ID FPPS_HUMAN Reviewed; 419 AA. AC P14324; D3DV91; E9PCI9; Q96G29; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 4. DT 27-MAR-2024, entry version 240. DE RecName: Full=Farnesyl pyrophosphate synthase {ECO:0000305}; DE Short=FPP synthase; DE Short=FPS; DE EC=2.5.1.10 {ECO:0000269|PubMed:16684881}; DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase; DE AltName: Full=Dimethylallyltranstransferase; DE EC=2.5.1.1 {ECO:0000269|PubMed:16684881}; DE AltName: Full=Farnesyl diphosphate synthase; DE AltName: Full=Geranyltranstransferase; GN Name=FDPS {ECO:0000312|HGNC:HGNC:3631}; Synonyms=FPS, KIAA1293; 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 2). RX PubMed=1968462; DOI=10.1016/s0021-9258(19)39606-1; RA Wilkin D.J., Kutsunai S.Y., Edwards P.A.; RT "Isolation and sequence of the human farnesyl pyrophosphate synthetase RT cDNA. Coordinate regulation of the mRNAs for farnesyl pyrophosphate RT synthetase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and 3-hydroxy- RT 3-methylglutaryl coenzyme A synthase by phorbol ester."; RL J. Biol. Chem. 265:4607-4614(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584026; DOI=10.1093/dnares/1.1.27; RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., RA Nagase T., Seki N., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. I. The RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of RT randomly sampled cDNA clones from human immature myeloid cell line KG-1."; RL DNA Res. 1:27-35(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-312 (ISOFORM 2). RG The MGC Project Team; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 74-419. RC TISSUE=Liver; RX PubMed=2690933; DOI=10.1021/bi00446a025; RA Sheares B.T., White S.S., Molowa D.T., Chan K., Ding V.D.-H., Kroon P.A., RA Bostedor R.G., Karkas J.D.; RT "Cloning, analysis, and bacterial expression of human farnesyl RT pyrophosphate synthetase and its regulation in Hep G2 cells."; RL Biochemistry 28:8129-8135(1989). RN [9] RP INTERACTION WITH HTLV-1 P13(II) (MICROBIAL INFECTION). RX PubMed=11773414; DOI=10.1128/jvi.76.3.1400-1414.2002; RA Lefebvre L., Vanderplasschen A., Ciminale V., Heremans H., Dangoisse O., RA Jauniaux J.-C., Toussaint J.-F., Zelnik V., Burny A., Kettmann R., RA Willems L.; RT "Oncoviral bovine leukemia virus G4 and human T-cell leukemia virus type 1 RT p13(II) accessory proteins interact with farnesyl pyrophosphate RT synthetase."; RL J. Virol. 76:1400-1414(2002). RN [10] RP INTERACTION WITH RSAD2, AND ACTIVITY REGULATION. RX PubMed=18005724; DOI=10.1016/j.chom.2007.06.009; RA Wang X., Hinson E.R., Cresswell P.; RT "The interferon-inducible protein viperin inhibits influenza virus release RT by perturbing lipid rafts."; RL Cell Host Microbe 2:96-105(2007). RN [11] RP REVIEW. RX PubMed=15827605; RA Szkopinska A., Plochocka D.; RT "Farnesyl diphosphate synthase; regulation of product specificity."; RL Acta Biochim. Pol. 52:45-55(2005). