ID   INO1_MOUSE              Reviewed;         557 AA.
AC   Q9JHU9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=Inositol-3-phosphate synthase 1;
DE            Short=IPS 1;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol 1-phosphate synthase;
DE            Short=MI-1-P synthase;
DE            Short=MIP synthase;
GN   Name=Isyna1; Synonyms=Ino1;
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 [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17121280; DOI=10.1007/0-387-27600-9_12;
RA   Parthasarathy L.K., Seelan R.S., Tobias C., Casanova M.F.,
RA   Parthasarathy R.N.;
RT   "Mammalian inositol 3-phosphate synthase: its role in the biosynthesis of
RT   brain inositol and its clinical use as a psychoactive agent.";
RL   Subcell. Biochem. 39:293-314(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Liver;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=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   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14613899; DOI=10.1095/biolreprod.103.022731;
RA   Chauvin T.R., Griswold M.D.;
RT   "Characterization of the expression and regulation of genes necessary for
RT   myo-inositol biosynthesis and transport in the seminiferous epithelium.";
RL   Biol. Reprod. 70:744-751(2004).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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: Key enzyme in myo-inositol biosynthesis pathway that
CC       catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-
CC       phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC       synthesis of all inositol-containing compounds (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate;
CC         Xref=Rhea:RHEA:10716, ChEBI:CHEBI:58401, ChEBI:CHEBI:61548;
CC         EC=5.5.1.4;
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: In testis, it is expressed in Sertoli cells. Highly
CC       expressed in 2 types of germ cells, pachytene spermatocytes and round
CC       spermatids. {ECO:0000269|PubMed:14613899}.
CC   -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AF288525; AAF90201.1; -; mRNA.
DR   EMBL; AK005029; BAB23756.1; -; mRNA.
DR   EMBL; AK079323; BAC37607.1; -; mRNA.
DR   EMBL; BC003458; AAH03458.1; -; mRNA.
DR   CCDS; CCDS22373.1; -.
DR   RefSeq; NP_076116.1; NM_023627.1.
DR   AlphaFoldDB; Q9JHU9; -.
DR   SMR; Q9JHU9; -.
DR   BioGRID; 214923; 6.
DR   IntAct; Q9JHU9; 4.
DR   MINT; Q9JHU9; -.
DR   STRING; 10090.ENSMUSP00000019283; -.
DR   iPTMnet; Q9JHU9; -.
DR   PhosphoSitePlus; Q9JHU9; -.
DR   SwissPalm; Q9JHU9; -.
DR   REPRODUCTION-2DPAGE; IPI00119886; -.
DR   REPRODUCTION-2DPAGE; Q9JHU9; -.
DR   EPD; Q9JHU9; -.
DR   jPOST; Q9JHU9; -.
DR   MaxQB; Q9JHU9; -.
DR   PaxDb; Q9JHU9; -.
DR   PeptideAtlas; Q9JHU9; -.
DR   PRIDE; Q9JHU9; -.
DR   ProteomicsDB; 267142; -.
DR   Antibodypedia; 28044; 94 antibodies from 23 providers.
DR   DNASU; 71780; -.
DR   Ensembl; ENSMUST00000019283; ENSMUSP00000019283; ENSMUSG00000019139.
DR   Ensembl; ENSMUST00000210005; ENSMUSP00000148077; ENSMUSG00000019139.
DR   GeneID; 71780; -.
DR   KEGG; mmu:71780; -.
DR   UCSC; uc009mav.1; mouse.
DR   CTD; 51477; -.
DR   MGI; MGI:1919030; Isyna1.
DR   VEuPathDB; HostDB:ENSMUSG00000019139; -.
DR   eggNOG; KOG0693; Eukaryota.
DR   GeneTree; ENSGT00390000018395; -.
DR   HOGENOM; CLU_021486_2_1_1; -.
DR   InParanoid; Q9JHU9; -.
DR   OMA; EHDLFIQ; -.
DR   OrthoDB; 451916at2759; -.
DR   PhylomeDB; Q9JHU9; -.
DR   TreeFam; TF300382; -.
DR   Reactome; R-MMU-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR   UniPathway; UPA00823; UER00787.
DR   BioGRID-ORCS; 71780; 1 hit in 75 CRISPR screens.
DR   ChiTaRS; Isyna1; mouse.
DR   PRO; PR:Q9JHU9; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9JHU9; protein.
DR   Bgee; ENSMUSG00000019139; Expressed in morula and 235 other tissues.
DR   ExpressionAtlas; Q9JHU9; baseline and differential.
DR   Genevisible; Q9JHU9; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; ISO:MGI.
DR   GO; GO:0006021; P:inositol biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR   InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11510; PTHR11510; 1.
DR   Pfam; PF01658; Inos-1-P_synth; 1.
DR   Pfam; PF07994; NAD_binding_5; 1.
DR   PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Inositol biosynthesis; Isomerase; Lipid biosynthesis;
KW   Lipid metabolism; NAD; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome.
FT   CHAIN           1..557
FT                   /note="Inositol-3-phosphate synthase 1"
FT                   /id="PRO_0000324630"
FT   REGION          512..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..557
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   557 AA;  60932 MW;  91166BD2A2C53ADA CRC64;
     MEPAAEILVD SPDVVYSPET IEARYEYRTT RVSREGGVLR VQPRATRFTF RTARQVPRLG
     VMLVGWGGNN GSTLTAAVLA NRLRLTWPTR TGRKEANYYG SLTQAGTVNL GLDENGREVF
     VPFSALLPMV APNDLVFDGW DISSLNLAEA MRRAQVLDCG LQEQLWPHME SLRPRPSVYI
     PEFIAANQTA RADNLIPGTR AQQLEQIRKD IRDFRSSAGL DKVIVLWTAN TERFCEVVPG
     RNDTAENLLH TIQLGLEVSP STLFAVASIL EDCAFLNGSP QNTLVPGALE LASQRHVFVG
     GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG QNLSAPLQFR SKEVTKSSVV
     DDMVHSNHVL YAPGERPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
     LLAAPIMLDL VLLTELCQRV SFCTDSDPEP QGFHTVLSLL SFLFKAPLVP PGSPVVNALF
     RQRSCIENIF RACVGLPPQN HMLLEHKMER PGPGIKPGEV VATSPLPCKK EPTPATNGCT
     GDANGHPQAP TPKLSTA