntAct=EBI-2552594, EBI-5278370;
CC       P50440; Q96CM3: RPUSD4; NbExp=3; IntAct=EBI-2552594, EBI-7825200;
CC       P50440; P11684: SCGB1A1; NbExp=3; IntAct=EBI-2552594, EBI-7797649;
CC       P50440; Q9P1W8: SIRPG; NbExp=3; IntAct=EBI-2552594, EBI-1268284;
CC       P50440; Q8NFB2: TMEM185A; NbExp=3; IntAct=EBI-2552594, EBI-21757569;
CC       P50440; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-2552594, EBI-2505861;
CC       P50440; Q6ZMY6-2: WDR88; NbExp=3; IntAct=EBI-2552594, EBI-25857007;
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion inner membrane;
CC       Peripheral membrane protein; Intermembrane side. Note=Probably attached
CC       to the outer side of the inner membrane.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Mitochondrial;
CC         IsoId=P50440-1; Sequence=Displayed;
CC       Name=2; Synonyms=Cytoplasmic;
CC         IsoId=P50440-2; Sequence=VSP_000235;
CC       Name=3;
CC         IsoId=P50440-3; Sequence=VSP_039871;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC       salivary gland and skeletal muscle tissue, with the highest expression
CC       in kidney. Biallelically expressed in placenta and fetal tissues.
CC       {ECO:0000269|PubMed:16125225, ECO:0000269|PubMed:16614068,
CC       ECO:0000269|PubMed:16820567}.
CC   -!- INDUCTION: Expression is elevated in the myocardium during heart
CC       failure, and decreased in inter-uterine growth restriction (IUGR)-
CC       associated placenta. {ECO:0000269|PubMed:16125225,
CC       ECO:0000269|PubMed:16820567}.
CC   -!- DOMAIN: One chain folds into a compact single domain composed of
CC       repeating units, five beta-beta-alpha-beta modules, which surround the
CC       central active site.
CC   -!- DISEASE: Cerebral creatine deficiency syndrome 3 (CCDS3) [MIM:612718]:
CC       An autosomal recessive disorder characterized by developmental
CC       delay/regression, intellectual disability, severe disturbance of
CC       expressive and cognitive speech, and severe depletion of
CC       creatine/phosphocreatine in the brain. Most patients develop a myopathy
CC       characterized by muscle weakness and atrophy later in life.
CC       {ECO:0000269|PubMed:11555793, ECO:0000269|PubMed:20682460,
CC       ECO:0000269|PubMed:22386973, ECO:0000269|PubMed:23660394,
CC       ECO:0000269|PubMed:23770102, ECO:0000269|PubMed:26490222,
CC       ECO:0000269|PubMed:27233232}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Fanconi renotubular syndrome 1 (FRTS1) [MIM:134600]: A form of
CC       Fanconi renotubular syndrome, a disease due to a generalized
CC       dysfunction of the proximal kidney tubule resulting in decreased solute
CC       and water reabsorption. Patients have polydipsia and polyuria with
CC       phosphaturia, glycosuria and aminoaciduria. They may develop
CC       hypophosphatemic rickets or osteomalacia, acidosis and a tendency
CC       toward dehydration. Some eventually develop renal insufficiency. FRTS1
CC       inheritance is autosomal dominant. {ECO:0000269|PubMed:29654216}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG60595.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; S68805; AAB29892.1; -; mRNA.
DR   EMBL; X86401; CAA60153.1; -; mRNA.
DR   EMBL; AK294995; BAG58060.1; -; mRNA.
DR   EMBL; AK298350; BAG60595.1; ALT_INIT; mRNA.
DR   EMBL; AK223585; BAD97305.1; -; mRNA.
DR   EMBL; AC025580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC004141; AAH04141.1; -; mRNA.
DR   CCDS; CCDS10122.1; -. [P50440-1]
DR   PIR; S41734; S41734.
DR   PIR; S54161; S54161.
DR   RefSeq; NP_001473.1; NM_001482.2. [P50440-1]
DR   PDB; 1JDW; X-ray; 1.90 A; A=1-423.
DR   PDB; 1JDX; X-ray; 2.40 A; A=38-423.
DR   PDB; 2JDW; X-ray; 2.10 A; A=1-423.
DR   PDB; 2JDX; X-ray; 2.90 A; A=38-423.
DR   PDB; 3JDW; X-ray; 2.40 A; A=1-423.
DR   PDB; 4JDW; X-ray; 2.50 A; A=1-423.
