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Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (dNTPase) (EC 3.1.5.-) (Interferon-gamma-inducible protein Mg11) (SAM domain and HD domain-containing protein 1)

 SAMH1_MOUSE             Reviewed;         627 AA.
Q60710; Q3U5X2; Q543A4; Q91VK8;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
13-AUG-2002, sequence version 2.
27-SEP-2017, entry version 145.
RecName: Full=Deoxynucleoside triphosphate triphosphohydrolase SAMHD1;
Short=dNTPase;
EC=3.1.5.-;
AltName: Full=Interferon-gamma-inducible protein Mg11;
AltName: Full=SAM domain and HD domain-containing protein 1;
Name=Samhd1; Synonyms=Mg11;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Macrophage;
PubMed=7884320;
Lafuse W.P., Brown D., Castle L., Zwilling B.S.;
"Cloning and characterization of a novel cDNA that is IFN-gamma-
induced in mouse peritoneal macrophages and encodes a putative GTP-
binding protein.";
J. Leukoc. Biol. 57:477-483(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Ovary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-21 AND THR-603,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-603, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[7]
INDUCTION.
PubMed=19525956; DOI=10.1038/ng.373;
Rice G.I., Bond J., Asipu A., Brunette R.L., Manfield I.W., Carr I.M.,
Fuller J.C., Jackson R.M., Lamb T., Briggs T.A., Ali M., Gornall H.,
Couthard L.R., Aeby A., Attard-Montalto S.P., Bertini E., Bodemer C.,
Brockmann K., Brueton L.A., Corry P.C., Desguerre I., Fazzi E.,
Cazorla A.G., Gener B., Hamel B.C.J., Heiberg A., Hunter M.,
van der Knaap M.S., Kumar R., Lagae L., Landrieu P.G., Lourenco C.M.,
Marom D., McDermott M.F., van der Merwe W., Orcesi S.,
Prendiville J.S., Rasmussen M., Shalev S.A., Soler D.M., Shinawi M.,
Spiegel R., Tan T.Y., Vanderver A., Wakeling E.L., Wassmer E.,
Whittaker E., Lebon P., Stetson D.B., Bonthron D.T., Crow Y.J.;
"Mutations involved in Aicardi-Goutieres syndrome implicate SAMHD1 as
regulator of the innate immune response.";
Nat. Genet. 41:829-832(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-21; SER-24;
THR-25 AND THR-603, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Host restriction nuclease involved in defense response
to virus. Has dNTPase activity and reduces cellular dNTP levels to
levels too low for retroviral reverse transcription to occur.
Blocks early-stage virus replication in dendritic and other
myeloid cells. Likewise, suppresses LINE-1 retrotransposon
activity. May play a role in mediating proinflammatory responses
to TNF-alpha signaling. Has ribonuclease activity, acting on
single-stranded RNA. {ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- CATALYTIC ACTIVITY: dNTP + H(2)O = Deoxynucleoside + triphosphate.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9Y3Z3};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9Y3Z3};
-!- ENZYME REGULATION: Allosterically stimulated by dGTP which binds
in a cleft at the interface of the homodimer and promotes the
formation of highly active homotetramers. Each allosteric site
binds two molecules of dGTP (dGTP1 and dGTP 2) between adjoining
subunits. Not activated by dATP, dCTP and dTTP (By similarity).
{ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- SUBUNIT: Homodimer. Homotetramer; in dGTP-bound form (By
similarity). {ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- INDUCTION: By interferon alpha, beta and gamma (IFN-alpha, IFN-
beta and IFN-gamma). {ECO:0000269|PubMed:19525956}.
-!- PTM: Ubiquitinated and targeted for proteasomal degradation by a
DCX (DDB1-CUL4-X-box) E3 ubiquitin ligase with the help of the
viral accessory protein Vpx. {ECO:0000250|UniProtKB:Q9Y3Z3}.
-!- SIMILARITY: Belongs to the SAMHD1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA66219.1; Type=Frameshift; Positions=576; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U15635; AAA66219.1; ALT_FRAME; mRNA.
EMBL; AK054490; BAC35801.1; -; mRNA.
EMBL; AK151335; BAE30313.1; -; mRNA.
EMBL; AK153390; BAE31954.1; -; mRNA.
EMBL; AL669828; CAM15970.1; -; Genomic_DNA.
EMBL; BC012721; AAH12721.1; -; mRNA.
EMBL; BC067198; AAH67198.1; -; mRNA.
PIR; I49127; I49127.
RefSeq; NP_001132992.1; NM_001139520.1.
RefSeq; NP_061339.3; NM_018851.3.
UniGene; Mm.248478; -.
UniGene; Mm.468781; -.
ProteinModelPortal; Q60710; -.
SMR; Q60710; -.
BioGrid; 207791; 11.
IntAct; Q60710; 3.
MINT; MINT-4133768; -.
STRING; 10090.ENSMUSP00000059717; -.
iPTMnet; Q60710; -.
PhosphoSitePlus; Q60710; -.
SwissPalm; Q60710; -.
EPD; Q60710; -.
MaxQB; Q60710; -.
PaxDb; Q60710; -.
PeptideAtlas; Q60710; -.
PRIDE; Q60710; -.
DNASU; 56045; -.
GeneID; 56045; -.
KEGG; mmu:56045; -.
CTD; 25939; -.
MGI; MGI:1927468; Samhd1.
eggNOG; KOG2681; Eukaryota.
eggNOG; COG1078; LUCA.
