IDI2_MOUSE
ID IDI2_MOUSE Reviewed; 227 AA.
AC Q8BFZ6; Q4FZF0;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Isopentenyl-diphosphate delta-isomerase 2;
DE EC=5.3.3.2 {ECO:0000250|UniProtKB:Q9BXS1};
DE AltName: Full=Isopentenyl pyrophosphate isomerase 2;
DE Short=IPP isomerase 2;
DE Short=IPPI2;
GN Name=Idi2; Synonyms=Gm9745;
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 STRAIN=C57BL/6J;
RX PubMed=14629038; DOI=10.1007/s00239-003-2476-8;
RA Breitling R., Laubner D., Clizbe D., Adamski J., Krisans S.K.;
RT "Isopentenyl-diphosphate isomerases in human and mouse: evolutionary
RT analysis of a mammalian gene duplication.";
RL J. Mol. Evol. 57:282-291(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head, and Head;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic
CC substrate isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC dimethylallyl diphosphate (DMAPP). {ECO:0000250|UniProtKB:Q9BXS1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=isopentenyl diphosphate = dimethylallyl diphosphate;
CC Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769;
CC EC=5.3.3.2; Evidence={ECO:0000250|UniProtKB:Q9BXS1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BXS1};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000250|UniProtKB:Q9BXS1}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q9BXS1}.
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
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DR EMBL; AY263178; AAP21674.1; -; mRNA.
DR EMBL; AK029364; BAC26418.1; -; mRNA.
DR EMBL; AK081319; BAC38194.1; -; mRNA.
DR EMBL; AC124732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC099586; AAH99586.1; -; mRNA.
DR EMBL; BC125310; AAI25311.1; -; mRNA.
DR EMBL; BC138100; AAI38101.1; -; mRNA.
DR CCDS; CCDS26235.1; -.
DR RefSeq; NP_796171.1; NM_177197.4.
DR AlphaFoldDB; Q8BFZ6; -.
DR SMR; Q8BFZ6; -.
DR STRING; 10090.ENSMUSP00000036621; -.
DR PaxDb; Q8BFZ6; -.
DR PRIDE; Q8BFZ6; -.
DR ProteomicsDB; 267253; -.
DR DNASU; 320581; -.
DR Ensembl; ENSMUST00000021573; ENSMUSP00000021573; ENSMUSG00000021148.
DR Ensembl; ENSMUST00000038598; ENSMUSP00000036621; ENSMUSG00000033520.
DR Ensembl; ENSMUST00000187196; ENSMUSP00000139705; ENSMUSG00000021148.
DR GeneID; 320581; -.
DR KEGG; mmu:320581; -.
DR UCSC; uc007pko.1; mouse.
DR CTD; 91734; -.
DR MGI; MGI:3704398; Gm9745.
DR MGI; MGI:2444315; Idi2.
DR VEuPathDB; HostDB:ENSMUSG00000021148; -.
DR VEuPathDB; HostDB:ENSMUSG00000033520; -.
DR eggNOG; KOG0142; Eukaryota.
DR GeneTree; ENSGT00390000008527; -.
DR HOGENOM; CLU_060552_0_1_1; -.
DR InParanoid; Q8BFZ6; -.
DR OMA; RCSHPLY; -.
DR OrthoDB; 1281908at2759; -.
DR PhylomeDB; Q8BFZ6; -.
DR TreeFam; TF300129; -.
DR Reactome; R-MMU-191273; Cholesterol biosynthesis.
DR UniPathway; UPA00059; UER00104.
DR BioGRID-ORCS; 320581; 8 hits in 41 CRISPR screens.
DR PRO; PR:Q8BFZ6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BFZ6; protein.
DR Bgee; ENSMUSG00000021148; Expressed in morula and 4 other tissues.
DR Genevisible; Q8BFZ6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009240; P:isopentenyl diphosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0046490; P:isopentenyl diphosphate metabolic process; ISO:MGI.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISO:MGI.
DR GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; IDA:UniProtKB.
DR CDD; cd02885; IPP_Isomerase; 1.
DR InterPro; IPR011876; IsopentenylPP_isomerase_typ1.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PIRSF; PIRSF018427; Isopntndiph_ism; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR02150; IPP_isom_1; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 2: Evidence at transcript level;
KW Cholesterol biosynthesis; Cholesterol metabolism; Isomerase;
KW Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Metal-binding; Peroxisome; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..227
FT /note="Isopentenyl-diphosphate delta-isomerase 2"
FT /id="PRO_0000420867"
FT DOMAIN 49..199
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 225..227
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 86
FT /evidence="ECO:0000250"
FT ACT_SITE 148
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="M -> I (in Ref. 4; AAH99586)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="E -> G (in Ref. 4; AAH99586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 26665 MW; DACEA662BA4209A0 CRC64;
MFQASKTHLD ELQLKRLEEM CIVIDKQDQI IGADTKKNCH LMENINKGLL HRAFSVVLFN
MKNELLVQQR ADAKYTFPGH FTDSCSSHPL YVPEELEEKD ALGVRRAALR RLQAELGISQ
DQISIKDIIF MTRKYHKCQS DAIWGEHEIG YLLLVRKDLM LNPDTREVRR CCYMSQKDVQ
ELLDREARGE EKITPWFRSM VEDFLFSWWP HLEDVSSFVE PDKIYGL