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123 AND LYS-353, AND RP IDENTIFICATION BY MASS 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 [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] 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 [18] RP INVOLVEMENT IN POROK9, AND VARIANT POROK9 GLN-179. RX PubMed=26202976; DOI=10.7554/elife.06322; RA Zhang Z., Li C., Wu F., Ma R., Luan J., Yang F., Liu W., Wang L., Zhang S., RA Liu Y., Gu J., Hua W., Fan M., Peng H., Meng X., Song N., Bi X., Gu C., RA Zhang Z., Huang Q., Chen L., Xiang L., Xu J., Zheng Z., Jiang Z.; RT "Genomic variations of the mevalonate pathway in porokeratosis."; RL Elife 4:E06322-E06322(2015). RN [19] 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 [20] RP HYDROXYBUTYRYLATION AT LYS-123. RX PubMed=29192674; DOI=10.1038/cr.2017.149; RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J., RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.; RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation RT pathway."; RL Cell Res. 28:111-125(2018). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 72-419, AND SUBUNIT. RX PubMed=16892359; DOI=10.1002/cmdc.200500059; RA Rondeau J.-M., Bitsch F., Bourgier E., Geiser M., Hemmig R., Kroemer M., RA Lehmann S., Ramage P., Rieffel S., Strauss A., Green J.R., Jahnke W.; RT "Structural basis for the exceptional in vivo efficacy of bisphosphonate RT drugs."; RL ChemMedChem 1:267-273(2006). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 67-419 IN COMPLEXES WITH RP MAGNESIUM IONS; ISOPENTENYL DIPHOSPHATE; RISEDRONATE AND ZOLEDRONATE, AND RP CATALYTIC ACTIVITY. RX PubMed=16684881; DOI=10.1073/pnas.0601643103; RA Kavanagh K.L., Guo K., Dunford J.E., Wu X., Knapp S., Ebetino F.H., RA Rogers M.J., Russell R.G., Oppermann U.; RT "The molecular mechanism of nitrogen-containing bisphosphonates as RT antiosteoporosis drugs."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7829-7834(2006). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 67-419 IN COMPLEXES WITH MAGNESIUM RP AND BIPHOSPHONATES. RX PubMed=19309137; DOI=10.1021/ja808285e; RA Zhang Y., Cao R., Yin F., Hudock M.P., Guo R.-T., Krysiak K., Mukherjee S., RA Gao Y.-G., Robinson H., Song Y., No J.H., Bergan K., Leon A., Cass L., RA Goddard A., Chang T.-K., Lin F.-Y., Van Beek E., Papapoulos S., RA Wang A.H.-J., Kubo T., Ochi M., Mukkamala D., Oldfield E.; RT "Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate RT synthase inhibitors: an X-ray and NMR investigation."; RL J. Am. Chem. Soc. 131:5153-5162(2009). CC -!- FUNCTION: Key enzyme in isoprenoid biosynthesis which catalyzes the CC formation of farnesyl diphosphate (FPP), a precursor for several CC classes of essential metabolites including sterols, dolichols, CC carotenoids, and ubiquinones. FPP also serves as substrate for protein CC farnesylation and geranylgeranylation. Catalyzes the sequential CC condensation of isopentenyl pyrophosphate with the allylic CC pyrophosphates, dimethylallyl pyrophosphate, and then with the CC resultant geranylpyrophosphate to the ultimate product farnesyl CC pyrophosphate. CC -!- CATALYTIC ACTIVITY: CC Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)- CC geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, CC ChEBI:CHEBI:128769; EC=2.5.1.1; CC Evidence={ECO:0000269|PubMed:16684881}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)- CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, CC ChEBI:CHEBI:175763; EC=2.5.1.10; CC Evidence={ECO:0000269|PubMed:16684881}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:19309137}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:19309137}; CC -!