IDI1_HUMAN
ID IDI1_HUMAN Reviewed; 227 AA.
AC Q13907; B4E155; Q32Q13; Q53GQ6; Q86U81; Q8WUX8; Q96IZ4; Q9BQ74;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Isopentenyl-diphosphate Delta-isomerase 1;
DE EC=5.3.3.2 {ECO:0000269|PubMed:8806705};
DE AltName: Full=Isopentenyl pyrophosphate isomerase 1;
DE Short=IPP isomerase 1;
DE Short=IPPI1;
GN Name=IDI1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8020941; DOI=10.1006/geno.1994.1139;
RA Xuan J.W., Kowalski J., Chambers A.F., Denhardt D.T.;
RT "A human promyelocyte mRNA transiently induced by TPA is homologous to
RT yeast IPP isomerase.";
RL Genomics 20:129-131(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Masuda K., Breitling R., Krisans S.K., Keller B., Moeller G., Adamski J.;
RT "Two genes for isopentenyl diphosphate isomerase in human.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RA Masuda K., Krisans S.K., Keller B., Moeller G., Adamski J.;
RT "Characterisation of a human gene for isopentenyl diphosphate dimethylally
RT diphosphate isomerase 1 (IDI1).";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Bone marrow, Skin, and Urinary bladder;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-227 (ISOFORM 2).
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=8806705; DOI=10.1006/abbi.1996.0312;
RA Hahn F.M., Xuan J.W., Chambers A.F., Poulter C.D.;
RT "Human isopentenyl diphosphate: dimethylallyl diphosphate isomerase:
RT overproduction, purification, and characterization.";
RL Arch. Biochem. Biophys. 332:30-34(1996).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND METAL
RP IONS, AND SUBUNIT.
RX PubMed=17250851; DOI=10.1016/j.jmb.2006.12.055;
RA Zheng W., Sun F., Bartlam M., Li X., Li R., Rao Z.;
RT "The crystal structure of human isopentenyl diphosphate isomerase at 1.7 A
RT resolution reveals its catalytic mechanism in isoprenoid biosynthesis.";
RL J. Mol. Biol. 366:1447-1458(2007).
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:0000269|PubMed:8806705}.
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:0000269|PubMed:8806705};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8806705};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:8806705};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate:
CC step 1/1. {ECO:0000269|PubMed:8806705}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17250851}.
CC -!- INTERACTION:
CC Q13907-2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-13341351, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O35586}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13907-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13907-2; Sequence=VSP_037889;
CC -!- SIMILARITY: Belongs to the IPP isomerase type 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57827.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK29357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK49434.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK49435.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP35407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA34890.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17025; CAA34890.1; ALT_INIT; mRNA.
DR EMBL; AF291755; AAK29357.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF271720; AAK49435.1; ALT_INIT; mRNA.
DR EMBL; AF271724; AAK49434.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF271721; AAK49434.1; JOINED; Genomic_DNA.
DR EMBL; AF271722; AAK49434.1; JOINED; Genomic_DNA.
DR EMBL; AF271723; AAK49434.1; JOINED; Genomic_DNA.
DR EMBL; BT006761; AAP35407.1; ALT_INIT; mRNA.
DR EMBL; AK303669; BAG64667.1; -; mRNA.
DR EMBL; AC022536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86521.1; -; Genomic_DNA.
DR EMBL; BC005247; AAH05247.2; -; mRNA.
DR EMBL; BC006999; AAH06999.2; -; mRNA.
DR EMBL; BC019227; AAH19227.2; -; mRNA.
DR EMBL; BC022418; AAH22418.2; -; mRNA.
DR EMBL; BC025375; AAH25375.2; -; mRNA.
DR EMBL; BC057827; AAH57827.1; ALT_INIT; mRNA.
DR EMBL; BC107893; AAI07894.1; -; mRNA.
DR EMBL; AK222875; BAD96595.1; -; mRNA.
DR CCDS; CCDS7056.1; -. [Q13907-2]
DR RefSeq; NP_001304884.1; NM_001317955.1.
DR RefSeq; NP_001304885.1; NM_001317956.1.
DR RefSeq; NP_001304886.1; NM_001317957.1.
DR RefSeq; NP_004499.2; NM_004508.3. [Q13907-2]
DR RefSeq; XP_011517759.1; XM_011519457.1.
DR PDB; 2DHO; X-ray; 1.60 A; A=1-227.
DR PDB; 2I6K; X-ray; 2.00 A; A/B=1-227.
DR PDB; 2ICJ; X-ray; 1.70 A; A=1-227.
DR PDB; 2ICK; X-ray; 1.93 A; A=1-227.
DR PDBsum; 2DHO; -.
DR PDBsum; 2I6K; -.
DR PDBsum; 2ICJ; -.
DR PDBsum; 2ICK; -.
DR AlphaFoldDB; Q13907; -.
DR SMR; Q13907; -.
DR BioGRID; 109648; 19.
DR IntAct; Q13907; 10.
DR MINT; Q13907; -.
