LOCUS       NM_002004               1417 bp    mRNA    linear   PRI 23-JUL-2024
DEFINITION  Homo sapiens farnesyl diphosphate synthase (FDPS), transcript
            variant 1, mRNA.
ACCESSION   NM_002004
VERSION     NM_002004.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1417)
  AUTHORS   Guarana,W.L., Lima,C.A.D., Barbosa,A.D., Crovella,S. and
            Sandrin-Garcia,P.
  TITLE     Farnesyl Diphosphate Synthase Gene Associated with Loss of Bone
            Mass Density and Alendronate Treatment Failure in Patients with
            Primary Osteoporosis
  JOURNAL   Int J Mol Sci 25 (11), 5623 (2024)
   PUBMED   38891810
  REMARK    GeneRIF: Farnesyl Diphosphate Synthase Gene Associated with Loss of
            Bone Mass Density and Alendronate Treatment Failure in Patients
            with Primary Osteoporosis.
            Publication Status: Online-Only
REFERENCE   2  (bases 1 to 1417)
  AUTHORS   Liu,J., Zhang,X., Zhang,Y., Qian,M., Yang,M., Yang,S. and Wang,L.
  TITLE     Farnesyl diphosphate synthase exacerbates nonalcoholic
            steatohepatitis via the activation of AHR-CD36 axis
  JOURNAL   FASEB J 37 (7), e23035 (2023)
   PUBMED   37310396
  REMARK    GeneRIF: Farnesyl diphosphate synthase exacerbates nonalcoholic
            steatohepatitis via the activation of AHR-CD36 axis.
REFERENCE   3  (bases 1 to 1417)
  AUTHORS   Li,L., Zuo,N., Yang,D., Zhang,D., Feng,Y. and Li,X.
  TITLE     Novel missense mutations of MVK and FDPS gene in Chinese patients
            with disseminated superficial actinic porokeratosis
  JOURNAL   Clin Chim Acta 523, 441-445 (2021)
   PUBMED   34751146
  REMARK    GeneRIF: Novel missense mutations of MVK and FDPS gene in Chinese
            patients with disseminated superficial actinic porokeratosis.
REFERENCE   4  (bases 1 to 1417)
  AUTHORS   Covelli,V., Grimaldi,M., Randino,R., Firoznezhad,M., Proto,M.C.,
            Simone,V., Matteoli,G., Gazzerro,P., Bifulco,M., D'Ursi,A.M. and
            Rodriquez,M.
  TITLE     Towards an Improvement of Anticancer Activity of Benzyl Adenosine
            Analogs
  JOURNAL   Molecules 26 (23), 7146 (2021)
   PUBMED   34885721
  REMARK    GeneRIF: Towards an Improvement of Anticancer Activity of Benzyl
            Adenosine Analogs.
            Publication Status: Online-Only
REFERENCE   5  (bases 1 to 1417)
  AUTHORS   Haenig,C., Atias,N., Taylor,A.K., Mazza,A., Schaefer,M.H., Russ,J.,
            Riechers,S.P., Jain,S., Coughlin,M., Fontaine,J.F., Freibaum,B.D.,
            Brusendorf,L., Zenkner,M., Porras,P., Stroedicke,M., Schnoegl,S.,
            Arnsburg,K., Boeddrich,A., Pigazzini,L., Heutink,P., Taylor,J.P.,
            Kirstein,J., Andrade-Navarro,M.A., Sharan,R. and Wanker,E.E.
  TITLE     Interactome Mapping Provides a Network of Neurodegenerative Disease
            Proteins and Uncovers Widespread Protein Aggregation in Affected
            Brains
  JOURNAL   Cell Rep 32 (7), 108050 (2020)
   PUBMED   32814053
REFERENCE   6  (bases 1 to 1417)
  AUTHORS   Ohnuma,Si., Hirooka,K., Ohto,C. and Nishino,T.