- ACTIVITY REGULATION: Inactivated by interferon-induced RSAD2. This CC inactivation may result of disruption of lipid rafts at the plasma CC membrane, and thus have an antiviral effect since many enveloped CC viruses need lipid rafts to bud efficiently out of the cell. CC {ECO:0000269|PubMed:18005724}. CC -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; CC farnesyl diphosphate from geranyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; CC geranyl diphosphate from dimethylallyl diphosphate and isopentenyl CC diphosphate: step 1/1. CC -!- SUBUNIT: Homodimer. Interacts with RSAD2. {ECO:0000269|PubMed:11773414, CC ECO:0000269|PubMed:16892359, ECO:0000269|PubMed:18005724}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 protein p13(II). CC {ECO:0000269|PubMed:11773414}. CC -!- INTERACTION: CC P14324; O95870: ABHD16A; NbExp=3; IntAct=EBI-948245, EBI-348517; CC P14324; P54253: ATXN1; NbExp=4; IntAct=EBI-948245, EBI-930964; CC P14324; Q6ZMZ0: RNF19B; NbExp=3; IntAct=EBI-948245, EBI-2466594; CC P14324; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-948245, EBI-8644112; CC P14324; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-948245, EBI-17280858; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P14324-1; Sequence=Displayed; CC Name=2; CC IsoId=P14324-2; Sequence=VSP_046958; CC -!- DISEASE: Porokeratosis 9, multiple types (POROK9) [MIM:616631]: A form CC of porokeratosis, a disorder of faulty keratinization characterized by CC one or more atrophic patches surrounded by a distinctive hyperkeratotic CC ridgelike border called the cornoid lamella. The keratotic lesions can CC progress to overt cutaneous neoplasms, typically squamous cell CC carcinomas. Multiple clinical variants of porokeratosis are recognized, CC including porokeratosis of Mibelli, linear porokeratosis, disseminated CC superficial actinic porokeratosis, palmoplantar porokeratosis, and CC punctate porokeratosis. Different clinical presentations can be CC observed among members of the same family. Individuals expressing more CC than one variant have also been reported. CC {ECO:0000269|PubMed:26202976}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA03523.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; J05262; AAA52423.1; -; mRNA. DR EMBL; D14697; BAA03523.2; ALT_INIT; mRNA. DR EMBL; AK291084; BAF83773.1; -; mRNA. DR EMBL; AL139410; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471121; EAW53076.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53077.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53078.1; -; Genomic_DNA. DR EMBL; BC010004; AAH10004.1; -; mRNA. DR EMBL; BQ062616; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M29863; AAA35820.1; -; mRNA. DR CCDS; CCDS1110.1; -. [P14324-1] DR CCDS; CCDS44241.1; -. [P14324-2] DR PIR; A35726; A35726. DR RefSeq; NP_001129293.1; NM_001135821.1. [P14324-1] DR RefSeq; NP_001129294.1; NM_001135822.1. [P14324-2] DR RefSeq; NP_001229753.1; NM_001242824.1. [P14324-2] DR RefSeq; NP_001229754.1; NM_001242825.1. DR RefSeq; NP_001995.1; NM_002004.3. [P14324-1] DR RefSeq; XP_005245019.1; XM_005244962.1. DR RefSeq; XP_005245020.1; XM_005244963.1. DR PDB; 1YQ7; X-ray; 2.20 A; A=67-419. DR PDB; 1YV5; X-ray; 2.00 A; A=67-419. DR PDB; 1ZW5; X-ray; 2.30 A; A=67-419. DR PDB; 2F7M; X-ray; 2.30 A; F=72-419. DR PDB; 2F89; X-ray; 2.60 A; F=72-419. DR PDB; 2F8C; X-ray; 2.20 A; F=72-419. DR PDB; 2F8Z; X-ray; 2.60 A; F=72-419. DR PDB; 2F92; X-ray; 2.15 A; F=72-419. DR PDB; 2F94; X-ray; 1.94 