MESH1_MOUSE
ID MESH1_MOUSE Reviewed; 179 AA.
AC Q9D114;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1;
DE EC=3.1.7.2;
DE AltName: Full=HD domain-containing protein 3;
DE AltName: Full=Metazoan SpoT homolog 1;
DE Short=MESH1;
DE AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE Short=(ppGpp)ase;
GN Name=Hddc3; Synonyms=Mesh1;
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].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 MRNA].
RC STRAIN=Czech II; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Pancreas, Spleen,
RC 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: ppGpp hydrolyzing enzyme involved in starvation response.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the MESH1 family. {ECO:0000305}.
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DR EMBL; AK004078; BAB23158.1; -; mRNA.
DR EMBL; BC038310; AAH38310.1; -; mRNA.
DR CCDS; CCDS21396.1; -.
DR RefSeq; NP_081088.1; NM_026812.2.
DR AlphaFoldDB; Q9D114; -.
DR SMR; Q9D114; -.
DR BioGRID; 212997; 1.
DR STRING; 10090.ENSMUSP00000032747; -.
DR iPTMnet; Q9D114; -.
DR PhosphoSitePlus; Q9D114; -.
DR MaxQB; Q9D114; -.
DR PaxDb; Q9D114; -.
DR PeptideAtlas; Q9D114; -.
DR PRIDE; Q9D114; -.
DR ProteomicsDB; 295929; -.
DR Antibodypedia; 43848; 122 antibodies from 21 providers.
DR DNASU; 68695; -.
DR Ensembl; ENSMUST00000032747; ENSMUSP00000032747; ENSMUSG00000030532.
DR GeneID; 68695; -.
DR KEGG; mmu:68695; -.
DR UCSC; uc009ian.1; mouse.
DR CTD; 374659; -.
DR MGI; MGI:1915945; Hddc3.
DR VEuPathDB; HostDB:ENSMUSG00000030532; -.
DR eggNOG; KOG1157; Eukaryota.
DR GeneTree; ENSGT00390000011608; -.
DR HOGENOM; CLU_084517_1_0_1; -.
DR InParanoid; Q9D114; -.
DR OMA; FVWASEV; -.
DR OrthoDB; 1372331at2759; -.
DR PhylomeDB; Q9D114; -.
DR TreeFam; TF313524; -.
DR BioGRID-ORCS; 68695; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q9D114; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D114; protein.
DR Bgee; ENSMUSG00000030532; Expressed in floor plate of midbrain and 218 other tissues.
DR ExpressionAtlas; Q9D114; baseline and differential.
DR Genevisible; Q9D114; MM.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR SMART; SM00471; HDc; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Manganese; Metal-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8N4P3"
FT CHAIN 2..179
FT /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT pyrophosphohydrolase MESH1"
FT /id="PRO_0000263111"
FT DOMAIN 32..127
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT ACT_SITE 65
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 66
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4P3"
FT MOD_RES 25
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4P3"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4P3"
FT MOD_RES 123
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4P3"
SQ SEQUENCE 179 AA; 20262 MW; D52FF1DA540A6ED3 CRC64;
MGSEAAQLLE AADFAAHKHR QQRRKDPEGT PYINHPIGVA RILTHEAGIT DIVVLQAALL
HDTVEDTDTT LDEVELHFGA QVRRLVEEVT DDKTLPKLER KRQQVEQAPH SSPGAKLVKL
ADKLYNLRDL NRCTPTGWSE HRVQEYFEWA AQVVKGLQGT NQQLEEALKQ LFEERGLTL