HOGENOM; HOG000264286; -.
HOVERGEN; HBG054208; -.
InParanoid; Q60710; -.
PhylomeDB; Q60710; -.
ChiTaRS; Samhd1; mouse.
PMAP-CutDB; Q60710; -.
PRO; PR:Q60710; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_SAMHD1; -.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032567; F:dGTP binding; ISS:UniProtKB.
GO; GO:0008832; F:dGTPase activity; ISS:UniProtKB.
GO; GO:0003676; F:nucleic acid binding; ISS:UniProtKB.
GO; GO:0004540; F:ribonuclease activity; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
GO; GO:0016793; F:triphosphoric monoester hydrolase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0046061; P:dATP catabolic process; ISS:UniProtKB.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0006203; P:dGTP catabolic process; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
GO; GO:0045088; P:regulation of innate immune response; ISS:UniProtKB.
CDD; cd00077; HDc; 1.
InterPro; IPR003607; HD/PDEase_dom.
InterPro; IPR006674; HD_domain.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
Pfam; PF01966; HD; 1.
Pfam; PF07647; SAM_2; 1.
SMART; SM00471; HDc; 1.
SMART; SM00454; SAM; 1.
SUPFAM; SSF47769; SSF47769; 1.
PROSITE; PS51831; HD; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Allosteric enzyme; Antiviral defense; Complete proteome;
Hydrolase; Immunity; Innate immunity; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Zinc.
CHAIN 1 627 Deoxynucleoside triphosphate
triphosphohydrolase SAMHD1.
/FTId=PRO_0000153733.
DOMAIN 46 111 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 165 317 HD. {ECO:0000255|PROSITE-
ProRule:PRU01175}.
NP_BIND 138 146 dGTP. {ECO:0000250}.
NP_BIND 138 146 dGTP 1. {ECO:0000250}.
NP_BIND 364 366 dGTP 2. {ECO:0000250}.
REGION 310 316 Substrate binding. {ECO:0000250}.
REGION 382 387 Substrate binding. {ECO:0000250}.
ACT_SITE 234 234 {ECO:0000250}.
METAL 168 168 Zinc; via tele nitrogen. {ECO:0000250}.
METAL 207 207 Zinc; via tele nitrogen. {ECO:0000250}.
METAL 208 208 Zinc. {ECO:0000250}.
METAL 312 312 Zinc. {ECO:0000250}.
BINDING 117 117 dGTP 1. {ECO:0000250}.
BINDING 120 120 dGTP 2; via amide nitrogen; shared with
neighboring subunit. {ECO:0000250}.
BINDING 150 150 Substrate. {ECO:0000250}.
BINDING 165 165 Substrate. {ECO:0000250}.
BINDING 211 211 Substrate. {ECO:0000250}.
BINDING 316 316 Substrate. {ECO:0000250}.
BINDING 320 320 Substrate. {ECO:0000250}.
BINDING 334 334 dGTP 2. {ECO:0000250}.
BINDING 370 370 dGTP 2. {ECO:0000250}.
BINDING 378 378 Substrate. {ECO:0000250}.
BINDING 388 388 dGTP 2; shared with neighboring subunit.
{ECO:0000250}.
BINDING 389 389 dGTP 2; shared with neighboring subunit.
{ECO:0000250}.
BINDING 463 463 dGTP 1; shared with neighboring subunit.
{ECO:0000250}.
BINDING 467 467 dGTP 1; shared with neighboring subunit.
{ECO:0000250}.
BINDING 534 534 dGTP 2. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 21 21 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 94 94 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y3Z3}.
MOD_RES 603 603 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
CROSSLNK 478 478 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y3Z3}.
CONFLICT 340 340 R -> L (in Ref. 2; BAE31954/BAE30313).
{ECO:0000305}.
SEQUENCE 627 AA; 72650 MW; C68BB653C3F4B17C CRC64;
MQSAPLEQPA KRPRCDGSPR TPPSTPPATA NLSADDDFQN TDLRTWEPED VCSFLENRGF
REKKVLDIFR DNKIAGSFLP FLDEDRLEDL GVSSLEERKK MIECIQQLSQ SRIDLMKVFN
DPIHGHIEFH PLLIRIIDTP QFQRLRYIKQ LGGGYYVFPG ASHNRFEHSL GVGYLAGCLV
RALAEKQPEL QISERDILCV QIAGLCHDLG HGPFSHMFDG RFIPRARPEK KWKHEQGSIE
MFEHLVNSNE LKLVMKNYGL VPEEDITFIK EQIMGPPITP VKDSLWPYKG RPATKSFLYE
IVSNKRNGID VDKWDYFARD CHHLGIQNNF DYKRFIKFAR ICEVEYKVKE DKTYIRKVKH
ICSREKEVGN LYDMFHTRNC LHRRAYQHKI SNLIDIMITD AFLKADPYVE ITGTAGKKFR
ISTAIDDMEA FTKLTDNIFL EVLHSTDPQL SEAQSILRNI ECRNLYKYLG ETQPKREKIR
KEEYERLPQE VAKAKPEKAP DVELKAEDFI VDVINVDYGM EDKNPIDRVH FYCKSNSKQA
VRINKEQVSQ LLPEKFAEQL IRVYCKKKDG KSLDAAGKHF VQWCALRDFT KPQDGDIIAP
LITPLKWNNK TSSCLQEVSK VKTCLKF


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