A; F=72-419. DR PDB; 2F9K; X-ray; 2.06 A; F=72-419. DR PDB; 2OPM; X-ray; 2.40 A; A=67-419. DR PDB; 2OPN; X-ray; 2.70 A; A=67-419. DR PDB; 2QIS; X-ray; 1.80 A; A=67-419. DR PDB; 2RAH; X-ray; 2.00 A; A=67-419. DR PDB; 2VF6; X-ray; 2.10 A; A=67-419. DR PDB; 3B7L; X-ray; 1.95 A; A=67-419. DR PDB; 3CP6; X-ray; 1.95 A; A=67-419. DR PDB; 3N1V; X-ray; 2.18 A; F=72-419. DR PDB; 3N1W; X-ray; 2.56 A; F=72-419. DR PDB; 3N3L; X-ray; 2.74 A; F=72-419. DR PDB; 3N45; X-ray; 1.88 A; F=72-419. DR PDB; 3N46; X-ray; 2.35 A; F=72-419. DR PDB; 3N49; X-ray; 2.50 A; F=72-419. DR PDB; 3N5H; X-ray; 2.20 A; F=72-419. DR PDB; 3N5J; X-ray; 2.35 A; F=72-419. DR PDB; 3N6K; X-ray; 2.25 A; F=72-419. DR PDB; 3RYE; X-ray; 2.10 A; A=71-419. DR PDB; 3S4J; X-ray; 1.95 A; A=71-419. DR PDB; 4DEM; X-ray; 1.85 A; F=67-419. DR PDB; 4GA3; X-ray; 2.39 A; A=72-419. DR PDB; 4H5C; X-ray; 2.02 A; F=67-419. DR PDB; 4H5D; X-ray; 2.02 A; F=67-419. DR PDB; 4H5E; X-ray; 2.04 A; F=67-419. DR PDB; 4JVJ; X-ray; 2.80 A; F=67-419. DR PDB; 4KFA; X-ray; 1.98 A; A=67-419. DR PDB; 4KPD; X-ray; 1.96 A; A=67-419. DR PDB; 4KPJ; X-ray; 1.95 A; A=67-419. DR PDB; 4KQ5; X-ray; 2.40 A; A=67-419. DR PDB; 4KQS; X-ray; 1.97 A; A=67-419. DR PDB; 4KQU; X-ray; 2.07 A; A=67-419. DR PDB; 4L2X; X-ray; 2.55 A; F=67-419. DR PDB; 4LFV; X-ray; 2.00 A; F=67-419. DR PDB; 4LPG; X-ray; 2.35 A; F=67-419. DR PDB; 4LPH; X-ray; 2.30 A; F=67-419. DR PDB; 4N1Z; X-ray; 2.35 A; F=72-419. DR PDB; 4N9U; X-ray; 2.11 A; A=67-419. DR PDB; 4NFI; X-ray; 1.85 A; F=67-419. DR PDB; 4NFJ; X-ray; 2.05 A; F=67-419. DR PDB; 4NFK; X-ray; 1.85 A; F=67-419. DR PDB; 4NG6; X-ray; 2.35 A; A=67-419. DR PDB; 4NKE; X-ray; 1.46 A; A=67-419. DR PDB; 4NKF; X-ray; 2.00 A; A=67-419. DR PDB; 4NUA; X-ray; 1.43 A; A=67-419. DR PDB; 4OGU; X-ray; 2.10 A; A=67-419. DR PDB; 4P0V; X-ray; 2.40 A; A=73-419. DR PDB; 4P0W; X-ray; 2.41 A; A=72-419. DR PDB; 4P0X; X-ray; 2.50 A; A=72-419. DR PDB; 4PVX; X-ray; 2.18 A; F=67-419. DR PDB; 4PVY; X-ray; 2.05 A; F=67-419. DR PDB; 4Q23; X-ray; 1.98 A; A=67-419. DR PDB; 4QPF; X-ray; 1.59 A; A=67-419. DR PDB; 4QXS; X-ray; 1.90 A; F=67-419. DR PDB; 4RXA; X-ray; 2.20 A; A=72-419. DR PDB; 4XQR; X-ray; 2.15 A; F=67-419. DR PDB; 4XQS; X-ray; 2.30 A; F=67-419. DR PDB; 4XQT; X-ray; 2.10 A; F=67-419. DR PDB; 5CG5; Other; 1.40 A; A=74-419. DR PDB; 5CG6; Other; 1.70 A; A=74-419. DR PDB; 5DGM; X-ray; 2.86 A; F=72-419. DR PDB; 5DGN; X-ray; 2.08 A; F=72-419. DR PDB; 5DGS; X-ray; 2.62 A; F=72-419. DR PDB; 5DIQ; X-ray; 2.10 A; F=72-419. DR PDB; 5DJP; X-ray; 2.40 A; F=72-419. DR PDB; 5DJR; X-ray; 2.40 A; F=72-419. DR PDB; 5DJV; X-ray; 2.30 A; F=72-419. DR PDB; 5JA0; X-ray; 1.90 A; F=67-419. DR PDB; 5JUZ; X-ray; 2.40 A; F=67-419. DR PDB; 5JV0; X-ray; 2.40 A; F=67-419. DR PDB; 5JV1; X-ray; 2.30 A; F=67-419. DR PDB; 5JV2; X-ray; 2.30 A; F=67-419. DR PDB; 5KSX; X-ray; 2.65 A; F=67-419. DR PDB; 5YGI; X-ray; 2.18 A; A=72-419. DR PDB; 6N7Y; X-ray; 2.00 A; F=67-419. DR PDB; 6N7Z; X-ray; 2.55 A; F=67-419. DR PDB; 6N82; X-ray; 2.00 A; F=67-419. DR PDB; 6N83; X-ray; 2.00 A; F=67-419. DR PDB; 6OAG; X-ray; 2.30 A; F=67-419. DR PDB; 6OAH; X-ray; 2.20 A; F=67-419. DR PDBsum; 1YQ7; -. DR PDBsum; 1YV5; -. DR PDBsum; 1ZW5; -. DR PDBsum; 2F7M; -. DR PDBsum; 2F89; -. DR PDBsum; 2F8C; -. DR PDBsum; 2F8Z; -. DR PDBsum; 2F92; -. DR PDBsum; 2F94; -. DR PDBsum; 2F9K; -. DR PDBsum; 2OPM; -. DR PDBsum; 2OPN; -. DR PDBsum; 2QIS; -. DR