O97477 (INO1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inositol-3-phosphate synthase
Short name=MIP synthase
EC=5.5.1.4

Alternative name(s):
Myo-inositol 1-phosphate synthase
Short name=IPS
Short name=MI-1-P synthase

Gene names

Name:	Inos
ORF Names:	CG11143

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	565 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate. Ref.1
Cofactor	NAD By similarity. UniProtKB P11986
Pathway	Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 1/2.
Subcellular location	Cytoplasm By similarity UniProtKB P11986.
Tissue specificity	Higher expression in adult heads than bodies. Ref.1
Sequence similarities	Belongs to the myo-inositol 1-phosphate synthase family.

Ontologies

Keywords
Biological process	Inositol biosynthesis Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	inositol-3-phosphate synthase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 565	565	Inositol-3-phosphate synthase		PRO_0000195182
Amino acid modifications
	Modified residue	536	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	324	1	V → L in AAN71315. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O97477 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6CF53D0D27BE186F	FASTA	565	62,249
	10 20 30 40 50 60 MKPTNNSTLE VISPKVQVDD EFITTDYDYQ TSHVKRTADG QLQVHPQTTS LKIRTGRHVP 70 80 90 100 110 120 KLGVMLVGWG GNNGSTLTAA LEANRRQLKW RKRTGVQEAN WYGSITQAST VFIGSDEDGG 130 140 150 160 170 180 DVYVPMKELL PMVEPDNIIV DGWDISGLHL GDAMRRAEVL DVALQDQIYD QLAQLRPRPS 190 200 210 220 230 240 IYDPDFIAAN QSDRADNVIR GTRLEQYEQI RKDIRDFRER SGVDSVIVLW TANTERFADV 250 260 270 280 290 300 QPGLNTTSQE LIASLEANHS EVSPSTIFAM ASIAEGCTYI NGSPQNTFVP GLIQLAEEKN 310 320 330 340 350 360 VFIAGDDFKS GQTKIKSVLV DFLVGAGIKP VSIASYNHLG NNDGKNLSAP QQFRSKEISK 370 380 390 400 410 420 SNVVDDMVAS NRLLYGPDEH PDHVVVIKYV PYVGDSKRAM DEYTSEIMMG GHNTLVIHNT 430 440 450 460 470 480 CEDSLLATPL ILDLVILGEL STRIQLRNAE KESAPWVPFK PVLSLLSYLC KAPLVPQGSQ 490 500 510 520 530 540 VVNSLFRQRA AIENILRGCI GLPPISHMTL EQRFDFSTIT NEPPLKRVKI LGQPCSVESV 550 560 TNGKKLHANG HSNGSAKLAT NGNGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of Drosophila melanogaster myo-inositol-1-phosphate synthase." Park D., Jeong S., Lee S., Park S., Kim J.-I., Yim J. Biochim. Biophys. Acta 1494:277-281(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: Oregon-R.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo, Head and Ovary.
[5]	"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells." Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A. Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF071103 mRNA. Translation: AAD02819.1. AF071104 Genomic DNA. Translation: AAD13140.1. AE013599 Genomic DNA. Translation: AAF59252.1. AY122137 mRNA. Translation: AAM52649.1. BT001560 mRNA. Translation: AAN71315.1. Sequence problems. BT001772 mRNA. Translation: AAN71527.1.
RefSeq	NP_477405.1. NM_058057.6.
UniGene	Dm.3378.
3D structure databases
ProteinModelPortal	O97477.
SMR	O97477. Positions 7-514.
ModBase	Search...
Proteomic databases
PaxDb	O97477.
PRIDE	O97477.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0089329; FBpp0088368; FBgn0025885.
GeneID	35671.
KEGG	dme:Dmel_CG11143.
UCSC	CG11143-RA. d. melanogaster.
Organism-specific databases
CTD	35671.
FlyBase	FBgn0025885. Inos.
Phylogenomic databases
eggNOG	COG1260.
GeneTree	ENSGT00390000018395.
InParanoid	O97477.
KO	K01858.
OMA	NPVLYAP.
OrthoDB	EOG4R4XJ4.
PhylomeDB	O97477.
Enzyme and pathway databases
UniPathway	UPA00823; UER00787.
Gene expression databases
Bgee	O97477.
GermOnline	CG11143. Drosophila melanogaster.
Family and domain databases
Gene3D	3.40.50.720. 2 hits.
InterPro	IPR002587. Myo-inos-1-P_Synthase. IPR013021. Myo-inos-1-P_Synthase_GAPDH. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11510. PTHR11510. 1 hit.
Pfam	PF01658. Inos-1-P_synth. 1 hit. PF07994. NAD_binding_5. 1 hit. [Graphical view]
PIRSF	PIRSF015578. Myoinos-ppht_syn. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	35671.
NextBio	794650.

Entry information

Entry name

INO1_DROME

Accession

Primary (citable) accession number: O97477
Secondary accession number(s): Q8IGW1, Q8MR42

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 1, 1999
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project