LOCUS       NP_032014               2504 aa            linear   ROD 12-JUN-2025
DEFINITION  fatty acid synthase [Mus musculus].
ACCESSION   NP_032014
VERSION     NP_032014.3
DBSOURCE    REFSEQ: accession NM_007988.3
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 2504)
  AUTHORS   Wang,S., He,T., Luo,Y., Ren,K., Shen,H., Hou,L., Wei,Y., Fu,T.,
            Xie,W., Wang,P., Hu,J., Zhu,Y., Huang,Z., Li,Q., Li,W., Guo,H. and
            Li,B.
  TITLE     SOX4 facilitates brown fat development and maintenance through
            EBF2-mediated thermogenic gene program in mice
  JOURNAL   Cell Death Differ 32 (3), 447-465 (2025)
   PUBMED   39402212
REFERENCE   2  (residues 1 to 2504)
  AUTHORS   Korobkina,E.D., Calejman,C.M., Haley,J.A., Kelly,M.E., Li,H.,
            Gaughan,M., Chen,Q., Pepper,H.L., Ahmad,H., Boucher,A.,
            Fluharty,S.M., Lin,T.Y., Lotun,A., Peura,J., Trefely,S.,
            Green,C.R., Vo,P., Semenkovich,C.F., Pitarresi,J.R., Spinelli,J.B.,
            Aydemir,O., Metallo,C.M., Lynes,M.D., Jang,C., Snyder,N.W.,
            Wellen,K.E. and Guertin,D.A.
  TITLE     Brown fat ATP-citrate lyase links carbohydrate availability to
            thermogenesis and guards against metabolic stress
  JOURNAL   Nat Metab 6 (11), 2187-2202 (2024)
   PUBMED   39402290
REFERENCE   3  (residues 1 to 2504)
  AUTHORS   Kang,J., Wu,J., Liu,Q., Jiang,H., Li,W., Li,Y., Li,X., Ni,C.,
            Wu,L., Liu,M., Liu,H., Deng,L., Lin,Z., Wu,X., Zhao,Y. and Ren,J.
  TITLE     FASN regulates STING palmitoylation via malonyl-CoA in macrophages
            to alleviate sepsis-induced liver injury
  JOURNAL   Biochim Biophys Acta Mol Basis Dis 1870 (7), 167299 (2024)
   PUBMED   38878833
  REMARK    GeneRIF: FASN regulates STING palmitoylation via malonyl-CoA in
            macrophages to alleviate sepsis-induced liver injury.
REFERENCE   4  (residues 1 to 2504)
  AUTHORS   Velez-delValle,C., Hernandez-Mosqueira,C.P., Castro-Rodriguez,L.I.,
            Vazquez-Sandoval,A., Marsch-Moreno,M. and Kuri-Harcuch,W.
  TITLE     Gene expression and characterization of clonally derived murine
            embryonic brown and brite adipocytes
  JOURNAL   FEBS Open Bio 14 (9), 1503-1525 (2024)
   PUBMED   38972757
REFERENCE   5  (residues 1 to 2504)
  AUTHORS   Drury,J., Geisen,M.E., Tessmann,J.W., Rychahou,P.G., Kelson,C.O.,
            He,D., Wang,C., Evers,B.M. and Zaytseva,Y.Y.
  TITLE     Overexpression of Fatty Acid Synthase Upregulates
            Glutamine-Fructose-6-Phosphate Transaminase 1 and O-Linked
            N-Acetylglucosamine Transferase to Increase O-GlcNAc Protein
            Glycosylation and Promote Colorectal Cancer Growth
  JOURNAL   Int J Mol Sci 25 (9), 4883 (2024)
   PUBMED   38732103
  REMARK    Publication Status: Online-Only
REFERENCE   6  (residues 1 to 2504)
  AUTHORS   Semenkovich,C.F., Coleman,T. and Fiedorek,F.T. Jr.
  TITLE     Human fatty acid synthase mRNA: tissue distribution, genetic
            mapping, and kinetics of decay after glucose deprivation
  JOURNAL   J Lipid Res 36 (7), 1507-1521 (1995)
   PUBMED   7595075
REFERENCE   7  (residues 1 to 2504)
  AUTHORS   Myohanen,S., Wahlfors,J., Alhonen,L. and Janne,J.
  TITLE     Nucleotide sequence of mouse spermidine synthase cDNA
  JOURNAL   DNA Seq 4 (5), 343-346 (1994)
   PUBMED   7803821
REFERENCE   8  (residues 1 to 2504)
  AUTHORS   Hsu,D.K., Donohue,P.J., Alberts,G.F. and Winkles,J.A.
  TITLE     Fibroblast growth factor-1 induces phosphofructokinase, fatty acid
            synthase and Ca(2+)-ATPase mRNA expression in NIH 3T3 cells
  JOURNAL   Biochem Biophys Res Commun 197 (3), 1483-1491 (1993)
   PUBMED   7506544
REFERENCE   9  (residues 1 to 2504)
  AUTHORS   Paulauskis,J.D. and Sul,H.S.