  TITLE     Conversion from archaeal geranylgeranyl diphosphate synthase to
            farnesyl diphosphate synthase. Two amino acids before the first
            aspartate-rich motif solely determine eukaryotic farnesyl
            diphosphate synthase activity
  JOURNAL   J Biol Chem 272 (8), 5192-5198 (1997)
   PUBMED   9030588
REFERENCE   7  (bases 1 to 1417)
  AUTHORS   Krisans,S.K., Ericsson,J., Edwards,P.A. and Keller,G.A.
  TITLE     Farnesyl-diphosphate synthase is localized in peroxisomes
  JOURNAL   J Biol Chem 269 (19), 14165-14169 (1994)
   PUBMED   8188698
REFERENCE   8  (bases 1 to 1417)
  AUTHORS   Ding,V.D., Sheares,B.T., Bergstrom,J.D., Ponpipom,M.M., Perez,L.B.
            and Poulter,C.D.
  TITLE     Purification and characterization of recombinant human farnesyl
            diphosphate synthase expressed in Escherichia coli
  JOURNAL   Biochem J 275 (Pt 1) (Pt 1), 61-65 (1991)
   PUBMED   2018485
REFERENCE   9  (bases 1 to 1417)
  AUTHORS   Wilkin,D.J., Kutsunai,S.Y. and Edwards,P.A.
  TITLE     Isolation and sequence of the human farnesyl pyrophosphate
            synthetase cDNA. Coordinate regulation of the mRNAs for farnesyl
            pyrophosphate synthetase, 3-hydroxy-3-methylglutaryl coenzyme A
            reductase, and 3-hydroxy-3-methylglutaryl coenzyme A synthase by
            phorbol ester
  JOURNAL   J Biol Chem 265 (8), 4607-4614 (1990)
   PUBMED   1968462
REFERENCE   10 (bases 1 to 1417)
  AUTHORS   Sheares,B.T., White,S.S., Molowa,D.T., Chan,K., Ding,V.D.,
            Kroon,P.A., Bostedor,R.G. and Karkas,J.D.
  TITLE     Cloning, analysis, and bacterial expression of human farnesyl
            pyrophosphate synthetase and its regulation in Hep G2 cells
  JOURNAL   Biochemistry 28 (20), 8129-8135 (1989)
   PUBMED   2690933
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CN346026.1 and BC010004.2.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jun 2, 2019 this sequence version replaced NM_002004.3.
            
            Summary: This gene encodes an enzyme that catalyzes the production
            of geranyl pyrophosphate and farnesyl pyrophosphate from
            isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The
            resulting product, farnesyl pyrophosphate, is a key intermediate in
            cholesterol and sterol biosynthesis, a substrate for protein
            farnesylation and geranylgeranylation, and a ligand or agonist for
            certain hormone receptors and growth receptors. Drugs that inhibit
            this enzyme prevent the post-translational modifications of small
            GTPases and have been used to treat diseases related to bone
            resorption. Multiple pseudogenes have been found on chromosomes 1,
            7, 14, 15, 21 and X. Multiple transcript variants encoding
            different isoforms have been found for this gene.[provided by
            RefSeq, Oct 2008].
            
            Transcript Variant: This variant (1) represents the longest
            transcript and encodes the longer isoform (a). Both variants 1 and
            2 encode the same isoform (a).