PDBsum; 2RAH; -. DR PDBsum; 2VF6; -. DR PDBsum; 3B7L; -. DR PDBsum; 3CP6; -. DR PDBsum; 3N1V; -. DR PDBsum; 3N1W; -. DR PDBsum; 3N3L; -. DR PDBsum; 3N45; -. DR PDBsum; 3N46; -. DR PDBsum; 3N49; -. DR PDBsum; 3N5H; -. DR PDBsum; 3N5J; -. DR PDBsum; 3N6K; -. DR PDBsum; 3RYE; -. DR PDBsum; 3S4J; -. DR PDBsum; 4DEM; -. DR PDBsum; 4GA3; -. DR PDBsum; 4H5C; -. DR PDBsum; 4H5D; -. DR PDBsum; 4H5E; -. DR PDBsum; 4JVJ; -. DR PDBsum; 4KFA; -. DR PDBsum; 4KPD; -. DR PDBsum; 4KPJ; -. DR PDBsum; 4KQ5; -. DR PDBsum; 4KQS; -. DR PDBsum; 4KQU; -. DR PDBsum; 4L2X; -. DR PDBsum; 4LFV; -. DR PDBsum; 4LPG; -. DR PDBsum; 4LPH; -. DR PDBsum; 4N1Z; -. DR PDBsum; 4N9U; -. DR PDBsum; 4NFI; -. DR PDBsum; 4NFJ; -. DR PDBsum; 4NFK; -. DR PDBsum; 4NG6; -. DR PDBsum; 4NKE; -. DR PDBsum; 4NKF; -. DR PDBsum; 4NUA; -. DR PDBsum; 4OGU; -. DR PDBsum; 4P0V; -. DR PDBsum; 4P0W; -. DR PDBsum; 4P0X; -. DR PDBsum; 4PVX; -. DR PDBsum; 4PVY; -. DR PDBsum; 4Q23; -. DR PDBsum; 4QPF; -. DR PDBsum; 4QXS; -. DR PDBsum; 4RXA; -. DR PDBsum; 4XQR; -. DR PDBsum; 4XQS; -. DR PDBsum; 4XQT; -. DR PDBsum; 5CG5; -. DR PDBsum; 5CG6; -. DR PDBsum; 5DGM; -. DR PDBsum; 5DGN; -. DR PDBsum; 5DGS; -. DR PDBsum; 5DIQ; -. DR PDBsum; 5DJP; -. DR PDBsum; 5DJR; -. DR PDBsum; 5DJV; -. DR PDBsum; 5JA0; -. DR PDBsum; 5JUZ; -. DR PDBsum; 5JV0; -. DR PDBsum; 5JV1; -. DR PDBsum; 5JV2; -. DR PDBsum; 5KSX; -. DR PDBsum; 5YGI; -. DR PDBsum; 6N7Y; -. DR PDBsum; 6N7Z; -. DR PDBsum; 6N82; -. DR PDBsum; 6N83; -. DR PDBsum; 6OAG; -. DR PDBsum; 6OAH; -. DR AlphaFoldDB; P14324; -. DR SMR; P14324; -. DR BioGRID; 108517; 154. DR DIP; DIP-50059N; -. DR IntAct; P14324; 36. DR MINT; P14324; -. DR STRING; 9606.ENSP00000349078; -. DR BindingDB; P14324; -. DR ChEMBL; CHEMBL1782; -. DR DrugBank; DB00630; Alendronic acid. DR DrugBank; DB01785; Dimethylallyl Diphosphate. DR DrugBank; DB07780; Farnesyl diphosphate. DR DrugBank; DB02552; Geranyl Diphosphate. DR DrugBank; DB07841; Geranylgeranyl diphosphate. DR DrugBank; DB00710; Ibandronate. DR DrugBank; DB06255; Incadronic acid. DR DrugBank; DB04714; ISOPENTENYL PYROPHOSPHATE. DR DrugBank; DB02508; Isopentyl Pyrophosphate. DR DrugBank; DB06548; Minodronic acid. DR DrugBank; DB00282; Pamidronic acid. DR DrugBank; DB00884; Risedronic acid. DR DrugBank; DB00399; Zoledronic acid. DR DrugCentral; P14324; -. DR GuidetoPHARMACOLOGY; 644; -. DR SwissLipids; SLP:000001248; -. DR SwissLipids; SLP:000001252; -. [P14324-2] DR GlyGen; P14324; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P14324; -. DR MetOSite; P14324; -. DR PhosphoSitePlus; P14324; -. DR SwissPalm; P14324; -. DR BioMuta; FDPS; -. DR DMDM; 215274250; -. DR EPD; P14324; -. DR jPOST; P14324; -. DR MassIVE; P14324; -. DR MaxQB; P14324; -. DR PaxDb; 9606-ENSP00000349078; -. DR PeptideAtlas; P14324; -. DR ProteomicsDB; 19455; -. DR ProteomicsDB; 53046; -. [P14324-1] DR Pumba; P14324; -. DR TopDownProteomics; P14324-1; -. [P14324-1] DR Antibodypedia; 34190; 508 antibodies from 36 providers. DR DNASU; 2224; -. DR Ensembl; ENST00000356657.10; ENSP00000349078.6; ENSG00000160752.15. [P14324-1] DR Ensembl; ENST00000368356.9; ENSP00000357340.4; ENSG00000160752.15. [P14324-1] DR Ensembl; ENST00000447866.5; ENSP00000391755.1; ENSG00000160752.15. [P14324-2] DR Ensembl; ENST00000467076.5; ENSP00000480142.1; ENSG00000160752.15. [P14324-2] DR Ensembl; ENST00000612683.1; ENSP00000478235.1; ENSG00000160752.15. [P14324-2] DR