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   27-MAR-2024, entry version 141.
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,
RC   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: 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 2.
DR   STRING; 10090.ENSMUSP00000032747; -.
DR   iPTMnet; Q9D114; -.
DR   PhosphoSitePlus; Q9D114; -.
DR   MaxQB; Q9D114; -.
DR   PaxDb; 10090-ENSMUSP00000032747; -.
DR   PeptideAtlas; Q9D114; -.
DR   ProteomicsDB; 295929; -.
DR   Pumba; Q9D114; -.
DR   Antibodypedia; 43848; 125 antibodies from 21 providers.
DR   DNASU; 68695; -.
DR   Ensembl; ENSMUST00000032747.7; ENSMUSP00000032747.6; ENSMUSG00000030532.7.
DR   GeneID; 68695; -.
DR   KEGG; mmu:68695; -.
DR   UCSC; uc009ian.1; mouse.
DR   AGR; MGI:1915945; -.
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; PPWRERK; -.
DR   OrthoDB; 2783605at2759; -.
DR   PhylomeDB; Q9D114; -.
DR   TreeFam; TF313524; -.
DR   BioGRID-ORCS; 68695; 3 hits in 76 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 221 other cell types or tissues.
DR   ExpressionAtlas; Q9D114; baseline and differential.
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   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   PANTHER; PTHR46246; GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE MESH1; 1.
DR   PANTHER; PTHR46246:SF1; GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE MESH1; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
DR   Genevisible; Q9D114; MM.
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
//