ARMT1_MOUSE
ID ARMT1_MOUSE Reviewed; 439 AA.
AC A6H630; Q499H1; Q99M05; Q9D9L4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A6H630-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6H630-2; Sequence=VSP_036138, VSP_036139;
CC Name=3;
CC IsoId=A6H630-3; Sequence=VSP_036133, VSP_036135, VSP_036136;
CC Name=4;
CC IsoId=A6H630-4; Sequence=VSP_036134, VSP_036137;
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; AK006776; BAB24735.1; -; mRNA.
DR EMBL; AC133902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466562; EDL03585.1; -; Genomic_DNA.
DR EMBL; CH466562; EDL03588.1; -; Genomic_DNA.
DR EMBL; BC002139; AAH02139.1; -; mRNA.
DR EMBL; BC099894; AAH99894.1; -; mRNA.
DR EMBL; BC138908; AAI38909.1; -; mRNA.
DR EMBL; BC145732; AAI45733.1; -; mRNA.
DR CCDS; CCDS56676.1; -. [A6H630-1]
DR RefSeq; NP_077223.2; NM_024261.2. [A6H630-1]
DR AlphaFoldDB; A6H630; -.
DR SMR; A6H630; -.
DR STRING; 10090.ENSMUSP00000093581; -.
DR iPTMnet; A6H630; -.
DR PhosphoSitePlus; A6H630; -.
DR EPD; A6H630; -.
DR MaxQB; A6H630; -.
DR PaxDb; A6H630; -.
DR PeptideAtlas; A6H630; -.
DR PRIDE; A6H630; -.
DR ProteomicsDB; 283166; -. [A6H630-1]
DR ProteomicsDB; 283167; -. [A6H630-2]
DR ProteomicsDB; 283168; -. [A6H630-3]
DR ProteomicsDB; 283169; -. [A6H630-4]
DR Antibodypedia; 1089; 160 antibodies from 24 providers.
DR DNASU; 73419; -.
DR Ensembl; ENSMUST00000095893; ENSMUSP00000093581; ENSMUSG00000061759. [A6H630-1]
DR Ensembl; ENSMUST00000117489; ENSMUSP00000114025; ENSMUSG00000061759. [A6H630-4]
DR Ensembl; ENSMUST00000118544; ENSMUSP00000114073; ENSMUSG00000061759. [A6H630-2]
DR GeneID; 73419; -.
DR KEGG; mmu:73419; -.
DR UCSC; uc007egy.1; mouse. [A6H630-1]
DR UCSC; uc007egz.1; mouse. [A6H630-2]
DR UCSC; uc007ehb.1; mouse. [A6H630-4]
DR CTD; 79624; -.
DR MGI; MGI:1920669; Armt1.
DR VEuPathDB; HostDB:ENSMUSG00000061759; -.
DR eggNOG; KOG3870; Eukaryota.
DR GeneTree; ENSGT00530000064023; -.
DR HOGENOM; CLU_030117_0_0_1; -.
DR InParanoid; A6H630; -.
DR OMA; GFRPTNI; -.
DR OrthoDB; 856818at2759; -.
DR PhylomeDB; A6H630; -.
DR TreeFam; TF314853; -.
DR BioGRID-ORCS; 73419; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Armt1; mouse.
DR PRO; PR:A6H630; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; A6H630; protein.
DR Bgee; ENSMUSG00000061759; Expressed in spermatocyte and 245 other tissues.
DR ExpressionAtlas; A6H630; baseline and differential.
DR Genevisible; A6H630; MM.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
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; Alternative splicing; DNA damage; Hydrolase; Manganese;
KW Metal-binding; Methyltransferase; Nickel; Phosphoprotein;
KW Reference proteome; 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_0000358925"
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:0000250|UniProtKB:Q6AYT5"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H993"
FT VAR_SEQ 1..14
FT /note="MAESPAFLSAKDEG -> MLW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036133"
FT VAR_SEQ 131..136
FT /note="SPPIHD -> RQVYSQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036134"
FT VAR_SEQ 131..132
FT /note="SP -> RF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036135"
FT VAR_SEQ 133..439
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036136"
FT VAR_SEQ 137..439
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036137"
FT VAR_SEQ 186..208
FT /note="ISLWGNKCDLSLSGGESSSQKAN -> VYKEYSTQDPMQPRRVMQTVTLQ
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036138"
FT VAR_SEQ 209..439
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_036139"
SQ SEQUENCE 439 AA; 50549 MW; 86C98D716BD9996B CRC64;
MAESPAFLSA KDEGSFAYLT IKDRTPQILT KVIDTLHRHK SEFFEKHGEE GIEAEKKAIS
LLSKLRNELQ TDKPITPLVD KCVDTHIWNQ YLEYQRSLLN EGDGEPRWFF SPWLFVECYM
YRRIHEAIMQ SPPIHDFDVF KESKEENFFE SQGSIDALCS HLLQLKPVKG LREEQIQDEF
FKLLQISLWG NKCDLSLSGG ESSSQKANII NCLQDLKPFI LINDTESLWA LLSKLKKTVE
TPVVRVDIVL DNSGFELITD LVLADFLFSS ELATEIHFHG KSIPWFVSDV TEHDFNWIVE
HMKSSNLESM STCGACWEAY ARMGRWAYHD HAFWTLPHPY CVMPQVAPDL YAELQKAHLI
LFKGDLNYRK LMGDRKWKFT FPFHQALSGF HPAPLCSIRT LKCELQVGLQ PGQAEQLTAS
DPHWLTTGRY GILQFDGPL