GeneID; 2224; -. DR KEGG; hsa:2224; -. DR MANE-Select; ENST00000368356.9; ENSP00000357340.4; NM_002004.4; NP_001995.1. DR UCSC; uc001fkc.3; human. [P14324-1] DR AGR; HGNC:3631; -. DR CTD; 2224; -. DR DisGeNET; 2224; -. DR GeneCards; FDPS; -. DR HGNC; HGNC:3631; FDPS. DR HPA; ENSG00000160752; Tissue enhanced (liver). DR MalaCards; FDPS; -. DR MIM; 134629; gene. DR MIM; 616631; phenotype. DR neXtProt; NX_P14324; -. DR OpenTargets; ENSG00000160752; -. DR Orphanet; 79152; Disseminated superficial actinic porokeratosis. DR PharmGKB; PA28075; -. DR VEuPathDB; HostDB:ENSG00000160752; -. DR eggNOG; KOG0711; Eukaryota. DR GeneTree; ENSGT00900000141074; -. DR HOGENOM; CLU_028376_0_1_1; -. DR InParanoid; P14324; -. DR OMA; LEMGNFF; -. DR OrthoDB; 509027at2759; -. DR PhylomeDB; P14324; -. DR TreeFam; TF300897; -. DR BioCyc; MetaCyc:ENSG00000160752-MONOMER; -. DR BRENDA; 2.5.1.1; 2681. DR BRENDA; 2.5.1.10; 2681. DR PathwayCommons; P14324; -. DR Reactome; R-HSA-191273; Cholesterol biosynthesis. DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP). DR SABIO-RK; P14324; -. DR SignaLink; P14324; -. DR UniPathway; UPA00259; UER00368. DR UniPathway; UPA00260; UER00369. DR BioGRID-ORCS; 2224; 424 hits in 1180 CRISPR screens. DR ChiTaRS; FDPS; human. DR EvolutionaryTrace; P14324; -. DR GenomeRNAi; 2224; -. DR Pharos; P14324; Tclin. DR PRO; PR:P14324; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P14324; Protein. DR Bgee; ENSG00000160752; Expressed in adrenal tissue and 208 other cell types or tissues. DR ExpressionAtlas; P14324; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004161; F:dimethylallyltranstransferase activity; IBA:GO_Central. DR GO; GO:0004337; F:geranyltranstransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006695; P:cholesterol biosynthetic process; TAS:ProtInc. DR GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00685; Trans_IPPS_HT; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR InterPro; IPR039702; FPS1-like. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR033749; Polyprenyl_synt_CS. DR PANTHER; PTHR11525:SF0; FARNESYL PYROPHOSPHATE SYNTHASE; 1. DR PANTHER; PTHR11525; FARNESYL-PYROPHOSPHATE SYNTHETASE; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. DR Genevisible; P14324; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cholesterol biosynthesis; KW Cholesterol metabolism; Cytoplasm; Disease variant; Host-virus interaction; KW Hydroxylation; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Reference proteome; Steroid biosynthesis; KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase. FT CHAIN 1..419 FT /note="Farnesyl pyrophosphate synthase" FT /id="PRO_0000123944" FT BINDING 123 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 126 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 162 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 169 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 169 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 173 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 173 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 178 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 179 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000269|PubMed:16684881, FT ECO:0007744|PDB:1ZW5" FT BINDING 266 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 267 