ARMT1_RAT
ID ARMT1_RAT Reviewed; 439 AA.
AC Q6AYT5;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Damage-control phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:Q04371};
DE AltName: Full=Acidic residue methyltransferase 1 {ECO:0000250|UniProtKB:Q9H993};
DE AltName: Full=Protein-glutamate O-methyltransferase {ECO:0000250|UniProtKB:Q9H993};
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q9H993};
DE AltName: Full=Sugar phosphate phosphatase ARMT1 {ECO:0000250|UniProtKB:Q04371};
GN Name=Armt1 {ECO:0000250|UniProtKB:Q9H993};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Metal-dependent phosphatase that shows phosphatase activity
CC against several substrates, including fructose-1-phosphate and
CC fructose-6-phosphate (By similarity). Its preference for fructose-1-
CC phosphate, a strong glycating agent that causes DNA damage rather than
CC a canonical yeast metabolite, suggests a damage-control function in
CC hexose phosphate metabolism (By similarity). Has also been shown to
CC have O-methyltransferase activity that methylates glutamate residues of
CC target proteins to form gamma-glutamyl methyl ester residues (By
CC similarity). Possibly methylates PCNA, suggesting it is involved in the
CC DNA damage response (By similarity). {ECO:0000250|UniProtKB:Q04371,
CC ECO:0000250|UniProtKB:Q9H993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate + H2O = D-fructose + phosphate;
CC Xref=Rhea:RHEA:35603, ChEBI:CHEBI:15377, ChEBI:CHEBI:37721,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138881;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 6-phosphate = D-glyceraldehyde 3-phosphate +
CC dihydroxyacetone; Xref=Rhea:RHEA:28002, ChEBI:CHEBI:16016,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; Evidence={ECO:0000250|UniProtKB:Q9H993};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q04371};
CC -!- DOMAIN: Subfamily III proteins have a conserved RTxK motif about 40-50
CC residues from the C-terminus; the threonine may be replaced by serine
CC or cysteine. {ECO:0000250|UniProtKB:Q04371}.
CC -!- PTM: Automethylated. {ECO:0000250|UniProtKB:Q9H993}.
CC -!- SIMILARITY: Belongs to the damage-control phosphatase family. Sugar
CC phosphate phosphatase III subfamily. {ECO:0000305}.
CC -!- CAUTION: Human C6orf211 has been reportedly associated with a protein
CC carboxyl methyltransferase activity, but whether this protein indeed
CC has such an activity remains to be determined (By similarity). It has
CC been later shown to belong to a family of metal-dependent phosphatases
CC implicated in metabolite damage-control (By similarity).
CC {ECO:0000250|UniProtKB:Q9H993}.
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DR EMBL; BC078920; AAH78920.1; -; mRNA.
DR RefSeq; NP_001017447.1; NM_001017447.1.
DR AlphaFoldDB; Q6AYT5; -.
DR SMR; Q6AYT5; -.
DR STRING; 10116.ENSRNOP00000026367; -.
DR iPTMnet; Q6AYT5; -.
DR PhosphoSitePlus; Q6AYT5; -.
DR jPOST; Q6AYT5; -.
DR PaxDb; Q6AYT5; -.
DR PRIDE; Q6AYT5; -.
DR Ensembl; ENSRNOT00000026367; ENSRNOP00000026367; ENSRNOG00000019489.
DR GeneID; 292267; -.
DR KEGG; rno:292267; -.
DR CTD; 79624; -.
DR RGD; 1305235; Armt1.
DR eggNOG; KOG3870; Eukaryota.
DR GeneTree; ENSGT00530000064023; -.
DR HOGENOM; CLU_030117_0_0_1; -.
DR InParanoid; Q6AYT5; -.
DR OMA; GFRPTNI; -.
DR OrthoDB; 856818at2759; -.
DR PhylomeDB; Q6AYT5; -.
DR TreeFam; TF314853; -.
DR PRO; PR:Q6AYT5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019489; Expressed in testis and 19 other tissues.
DR ExpressionAtlas; Q6AYT5; baseline and differential.
DR Genevisible; Q6AYT5; RN.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0097023; F:fructose 6-phosphate aldolase activity; IEA:RHEA.
DR GO; GO:0103026; F:fructose-1-phosphatase activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0051998; F:protein carboxyl O-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:RHEA.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; ISS:UniProtKB.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; ISS:UniProtKB.
DR InterPro; IPR036075; ARMT-1-like_metal-bd_sf.
DR InterPro; IPR039763; ARMT1.
DR InterPro; IPR002791; ARMT1-like_metal-bd.
DR PANTHER; PTHR12260; PTHR12260; 1.
DR Pfam; PF01937; ARMT1-like_dom; 1.
DR SUPFAM; SSF111321; SSF111321; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; Hydrolase; Manganese; Metal-binding;
KW Methyltransferase; Nickel; Phosphoprotein; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT CHAIN 2..439
FT /note="Damage-control phosphatase ARMT1"
FT /id="PRO_0000230797"
FT MOTIF 399..402
FT /note="Subfamily III RTxK motif"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 251..252
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 256
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 289
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 289
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT BINDING 365..369
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT BINDING 402
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q04371"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
SQ SEQUENCE 439 AA; 50184 MW; 629FB0A67E2F6E41 CRC64;
MAESPAFLSA QDVGSFAYLT IKDRTPQILT KVIDTLHRHK SEFFEKHGEE GVEAEKKAIS
LLSKLRNELQ TDKPIIPLVD KCVDTDIWNQ YLEYQRSLLN EGDGEPRWFF SPWLFVECYM
YRRIHEAIMQ SPPIHDFDVF KESKDENFFE SQDSINALCT HLLQLKPITD LGEKQIQDEF
FKLLQISLWG NKCDLSLSGG ESSSQKADII NSLKDLKPFI LVNETESLWA LLSKLKKTAE
PPAVRVDIVL DNSGFELVTD LVFADFLLSS ELATEIHFHG KIIPWFVSDV TVRDFEWIVE
HMKGSHLESM SACGAAWEAY VGMKKWVYHD HAFWTLPHPF CAMPQVAPDL YAELQKAGVV
LFKGDLNYRK LMGDRKWKFT VPFHQALSGF HPAPLCSIRT LKCELQVGLQ PGQAEHLTAS
DPHWLTTGKY GIFQFDGPL
