Search by BoMiProt ID - Bomi5021


Primary Information

BoMiProt ID Bomi5021
Protein Name Damage-control phosphatase ARMT1/Acidic residue methyltransferase 1/Protein-glutamate O-methyltransferase/Sugar phosphate phosphatase ARMT1
Organism Bos taurus
Uniprot IDA3KMX8
Milk FractionWhey
Ref Sequence ID NP_001076968.1
Aminoacid Length 441
Molecular Weight 50964
FASTA Sequence Download
Gene Name ARMT1
Gene ID 540698
Protein Existence Status reviewed

Secondary Information

Protein Function shows phosphatase activity against several substrates andshown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues.
Biochemical Properties The biochemical activities of the human protein are conserved with those of a previously characterized budding yeast homolog, where an in vitro phosphatase activity is supported by divalent cations that include Co2+, Ni2+, Mn2+ or Mg2+.
PTMs Acetylation and phosphorylation
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|A3KMX8|ARMT1_BOVIN Damage-control phosphatase ARMT1 OS=Bos taurus OX=9913 GN=ARMT1 PE=2 SV=1 MAGPPASLSARDVGSFAYLSVKDRSPQILTKAIDTLHRHKSEFFEKHGEKGLEAEKKAIS LLSKLRNELQTDKPIVPLVEKFVDTDIWNQYLEYQQSLLNES*102DGKPRWFLSPWLFVECYM YRRIHEAIIQSPPIDDFDIFKEFKDQNFFESQESIIALCTHLQELRKTIEDLDENQLKNE FFKVLQISLWGNKCDLSLSGGEHISQKTNIMNSLEDLKPFILVNDMDRLWSLLSNCKKTR EKESVTRVDIVLDNSGFELITDLVLADFLLSSKLATKIHFYGKTIPWFVSDTTLHDFNWI IKQLKHSNNKWVSQCGVDWEDHVKTGRWVYLDHIFWTLPHEFSAMSQVAPDLHAALQKAH LIFFKGDLNYRKLTGDRRWEFTVPFHEALSGFHPAPLCSIRTLKAEVQVGLQPGQGEQLT ASEPNWLTAGKYGVFQFDGPL
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Additional Comments The sequence around the two cysteines involved in the redox-active disulphide bond is conserved and can be used as a signature pattern.
Bibliography 1.Dennis TN, Kenjić N, Kang AS, Lowenson JD, Kirkwood JS, Clarke SG, Perry JJP. Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase. J Struct Biol. 2020 Oct 1;212(1):107576. doi: 10.1016/j.jsb.2020.107576. Epub 2020 Jul 15. PMID: 32682077.