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK291084.1, SRR14038191.441596.1
                                           [ECO:0000332]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000368356.9/ ENSP00000357340.4
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      longest protein
            ##RefSeq-Attributes-END##
            COMPLETENESS: complete on the 3' end.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-93                CN346026.1         89-181
            94-1417             BC010004.2         1-1324
FEATURES             Location/Qualifiers
     source          1..1417
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1q22"
     gene            1..1417
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /note="farnesyl diphosphate synthase"
                     /db_xref="GeneID:2224"
                     /db_xref="HGNC:HGNC:3631"
                     /db_xref="MIM:134629"
     exon            1..100
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            101..277
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     CDS             102..1361
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /EC_number="2.5.1.1"
                     /EC_number="2.5.1.10"
                     /note="isoform a is encoded by transcript variant 1;
                     farnesyl pyrophosphate synthetase,
                     dimethylallyltranstransferase, geranyltranstransferase;
                     FPP synthetase; farnesyl pyrophosphate synthase; FPP
                     synthase; (2E,6E)-farnesyl diphosphate synthase"
                     /codon_start=1
                     /product="farnesyl pyrophosphate synthase isoform a"
                     /protein_id="NP_001995.1"
                     /db_xref="CCDS:CCDS1110.1"
                     /db_xref="GeneID:2224"
                     /db_xref="HGNC:HGNC:3631"
                     /db_xref="MIM:134629"
                     /translation="MPLSRWLRSVGVFLLPAPYWAPRERWLGSLRRPSLVHGYPVLAW
                     HSARCWCQAWTEEPRALCSSLRMNGDQNSDVYAQEKQDFVQHFSQIVRVLTEDEMGHP
                     EIGDAIARLKEVLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVEL
                     LQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPY
                     YLNLIELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPI
                     AAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCS
                     WLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIM
                     ALIEQYAAPLPPAVFLGLARKIYKRRK"
     exon            278..440
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            441..581
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            582..662
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            663..785
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            786..874
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            875..947
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            948..1025
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            1026..1160
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     exon            1161..1417
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1397..1402
                     /regulatory_class="polyA_signal_sequence"
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /note="hexamer: AATAAA"
     polyA_site      1417
                     /gene="FDPS"
                     /gene_synonym="FPPS; FPS; POROK9"
                     /note="major polyA site"
ORIGIN      
        1 gggaactact cgacccacag agccgatcgc ggagcggatt ctgcttttag gagtacccgc
       61 caacaagcgg gaccgagcag gaatccgtat ctgggaacag gatgcccctg tcccgctggt
      121 tgagatctgt gggggtcttc ctgctgccag ccccctactg ggcaccccgg gagaggtggc
      181 tgggttccct acggcggccc tccctggtgc acgggtaccc agtcctggcc tggcacagtg
      241 cccgctgctg gtgccaagcg tggacagagg aacctcgagc cctttgctcc tccctcagaa
      301 tgaacggaga ccagaattca gatgtttatg cccaagaaaa gcaggatttc gttcagcact
      361 tctcccagat cgttagggtg ctgactgagg atgagatggg gcacccagag ataggagatg
      421 ctattgcccg gctcaaggag gtcctggagt acaatgccat tggaggcaag tataaccggg
      481 gtttgacggt ggtagtagca ttccgggagc tggtggagcc aaggaaacag gatgctgata
      541 gtctccagcg ggcctggact gtgggctggt gtgtggaact gctgcaagct ttcttcctgg
      601 tggcagatga catcatggat tcatccctta cccgccgggg acagatctgc tggtatcaga
      661 agccgggcgt gggtttggat gccatcaatg atgctaacct cctggaagca tgtatctacc
      721 gcctgctgaa gctctattgc cgggagcagc cctattacct gaacctgatc gagctcttcc
      781 tgcagagttc ctatcagact gagattgggc agaccctgga cctcctcaca gccccccagg
      841 gcaatgtgga tcttgtcaga ttcactgaaa agaggtacaa atctattgtc aagtacaaga
      901 cagctttcta ctccttctac cttcctatag ctgcagccat gtacatggca ggaattgatg
      961 gcgagaagga gcacgccaat gccaagaaga tcctgctgga gatgggggag ttctttcaga
     1021 ttcaggatga ttaccttgac ctctttgggg accccagtgt gaccggcaaa attggcactg
     1081 acatccagga caacaaatgc agctggctgg tggttcagtg tctgcaacgg gccactccag
     1141 aacagtacca gatcctgaag gaaaattacg ggcagaagga ggctgagaaa gtggcccggg
     1201 tgaaggcgct atatgaggag ctggatctgc cagcagtgtt cttgcaatat gaggaagaca
     1261 gttacagcca cattatggct ctcattgaac agtacgcagc acccctgccc ccagccgtct
     1321 ttctggggct tgcgcgcaaa atctacaagc ggagaaagtg acctagagat tgcaagggcg
     1381 gggagaggag gctctcaata aataatcgtg taacctt
//