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 306 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 323 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT BINDING 332 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000250" FT SITE 164 FT /note="Important for determining product chain length" FT /evidence="ECO:0000250" FT SITE 165 FT /note="Important for determining product chain length" FT /evidence="ECO:0000250" FT MOD_RES 123 FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate" FT /evidence="ECO:0000269|PubMed:29192674" FT MOD_RES 123 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 353 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..66 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1968462, ECO:0000303|Ref.7" FT /id="VSP_046958" FT VARIANT 179 FT /note="R -> Q (in POROK9; dbSNP:rs863225241)" FT /evidence="ECO:0000269|PubMed:26202976" FT /id="VAR_075062" FT VARIANT 364 FT /note="V -> A (in dbSNP:rs41314549)" FT /id="VAR_061274" FT VARIANT 391 FT /note="I -> V (in dbSNP:rs17456)" FT /id="VAR_049644" FT CONFLICT 141 FT /note="R -> K (in Ref. 7; BQ062616)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="I -> T (in Ref. 1; AAA52423)" FT /evidence="ECO:0000305" FT CONFLICT 284 FT /note="G -> R (in Ref. 7; BQ062616)" FT /evidence="ECO:0000305" FT HELIX 76..85 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 87..94 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:4DEM" FT HELIX 102..104 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 105..118 FT /evidence="ECO:0007829|PDB:4NUA" FT STRAND 119..122 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 125..137 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 145..172 FT /evidence="ECO:0007829|PDB:4NUA" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:4QXS" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:4NUA" FT TURN 188..190 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 194..213 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 219..243 FT /evidence="ECO:0007829|PDB:4NUA" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:4JVJ" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 256..266 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 268..271 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 273..282 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 288..315 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:4NUA" FT TURN 327..331 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 335..343 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 346..355 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 361..373 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 376..398 FT /evidence="ECO:0007829|PDB:4NUA" FT HELIX 404..414 FT /evidence="ECO:0007829|PDB:4NUA" FT MOD_RES P14324-2:1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000305" SQ SEQUENCE 419 AA; 48275 MW; 52934B80A808FB67 CRC64; MPLSRWLRSV GVFLLPAPYW APRERWLGSL RRPSLVHGYP VLAWHSARCW CQAWTEEPRA LCSSLRMNGD QNSDVYAQEK QDFVQHFSQI VRVLTEDEMG HPEIGDAIAR LKEVLEYNAI GGKYNRGLTV VVAFRELVEP RKQDADSLQR AWTVGWCVEL LQAFFLVADD IMDSSLTRRG QICWYQKPGV GLDAINDANL LEACIYRLLK LYCREQPYYL NLIELFLQSS YQTEIGQTLD LLTAPQGNVD LVRFTEKRYK SIVKYKTAFY SFYLPIAAAM YMAGIDGEKE HANAKKILLE MGEFFQIQDD YLDLFGDPSV TGKIGTDIQD NKCSWLVVQC LQRATPEQYQ ILKENYGQKE AEKVARVKAL YEELDLPAVF LQYEEDSYSH IMALIEQYAA PLPPAVFLGL ARKIYKRRK //