  TITLE     Structure of mouse fatty acid synthase mRNA. Identification of the
            two NADPH binding sites
  JOURNAL   Biochem Biophys Res Commun 158 (3), 690-695 (1989)
   PUBMED   2920037
REFERENCE   10 (residues 1 to 2504)
  AUTHORS   Paulauskis,J.D. and Sul,H.S.
  TITLE     Cloning and expression of mouse fatty acid synthase and other
            specific mRNAs. Developmental and hormonal regulation in 3T3-L1
            cells
  JOURNAL   J Biol Chem 263 (15), 7049-7054 (1988)
   PUBMED   2452820
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            CJ125823.1, AK147694.1, AF127033.1, AK080374.1 and AK078721.1.
            
            On Apr 21, 2006 this sequence version replaced NP_032014.2.
            
            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 :: AK147694.1, AK147214.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849375, SAMN00849381
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2504
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 84.56 cM"
     Protein         1..2504
                     /product="fatty acid synthase"
                     /EC_number="2.3.1.85"
                     /EC_number="2.3.1.38"
                     /EC_number="2.3.1.39"
                     /EC_number="2.3.1.41"
                     /EC_number="3.1.2.14"
                     /EC_number="4.2.1.59"
                     /EC_number="1.1.1.100"
                     /EC_number="1.3.1.39"
                     /note="type I Fatty Acid Synthase"
                     /calculated_mol_wt=272299
     Region          1..1353
                     /region_name="PksD"
                     /note="Acyl transferase domain in polyketide synthase
                     (PKS) enzymes [Secondary metabolites biosynthesis,
                     transport and catabolism]; COG3321"
                     /db_xref="CDD:442550"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine. /evidence=ECO:0000269|Ref.4;
                     propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Site            59
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            63
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            70
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            298
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          429..817
                     /region_name="Acyl and malonyl transferases"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Site            528
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            673
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            725
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            790
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          844..967
                     /region_name="N-terminal hotdog fold.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01363"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Region          982..1104
                     /region_name="C-terminal hotdog fold.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU01363"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Site            993
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            1071
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            1276
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          1311..>1518
                     /region_name="KR_1_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 1, complex (x) SDRs; cd08954"
                     /db_xref="CDD:187657"
     Region          1557..1847
                     /region_name="PKS_ER"
                     /note="Enoylreductase; smart00829"
                     /db_xref="CDD:214840"
     Site            order(1566,1647,1668,1670..1673,1692..1693,1697,
                     1716..1717,1740,1762,1787..1789,1836..1837,1839,1841)
                     /site_type="other"
                     /note="NAD(P) binding site [chemical binding]"
                     /db_xref="CDD:176179"
     Site            1577
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            1587
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          1628..1856
                     /region_name="Enoyl reductase"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Site            1697
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            1764
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Site            1840
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          1857..2111
                     /region_name="Beta-ketoacyl reductase"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Region          <1869..2105
                     /region_name="KR_1_FAS_SDR_x"
                     /note="beta-ketoacyl reductase (KR) domain of fatty acid
                     synthase (FAS), subgroup 1, complex (x) SDRs; cd08954"
                     /db_xref="CDD:187657"
     Site            order(1886..1887,1889,1909..1912,1937..1940,1964..1966,
                     1987..1988,2012..2013,2027,2054..2055)
                     /site_type="other"
                     /note="putative NADP binding site [chemical binding]"
                     /db_xref="CDD:187657"
     Site            order(1988,2014,2027,2031)
                     /site_type="active"
                     /db_xref="CDD:187657"
     Site            1988
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          2118..>2173
                     /region_name="PKS_PP"
                     /note="Phosphopantetheine attachment site; smart00823"
                     /db_xref="CDD:214834"
     Site            2150
                     /site_type="phosphorylation"
                     /note="Phosphoserine, alternate.
