GATM_PIG
ID GATM_PIG Reviewed; 423 AA.
AC P50441; B3F4S6; Q6IU00;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Glycine amidinotransferase, mitochondrial;
DE EC=2.1.4.1 {ECO:0000250|UniProtKB:P50440};
DE AltName: Full=L-arginine:glycine amidinotransferase;
DE AltName: Full=Transamidinase;
DE Flags: Precursor;
GN Name=GATM; Synonyms=AGAT;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17660697; DOI=10.1266/ggs.82.265;
RA Zhou Q.Y., Huang J.N., Xiong Y.Z., Zhao S.H.;
RT "Imprinting analyses of the porcine GATM and PEG10 genes in placentas on
RT days 75 and 90 of gestation.";
RL Genes Genet. Syst. 82:265-269(2007).
RN [2]
RP PROTEIN SEQUENCE OF 38-423.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 123-362.
RA Zink R.M., Westberg M.C., Van Pilsum J.F.;
RT "The comparative cDNA sequences of some mammalian kidney L-arginine:glycine
RT amidinotransferase genes and their evolutionary significance.";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the biosynthesis of guanidinoacetate, the immediate
CC precursor of creatine. Creatine plays a vital role in energy metabolism
CC in muscle tissues. May play a role in embryonic and central nervous
CC system development (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:P50440};
CC -!- PATHWAY: Amine and polyamine biosynthesis; creatine biosynthesis;
CC creatine from L-arginine and glycine: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Kidney. Expressed biallelically in placenta.
CC {ECO:0000269|PubMed:17660697}.
CC -!- DEVELOPMENTAL STAGE: Expressed in placenta on days 75 and 90 of
CC gestation. {ECO:0000269|PubMed:17660697}.
CC -!- SIMILARITY: Belongs to the amidinotransferase family. {ECO:0000305}.
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DR EMBL; EF612462; ABS83814.1; -; mRNA.
DR EMBL; AY625268; AAT39894.1; -; mRNA.
DR PIR; S40296; S40296.
DR RefSeq; NP_001121914.1; NM_001128442.1.
DR AlphaFoldDB; P50441; -.
DR SMR; P50441; -.
DR STRING; 9823.ENSSSCP00000005032; -.
DR PaxDb; P50441; -.
DR PeptideAtlas; P50441; -.
DR PRIDE; P50441; -.
DR Ensembl; ENSSSCT00000005158; ENSSSCP00000005032; ENSSSCG00000004672.
DR Ensembl; ENSSSCT00015063751; ENSSSCP00015025524; ENSSSCG00015047679.
DR Ensembl; ENSSSCT00025066098; ENSSSCP00025028231; ENSSSCG00025048545.
DR Ensembl; ENSSSCT00030086703; ENSSSCP00030039989; ENSSSCG00030062004.
DR Ensembl; ENSSSCT00035040519; ENSSSCP00035016203; ENSSSCG00035030607.
DR Ensembl; ENSSSCT00040082194; ENSSSCP00040035776; ENSSSCG00040060383.
DR Ensembl; ENSSSCT00045002451; ENSSSCP00045001568; ENSSSCG00045001532.
DR Ensembl; ENSSSCT00050108069; ENSSSCP00050047870; ENSSSCG00050078417.
DR Ensembl; ENSSSCT00055025689; ENSSSCP00055020416; ENSSSCG00055013048.
DR Ensembl; ENSSSCT00060056129; ENSSSCP00060023980; ENSSSCG00060041404.
DR Ensembl; ENSSSCT00065078180; ENSSSCP00065034003; ENSSSCG00065057102.
DR Ensembl; ENSSSCT00070000066; ENSSSCP00070000060; ENSSSCG00070000042.
DR GeneID; 100126844; -.
DR KEGG; ssc:100126844; -.
DR CTD; 2628; -.
DR VGNC; VGNC:88372; GATM.
DR eggNOG; ENOG502QVCA; Eukaryota.
DR GeneTree; ENSGT00390000011613; -.
DR HOGENOM; CLU_047415_1_0_1; -.
DR InParanoid; P50441; -.
DR OMA; SHNEWDP; -.
DR OrthoDB; 636718at2759; -.
DR TreeFam; TF300256; -.
DR Reactome; R-SSC-71288; Creatine metabolism.
DR UniPathway; UPA00104; UER00579.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004672; Expressed in metanephros cortex and 43 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0015067; F:amidinotransferase activity; IBA:GO_Central.
DR GO; GO:0015068; F:glycine amidinotransferase activity; ISS:UniProtKB.
DR GO; GO:0006601; P:creatine biosynthetic process; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0014889; P:muscle atrophy; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR InterPro; IPR033195; AmidinoTrfase.
DR PANTHER; PTHR10488; PTHR10488; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8313955"
FT CHAIN 38..423
FT /note="Glycine amidinotransferase, mitochondrial"
FT /id="PRO_0000215474"
FT ACT_SITE 254
FT /evidence="ECO:0000250"
FT ACT_SITE 303
FT /evidence="ECO:0000250"
FT ACT_SITE 407
FT /note="Amidino-cysteine intermediate"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50440"
FT MOD_RES 385
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50440"
SQ SEQUENCE 423 AA; 48360 MW; F83FC21A1B14B018 CRC64;
MLRVRCLRGG SRGAEALHYI GSRLGRTVTG WVQRTFQSTQ AATASSGNSC AADDKATDPL
PKDCPVSSYN EWDPLEEVIV GRAENACVPP FTVEVKANTY EKYWPFYQKY GGHYFPKDHL
KKAVAEIEEM CNILKMEGVT VRRPDPIDWS VKYKTPDFES TGLYGAMPRD ILIVVGNEII
EAPMAWRARF FEYRAYRSII KDYFRRGAKW TTAPKPTMAD ELYDQDYPIY SVEDRHKLAA
QGKFVTTEFE PCFDAADFIR AGRDIFAQRS QVTNYMGIEW MRKHLAPDYR VHIISFKDPN
PMHIDATFNI IGPGLVLSNP DRPCHQIDLF KKAGWTIVTP PIPVIPDDHP LWMSSKWLSM
NVLMLDEKRV MVDANEVPIQ KMFEKLGIST IKISIRNANS LGGGFHCWTC DVRRRGTLQS
YFD