DR   PDB; 5JDW; X-ray; 2.60 A; A=38-423.
DR   PDB; 6JDW; X-ray; 2.50 A; A=38-423.
DR   PDB; 7JDW; X-ray; 2.37 A; A=38-423.
DR   PDB; 8JDW; X-ray; 2.30 A; A=38-423.
DR   PDB; 9JDW; X-ray; 2.50 A; A=38-423.
DR   PDBsum; 1JDW; -.
DR   PDBsum; 1JDX; -.
DR   PDBsum; 2JDW; -.
DR   PDBsum; 2JDX; -.
DR   PDBsum; 3JDW; -.
DR   PDBsum; 4JDW; -.
DR   PDBsum; 5JDW; -.
DR   PDBsum; 6JDW; -.
DR   PDBsum; 7JDW; -.
DR   PDBsum; 8JDW; -.
DR   PDBsum; 9JDW; -.
DR   AlphaFoldDB; P50440; -.
DR   SMR; P50440; -.
DR   BioGRID; 108898; 12.
DR   IntAct; P50440; 24.
DR   STRING; 9606.ENSP00000379895; -.
DR   DrugBank; DB04454; Alpha-Aminobutyric Acid.
DR   DrugBank; DB02068; Delta-Amino Valeric Acid.
DR   DrugBank; DB02530; gamma-Aminobutyric acid.
DR   DrugBank; DB00145; Glycine.
DR   DrugBank; DB04185; Norvaline.
DR   DrugBank; DB00129; Ornithine.
DR   iPTMnet; P50440; -.
DR   PhosphoSitePlus; P50440; -.
DR   SwissPalm; P50440; -.
DR   BioMuta; GATM; -.
DR   DMDM; 1730201; -.
DR   REPRODUCTION-2DPAGE; IPI00032103; -.
DR   EPD; P50440; -.
DR   jPOST; P50440; -.
DR   MassIVE; P50440; -.
DR   MaxQB; P50440; -.
DR   PaxDb; 9606-ENSP00000379895; -.
DR   PeptideAtlas; P50440; -.
DR   ProteomicsDB; 56222; -. [P50440-1]
DR   ProteomicsDB; 56223; -. [P50440-2]
DR   ProteomicsDB; 56224; -. [P50440-3]
DR   Pumba; P50440; -.
DR   Antibodypedia; 11803; 362 antibodies from 28 providers.
DR   DNASU; 2628; -.
DR   Ensembl; ENST00000396659.8; ENSP00000379895.3; ENSG00000171766.17. [P50440-1]
DR   Ensembl; ENST00000558336.5; ENSP00000454008.1; ENSG00000171766.17. [P50440-3]
DR   Ensembl; ENST00000675323.1; ENSP00000502445.1; ENSG00000171766.17. [P50440-3]
DR   GeneID; 2628; -.
DR   KEGG; hsa:2628; -.
DR   MANE-Select; ENST00000396659.8; ENSP00000379895.3; NM_001482.3; NP_001473.1.
DR   UCSC; uc001zvc.4; human. [P50440-1]
DR   AGR; HGNC:4175; -.
DR   CTD; 2628; -.
DR   DisGeNET; 2628; -.
DR   GeneCards; GATM; -.
DR   GeneReviews; GATM; -.
DR   HGNC; HGNC:4175; GATM.
DR   HPA; ENSG00000171766; Group enriched (kidney, liver, pancreas).
DR   MalaCards; GATM; -.
DR   MIM; 134600; phenotype.
DR   MIM; 602360; gene.
DR   MIM; 612718; phenotype.
DR   neXtProt; NX_P50440; -.
DR   OpenTargets; ENSG00000171766; -.
DR   Orphanet; 35704; L-Arginine:glycine amidinotransferase deficiency.
DR   Orphanet; 3337; Primary Fanconi renotubular syndrome.
DR   PharmGKB; PA28590; -.
DR   VEuPathDB; HostDB:ENSG00000171766; -.
DR   eggNOG; ENOG502QVCA; Eukaryota.
DR   GeneTree; ENSGT00390000011613; -.
DR   HOGENOM; CLU_047415_1_0_1; -.
DR   InParanoid; P50440; -.
DR   OMA; SHNEWDP; -.
DR   OrthoDB; 2347075at2759; -.
DR   PhylomeDB; P50440; -.
DR   TreeFam; TF300256; -.
DR   BioCyc; MetaCyc:HS10376-MONOMER; -.
DR   BRENDA; 2.1.4.1; 2681.
DR   PathwayCommons; P50440; -.
