INO1_DROME
ID INO1_DROME Reviewed; 565 AA.
AC O97477; Q8IGW1; Q8MR42;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Inositol-3-phosphate synthase;
DE Short=MIP synthase;
DE EC=5.5.1.4;
DE AltName: Full=Myo-inositol 1-phosphate synthase;
DE Short=IPS;
DE Short=MI-1-P synthase;
GN Name=Inos; ORFNames=CG11143;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Oregon-R;
RX PubMed=11121586; DOI=10.1016/s0167-4781(00)00085-3;
RA Park D., Jeong S., Lee S., Park S., Kim J.-I., Yim J.;
RT "Molecular characterization of Drosophila melanogaster myo-inositol-1-
RT phosphate synthase.";
RL Biochim. Biophys. Acta 1494:277-281(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569},
RC Head {ECO:0000269|PubMed:12537569}, and
RC Ovary {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
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; Evidence={ECO:0000269|PubMed:11121586};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000250|UniProtKB:P11986};
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: Higher expression in adult heads than bodies.
CC {ECO:0000269|PubMed:11121586}.
CC -!- SIMILARITY: Belongs to the myo-inositol 1-phosphate synthase family.
CC {ECO:0000305}.
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DR EMBL; AF071103; AAD02819.1; -; mRNA.
DR EMBL; AF071104; AAD13140.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF59252.1; -; Genomic_DNA.
DR EMBL; AY122137; AAM52649.1; -; mRNA.
DR EMBL; BT001560; AAN71315.1; ALT_SEQ; mRNA.
DR EMBL; BT001772; AAN71527.1; -; mRNA.
DR RefSeq; NP_477405.1; NM_058057.6.
DR AlphaFoldDB; O97477; -.
DR SMR; O97477; -.
DR BioGRID; 61549; 69.
DR STRING; 7227.FBpp0088368; -.
DR iPTMnet; O97477; -.
DR PaxDb; O97477; -.
DR PRIDE; O97477; -.
DR DNASU; 35671; -.
DR EnsemblMetazoa; FBtr0089329; FBpp0088368; FBgn0025885.
DR GeneID; 35671; -.
DR KEGG; dme:Dmel_CG11143; -.
DR UCSC; CG11143-RA; d. melanogaster.
DR CTD; 35671; -.
DR FlyBase; FBgn0025885; Inos.
DR VEuPathDB; VectorBase:FBgn0025885; -.
DR eggNOG; KOG0693; Eukaryota.
DR GeneTree; ENSGT00390000018395; -.
DR HOGENOM; CLU_021486_2_0_1; -.
DR InParanoid; O97477; -.
DR OMA; EHDLFIQ; -.
DR OrthoDB; 451916at2759; -.
DR PhylomeDB; O97477; -.
DR Reactome; R-DME-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR UniPathway; UPA00823; UER00787.
DR BioGRID-ORCS; 35671; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35671; -.
DR PRO; PR:O97477; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0025885; Expressed in seminal fluid secreting gland and 25 other tissues.
DR Genevisible; O97477; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0004512; F:inositol-3-phosphate synthase activity; IDA:FlyBase.
DR GO; GO:0006021; P:inositol biosynthetic process; ISS:FlyBase.
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 Phosphoprotein; Reference proteome.
FT CHAIN 1..565
FT /note="Inositol-3-phosphate synthase"
FT /id="PRO_0000195182"
FT REGION 546..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT CONFLICT 324
FT /note="V -> L (in Ref. 4; AAN71315)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 62249 MW; 6CF53D0D27BE186F CRC64;
MKPTNNSTLE VISPKVQVDD EFITTDYDYQ TSHVKRTADG QLQVHPQTTS LKIRTGRHVP
KLGVMLVGWG GNNGSTLTAA LEANRRQLKW RKRTGVQEAN WYGSITQAST VFIGSDEDGG
DVYVPMKELL PMVEPDNIIV DGWDISGLHL GDAMRRAEVL DVALQDQIYD QLAQLRPRPS
IYDPDFIAAN QSDRADNVIR GTRLEQYEQI RKDIRDFRER SGVDSVIVLW TANTERFADV
QPGLNTTSQE LIASLEANHS EVSPSTIFAM ASIAEGCTYI NGSPQNTFVP GLIQLAEEKN
VFIAGDDFKS GQTKIKSVLV DFLVGAGIKP VSIASYNHLG NNDGKNLSAP QQFRSKEISK
SNVVDDMVAS NRLLYGPDEH PDHVVVIKYV PYVGDSKRAM DEYTSEIMMG GHNTLVIHNT
CEDSLLATPL ILDLVILGEL STRIQLRNAE KESAPWVPFK PVLSLLSYLC KAPLVPQGSQ
VVNSLFRQRA AIENILRGCI GLPPISHMTL EQRFDFSTIT NEPPLKRVKI LGQPCSVESV
TNGKKLHANG HSNGSAKLAT NGNGH