DR STRING; 9606.ENSP00000370748; -.
DR DrugBank; DB01785; Dimethylallyl Diphosphate.
DR GuidetoPHARMACOLOGY; 646; -.
DR SwissLipids; SLP:000001219; -. [Q13907-1]
DR GlyGen; Q13907; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13907; -.
DR PhosphoSitePlus; Q13907; -.
DR BioMuta; IDI1; -.
DR DMDM; 6225527; -.
DR EPD; Q13907; -.
DR jPOST; Q13907; -.
DR MassIVE; Q13907; -.
DR MaxQB; Q13907; -.
DR PaxDb; Q13907; -.
DR PeptideAtlas; Q13907; -.
DR PRIDE; Q13907; -.
DR ProteomicsDB; 59723; -. [Q13907-1]
DR ProteomicsDB; 59724; -. [Q13907-2]
DR Antibodypedia; 23803; 170 antibodies from 28 providers.
DR DNASU; 3422; -.
DR Ensembl; ENST00000381344.8; ENSP00000370748.3; ENSG00000067064.12. [Q13907-2]
DR Ensembl; ENST00000429642.2; ENSP00000401879.2; ENSG00000067064.12. [Q13907-1]
DR GeneID; 3422; -.
DR KEGG; hsa:3422; -.
DR MANE-Select; ENST00000381344.8; ENSP00000370748.3; NM_004508.4; NP_004499.2. [Q13907-2]
DR UCSC; uc001iga.4; human. [Q13907-1]
DR CTD; 3422; -.
DR DisGeNET; 3422; -.
DR GeneCards; IDI1; -.
DR HGNC; HGNC:5387; IDI1.
DR HPA; ENSG00000067064; Low tissue specificity.
DR MIM; 604055; gene.
DR neXtProt; NX_Q13907; -.
DR OpenTargets; ENSG00000067064; -.
DR PharmGKB; PA29635; -.
DR VEuPathDB; HostDB:ENSG00000067064; -.
DR eggNOG; KOG0142; Eukaryota.
DR GeneTree; ENSGT00390000008527; -.
DR HOGENOM; CLU_060552_0_2_1; -.
DR InParanoid; Q13907; -.
DR OrthoDB; 871473at2759; -.
DR PhylomeDB; Q13907; -.
DR TreeFam; TF300129; -.
DR BioCyc; MetaCyc:HS00895-MON; -.
DR BRENDA; 5.3.3.2; 2681.
DR PathwayCommons; Q13907; -.
DR Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR SABIO-RK; Q13907; -.
DR SignaLink; Q13907; -.
DR UniPathway; UPA00059; UER00104.
DR BioGRID-ORCS; 3422; 189 hits in 1074 CRISPR screens.
DR ChiTaRS; IDI1; human.
DR EvolutionaryTrace; Q13907; -.
DR GenomeRNAi; 3422; -.
DR Pharos; Q13907; Tchem.
DR PRO; PR:Q13907; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q13907; protein.
DR Bgee; ENSG00000067064; Expressed in adrenal tissue and 206 other tissues.
DR ExpressionAtlas; Q13907; baseline and differential.
DR Genevisible; Q13907; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
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:0008299; P:isoprenoid 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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cholesterol biosynthesis;
KW Cholesterol metabolism; Isomerase; Isoprene biosynthesis;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding; Peroxisome;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..227
FT /note="Isopentenyl-diphosphate Delta-isomerase 1"
FT /id="PRO_0000205222"
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 ACT_SITE 86
FT ACT_SITE 148
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17250851"
FT BINDING 40
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17250851"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17250851"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17250851"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1
FT /note="M -> MWRGLALARAIGCAARGRGQWAVRAADCAQSGRHPGPAVVCGRRLIS
FT VLEQIRHFVMM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.9"
FT /id="VSP_037889"
FT CONFLICT 45
FT /note="I -> V (in Ref. 9; BAD96595)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> T (in Ref. 8; AAH19227)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="R -> G (in Ref. 9; BAD96595)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Y -> H (in Ref. 8; AAH06999)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2I6K"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:2ICJ"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:2DHO"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 128..139
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 141..156
FT /evidence="ECO:0007829|PDB:2DHO"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 205..209
FT /evidence="ECO:0007829|PDB:2DHO"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:2DHO"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:2DHO"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:2DHO"
FT CONFLICT Q13907-2:39
FT /note="V -> G (in Ref. 8; AAI07894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 26319 MW; 1255ACC2C4D1E8D1 CRC64;
MPEINTNHLD KQQVQLLAEM CILIDENDNK IGAETKKNCH LNENIEKGLL HRAFSVFLFN
TENKLLLQQR SDAKITFPGC FTNTCCSHPL SNPAELEESD ALGVRRAAQR RLKAELGIPL
EEVPPEEINY LTRIHYKAQS DGIWGEHEID YILLVRKNVT LNPDPNEIKS YCYVSKEELK
ELLKKAASGE IKITPWFKII AATFLFKWWD NLNHLNQFVD HEKIYRM