DR   Reactome; R-HSA-71288; Creatine metabolism.
DR   SABIO-RK; P50440; -.
DR   SignaLink; P50440; -.
DR   UniPathway; UPA00104; UER00579.
DR   BioGRID-ORCS; 2628; 7 hits in 1151 CRISPR screens.
DR   ChiTaRS; GATM; human.
DR   EvolutionaryTrace; P50440; -.
DR   GeneWiki; GATM_(gene); -.
DR   GenomeRNAi; 2628; -.
DR   Pharos; P50440; Tbio.
DR   PRO; PR:P50440; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P50440; Protein.
DR   Bgee; ENSG00000171766; Expressed in body of pancreas and 207 other cell types or tissues.
DR   ExpressionAtlas; P50440; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0015067; F:amidinotransferase activity; IDA:UniProtKB.
DR   GO; GO:0015068; F:glycine amidinotransferase activity; IDA:UniProtKB.
DR   GO; GO:0006601; P:creatine biosynthetic process; IDA:MGI.
DR   GO; GO:0006600; P:creatine metabolic process; IMP:CAFA.
DR   GO; GO:0007611; P:learning or memory; IMP:CAFA.
DR   GO; GO:0014889; P:muscle atrophy; IMP:CAFA.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   CDD; cd21136; amidinotransferase_AGAT-like; 1.
DR   DisProt; DP00099; -.
DR   InterPro; IPR033195; AmidinoTrfase.
DR   PANTHER; PTHR10488; GLYCINE AMIDINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10488:SF1; GLYCINE AMIDINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   SUPFAM; SSF55909; Pentein; 1.
DR   Genevisible; P50440; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Disease variant; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Phosphoprotein; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..423
FT                   /note="Glycine amidinotransferase, mitochondrial"
FT                   /id="PRO_0000001206"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   ACT_SITE        407
FT                   /note="Amidino-cysteine intermediate"
FT                   /evidence="ECO:0000269|PubMed:9148748,
FT                   ECO:0000269|PubMed:9218780, ECO:0007744|PDB:4JDW"
FT   BINDING         170
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   BINDING         305
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   BINDING         322
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   BINDING         354
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   BINDING         355
FT                   /ligand="arginine"
FT                   /ligand_id="ChEBI:CHEBI:32696"
FT                   /evidence="ECO:0000269|PubMed:9218780,
FT                   ECO:0007744|PDB:4JDW"
FT   MOD_RES         46
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         385
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..37
FT                   /note="MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQ -> MNILK (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_000235"
FT   VAR_SEQ         388..423
FT                   /note="ITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD -> MYNK (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_039871"
FT   VARIANT         23
FT                   /note="R -> Q (in CCDS3; uncertain significance; reduces
FT                   glycine amidinotransferase activity; dbSNP:rs370155767)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076483"
FT   VARIANT         93
FT                   /note="I -> V (in CCDS3; uncertain significance; reduces
FT                   glycine amidinotransferase activity; dbSNP:rs34991226)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076484"
FT   VARIANT         102
FT                   /note="K -> N (in CCDS3; uncertain significance; reduces
FT                   glycine amidinotransferase activity; dbSNP:rs376335787)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076485"
FT   VARIANT         105
FT                   /note="P -> L (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs147804855)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076486"
FT   VARIANT         110
FT                   /note="Q -> H (in dbSNP:rs1288775)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_020305"
FT   VARIANT         181
FT                   /note="E -> K (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs376982466)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076487"
FT   VARIANT         185
FT                   /note="A -> P (in CCDS3; decreases glycine
FT                   amidinotransferase activity)"
FT                   /evidence="ECO:0000269|PubMed:26490222,
FT                   ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076488"
FT   VARIANT         189
FT                   /note="R -> C (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs377578020)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076489"
FT   VARIANT         203
FT                   /note="Y -> S (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs397514709)"
FT                   /evidence="ECO:0000269|PubMed:23770102,
FT                   ECO:0000269|PubMed:26490222, ECO:0000269|PubMed:27233232"
FT                   /id="VAR_069816"
FT   VARIANT         208
FT                   /note="A -> T (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs374059924)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076490"
FT   VARIANT         231
FT                   /note="S -> C (decreases glycine amidinotransferase
FT                   activity; dbSNP:rs202225656)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076491"
FT   VARIANT         234
FT                   /note="D -> G (decreases glycine amidinotransferase
FT                   activity; dbSNP:rs146057680)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076492"
FT   VARIANT         282
FT                   /note="R -> H (in CCDS3; decreases glycine
FT                   amidinotransferase activity; dbSNP:rs371447931)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076493"
FT   VARIANT         320
FT                   /note="P -> S (in FRTS1; results in GATM protein
FT                   aggregation; GATM deposits affect mitochondrial morphology
FT                   leading to abnormal and elongated mitochondria;
FT                   dbSNP:rs1889443535)"
FT                   /evidence="ECO:0000269|PubMed:29654216"
FT                   /id="VAR_084378"
FT   VARIANT         329
FT                   /note="L -> V (in CCDS3; decreases glycine
FT                   amidinotransferase activity; dbSNP:rs373802463)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076494"
