FPPS_HUMAN
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 03-AUG-2022, entry version 231.
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};
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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; 113.
DR DIP; DIP-50059N; -.
DR IntAct; P14324; 34.
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 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; P14324; -.
DR PeptideAtlas; P14324; -.
DR PRIDE; P14324; -.
DR ProteomicsDB; 19455; -.
DR ProteomicsDB; 53046; -. [P14324-1]
DR TopDownProteomics; P14324-1; -. [P14324-1]
DR Antibodypedia; 34190; 457 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 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; DENYGQK; -.
DR OrthoDB; 1066656at2759; -.
DR PhylomeDB; P14324; -.
DR TreeFam; TF300897; -.
DR BioCyc; MetaCyc:ENSG00000160752-MON; -.
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; 419 hits in 1097 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 206 other tissues.
DR ExpressionAtlas; P14324; baseline and differential.
DR Genevisible; P14324; HS.
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; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
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