                     /evidence=ECO:0000250|UniProtKB:P12785; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          2181..2205
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Site            2190
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          2201..2504
                     /region_name="Thioesterase"
                     /note="propagated from UniProtKB/Swiss-Prot (P19096.2)"
     Site            2229
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:P49327; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     Region          2235..2494
                     /region_name="Thioesterase"
                     /note="Thioesterase domain; pfam00975"
                     /db_xref="CDD:395776"
     Site            2384
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23806337; propagated from
                     UniProtKB/Swiss-Prot (P19096.2)"
     CDS             1..2504
                     /gene="Fasn"
                     /gene_synonym="A630082H08Rik; FAS"
                     /coded_by="NM_007988.3:528..8042"
                     /db_xref="CCDS:CCDS25759.1"
                     /db_xref="GeneID:14104"
                     /db_xref="MGI:MGI:95485"
ORIGIN      
        1 meevviagms gklpesenlq efwanliggv dmvtdddrrw kaglyglpkr sgklkdlskf
       61 dasffgvhpk qahtmdpqlr lllevsyeai vdgginpasl rgtntgvwvg vsgseaseal
      121 srdpetllgy smvgcqramm anrlsfffdf kgpsialdta csssllalqn ayqairsgec
      181 paalvgginl llkpntsvqf mklgmlspdg tcrsfddsgs gycrseavva vlltkkslar
      241 rvyatilnag tntdgskeqg vtfpsgevqe qlicslyqpa glapesleyi eahgtgtkvg
      301 dpqelngitr slcafrqapl ligstksnmg hpepasglaa ltkvllsleh gvwapnlhfh
      361 npnpeipall dgrlqvvdrp lpvrggnvgi nsfgfggsnv hvilqpntrq apaptahaal
      421 phllhasgrt leavqdlleq grqhsqdlaf vsmlndiaat ptaampfrgy tvlgvegrvq
      481 evqqvstnkr plwficsgmg tqwrgmglsl mrldsfresi lrsdeavkpl gvkvsdllls
      541 tdertfddiv hafvsltaiq ialidlltsv glkpdgiigh slgevacgya dgclsqreav
      601 laaywrgqci kdahlppgsm aavglsweec kqrcpagvvp achnsedtvt isgpqaavne
      661 fveqlkqegv fakevrtggl afhsyfmegi aptllqalkk vireprprsa rwlstsipea
      721 qwqsslarts saeynvnnlv spvlfqealw hipehavvle iaphallqav lkrgvkssct
      781 iiplmkrdhk dnleffltnl gkvhltginv npnalfppve fpaprgtpli sphikwdhsq
      841 twdvpvaedf pngsssssat vysidaspes pdhylvdhci dgrvifpgtg ylclvwktla
      901 rslglsleet pvvfenvsfh qatilpktgt valevrllea shafevsdtg nlivsgkvyl
      961 wedpnsklfd hpevptppes asvsrltqge vykelrlrgy dygpqfqgic eatlegeqgk
     1021 llwkdnwvtf mdtmlqvsil gssqqslqlp trvtaiyidp athrqkvyrl kedtqvadvt
     1081 tsrclgitvs ggihisrlqt tatsrrqqeq lvptlekfvf tphmeaecls estalqkelq
     1141 lckglaralq tkatqqglka amlgqedppq hglprllaaa cqlqlngnlq lelgealaqe
     1201 rlllpedpli sgllnsqalk acvdtalenl stlkmkvaev lageghlysr ipallntqpm
     1261 lqleytatdr hpqalkdvqt klqqhdvaqg qwnpsdpaps slgaldllvc ncalatlgdp
     1321 alaldnmvaa lkeggfllvh tvlkghalge tlaclpsevq papsllsqee weslfsrkal
     1381 hlvglkrsfy gtalflcrra ipqekpifls vedtsfqwvd slkstlatss sqpvwltamd
     1441 cptsgvvglv nclrkepggh rircillsnl sntshapkld pgspelqqvl khdlvmnvyr
     1501 dgawgafrhf qleqdkpkeq tahafvnvlt rgdlasirwv ssplkhtqps ssgaqlctvy
     1561 yaslnfrdim latgklspda ipgkwasrdc mlgmefsgrd rcgrrvmglv paeglatsvl
     1621 lssdflwdvp sswtleeaas vpvvyttayy slvvrgriqr getvlihsgs ggvgqaaisi
     1681 alslgcrvft tvgsaekray lqarfpqldd tsfansrdts feqhvllhtg gkgvdlvlns
     1741 laeeklqasv rclaqhgrfl eigkfdlsnn hplgmaiflk nvtfhgilld alfeeandsw
     1801 revaallkag irdgvvkplk ctvfpkaqve dafrymaqgk higkvlvqvr eeepeavlpg
     1861 aqptlisais ktfcpahksy iitgglggfg lelarwlvlr gaqrlvltsr sgirtgyqak
     1921 hirewrrqgi qvlvstsnvs slegaralia eatklgpvgg vfnlamvlrd amlenqtpel
     1981 fqdvnkpkyn gtlnldratr eacpeldyfv afssvscgrg nagqtnygfa nstmericeq
     2041 rrhdglpgla vqwgaigdvg ivleamgtnd tviggtlpqr isscmevldl flnqphavls
     2101 sfvlaekkav ahgdgdtqrd lvkavahilg irdlaginld stladlglds lmgvevrqil
     2161 erehdlvlpm revrqltlrk lqemssktds atdttapksr sdtslkqnql nlstllvnpe
     2221 gptltqlnsv qsserplflv hpiegsttvf hslaaklsvp tyglqctqaa pldsipnlaa
     2281 yyidcikqvq pegpyriagy sfgacvafem csqlqaqqgp apthnnlflf dgshtyvlay
     2341 tqsyrakmtp gceaeaeaea lcffikqfld vehskvleal lplksledrv aasvdlitks
     2401 hhsldrrels faavsfyhkl raadqykpka kyhgnvtllr aktggtyged lgadynlsqv
     2461 cdgkvsvhii egdhrtlleg sglesiinii hsslaeprvs vreg
//