FT   VARIANT         336
FT                   /note="T -> A (in FRTS1; results in GATM protein
FT                   aggregation; GATM deposits affect mitochondrial morphology
FT                   leading to abnormal and elongated mitochondria;
FT                   dbSNP:rs1889422994)"
FT                   /evidence="ECO:0000269|PubMed:29654216"
FT                   /id="VAR_084379"
FT   VARIANT         336
FT                   /note="T -> I (in FRTS1; results in GATM protein
FT                   aggregation; GATM deposits affect mitochondrial morphology
FT                   and results in increased ROS production, activation of the
FT                   NLRP3 inflammasome and enhanced expression of the
FT                   profibrotic cytokine IL-18)"
FT                   /evidence="ECO:0000269|PubMed:29654216"
FT                   /id="VAR_084380"
FT   VARIANT         341
FT                   /note="P -> L (in FRTS1; results in GATM protein
FT                   aggregation; GATM deposits affect mitochondrial morphology
FT                   leading to abnormal and elongated mitochondria;
FT                   dbSNP:rs1889422661)"
FT                   /evidence="ECO:0000269|PubMed:29654216"
FT                   /id="VAR_084381"
FT   VARIANT         346
FT                   /note="P -> L (in CCDS3; decreases glycine
FT                   amidinotransferase activity; dbSNP:rs142814307)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076495"
FT   VARIANT         413
FT                   /note="R -> Q (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs1461653218)"
FT                   /evidence="ECO:0000269|PubMed:23660394,
FT                   ECO:0000269|PubMed:27233232"
FT                   /id="VAR_071789"
FT   VARIANT         413
FT                   /note="R -> W (in CCDS3; loss of glycine amidinotransferase
FT                   activity; dbSNP:rs1244824806)"
FT                   /evidence="ECO:0000269|PubMed:23660394,
FT                   ECO:0000269|PubMed:26490222, ECO:0000269|PubMed:27233232"
FT                   /id="VAR_071790"
FT   VARIANT         415
FT                   /note="R -> Q (in CCDS3; uncertain significance; reduces
FT                   glycine amidinotransferase activity; dbSNP:rs374592247)"
FT                   /evidence="ECO:0000269|PubMed:27233232"
FT                   /id="VAR_076496"
FT   MUTAGEN         170
FT                   /note="D->N: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         233
FT                   /note="E->K: Complete loss of activity; when associated
FT                   with S-407."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         254
FT                   /note="D->N: Significantly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         303
FT                   /note="H->V: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         305
FT                   /note="D->A: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         322
FT                   /note="R->E: Significantly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         355
FT                   /note="S->A: Significantly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         407
FT                   /note="C->S: Complete loss of activity; when associated
FT                   with K-233."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   MUTAGEN         410
FT                   /note="C->A: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:9266688"
FT   CONFLICT        98
FT                   /note="N -> I (in Ref. 3; BAG60595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        246
FT                   /note="T -> I (in Ref. 3; BAG60595)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        384
FT                   /note="E -> G (in Ref. 3; BAG58060)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        395
FT                   /note="I -> V (in Ref. 3; BAG60595)"
FT                   /evidence="ECO:0000305"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          75..80
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           104..110
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           117..136
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          152..154
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          159..161
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           168..171
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          178..181
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           192..195
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           197..205
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          209..212
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           220..222
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           232..240
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          248..250
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          258..261
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          264..267
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           275..285
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   TURN            286..288
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          290..293
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          308..312
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          315..318
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           327..332
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          352..354
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           356..360
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          363..366
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          369..373
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           377..385
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          389..393
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   HELIX           396..399
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   TURN            400..402
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   TURN            405..408
FT                   /evidence="ECO:0007829|PDB:1JDW"
FT   STRAND          409..415
FT                   /evidence="ECO:0007829|PDB:1JDW"
SQ   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
//