ID   FAS_BOVIN               Reviewed;        2513 AA.
AC   Q71SP7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85 {ECO:0000269|PubMed:16772574};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE              EC=2.3.1.38 {ECO:0000305|PubMed:16772574};
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE              EC=2.3.1.39 {ECO:0000305|PubMed:16772574};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE              EC=2.3.1.41 {ECO:0000305|PubMed:16772574};
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE              EC=1.1.1.100 {ECO:0000305|PubMed:16772574};
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE              EC=4.2.1.59 {ECO:0000305|PubMed:16772574};
DE   Includes:
DE     RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE              EC=1.3.1.39 {ECO:0000305|PubMed:16772574};
DE   Includes:
DE     RecName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE              EC=3.1.2.14 {ECO:0000305|PubMed:16772574};
GN   Name=FASN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA   Roy R., Eggen A., Rodellar C.;
RT   "Cloning, genomic organization and expression analysis of bovine FASN
RT   gene.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX   PubMed=16772574; DOI=10.3168/jds.s0022-0302(06)72331-1;
RA   Wright T.C., Cant J.P., Brenna J.T., McBride B.W.;
RT   "Acetyl CoA carboxylase shares control of fatty acid synthesis with fatty
RT   acid synthase in bovine mammary homogenate.";
RL   J. Dairy Sci. 89:2552-2558(2006).
CC   -!- FUNCTION: Fatty acid synthetase is a multifunctional enzyme that
CC       catalyzes the de novo biosynthesis of long-chain saturated fatty acids
CC       starting from acetyl-CoA and malonyl-CoA in the presence of NADPH. This
CC       multifunctional protein contains 7 catalytic activities and a site for
CC       the binding of the prosthetic group 4'-phosphopantetheine of the acyl
CC       carrier protein ([ACP]) domain. {ECO:0000269|PubMed:16772574}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC         fatty acid + n CO2 + (n+1) CoA + 2n NADP(+); Xref=Rhea:RHEA:14993,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=2.3.1.85;
CC         Evidence={ECO:0000269|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14994;
CC         Evidence={ECO:0000269|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + holo-[ACP] = acetyl-[ACP] + CoA;
CC         Xref=Rhea:RHEA:41788, Rhea:RHEA-COMP:9621, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446; EC=2.3.1.38;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41789;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=holo-[ACP] + malonyl-CoA = CoA + malonyl-[ACP];
CC         Xref=Rhea:RHEA:41792, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57384, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449; EC=2.3.1.39;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41793;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acyl-[ACP] + H(+) + malonyl-[ACP] = a 3-oxoacyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:22836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9916, Rhea:RHEA-COMP:14125,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78776, ChEBI:CHEBI:138651;
CC         EC=2.3.1.41; Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22837;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + H(+)
CC         + NADPH; Xref=Rhea:RHEA:17397, Rhea:RHEA-COMP:9916, Rhea:RHEA-
CC         COMP:9945, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78776, ChEBI:CHEBI:78827; EC=1.1.1.100;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17399;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:13097, Rhea:RHEA-COMP:9925, Rhea:RHEA-COMP:9945,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78784, ChEBI:CHEBI:78827; EC=4.2.1.59;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13098;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-saturated acyl-[ACP] + NADP(+) = a (2E)-enoyl-[ACP] +
CC         H(+) + NADPH; Xref=Rhea:RHEA:22564, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC         COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.39;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22566;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP];
CC         Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78483; EC=3.1.2.14;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41800, Rhea:RHEA-COMP:9621,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78446, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41801;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxobutanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxybutanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41804, Rhea:RHEA-COMP:9625,
CC         Rhea:RHEA-COMP:9626, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78450, ChEBI:CHEBI:78451;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41805;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxybutanoyl-[ACP] = (2E)-butenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41808, Rhea:RHEA-COMP:9626, Rhea:RHEA-COMP:9627,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78451, ChEBI:CHEBI:78453;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41809;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-butenoyl-[ACP] + H(+) + NADPH = butanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41812, Rhea:RHEA-COMP:9627, Rhea:RHEA-COMP:9628,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78453, ChEBI:CHEBI:78454;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41813;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41820, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9628, Rhea:RHEA-COMP:9629, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78454, ChEBI:CHEBI:78456;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41821;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyhexanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41824, Rhea:RHEA-COMP:9629,
CC         Rhea:RHEA-COMP:9630, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78456, ChEBI:CHEBI:78457;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41825;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexanoyl-[ACP] = (2E)-hexenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41828, Rhea:RHEA-COMP:9630, Rhea:RHEA-COMP:9631,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78457, ChEBI:CHEBI:78458;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41829;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexenoyl-[ACP] + H(+) + NADPH = hexanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41832, Rhea:RHEA-COMP:9631, Rhea:RHEA-COMP:9632,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78458, ChEBI:CHEBI:78459;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41833;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexanoyl-[ACP] + malonyl-[ACP] = 3-oxooctanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41836, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9632, Rhea:RHEA-COMP:9633, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78459, ChEBI:CHEBI:78460;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41837;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxyoctanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41840, Rhea:RHEA-COMP:9633,
CC         Rhea:RHEA-COMP:9634, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78460, ChEBI:CHEBI:78461;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41841;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctanoyl-[ACP] = (2E)-octenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41844, Rhea:RHEA-COMP:9634, Rhea:RHEA-COMP:9635,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78461, ChEBI:CHEBI:78462;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41845;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octenoyl-[ACP] + H(+) + NADPH = NADP(+) + octanoyl-[ACP];
CC         Xref=Rhea:RHEA:41848, Rhea:RHEA-COMP:9635, Rhea:RHEA-COMP:9636,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78462, ChEBI:CHEBI:78463;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41849;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + octanoyl-[ACP] = 3-oxodecanoyl-[ACP] +
CC         CO2 + holo-[ACP]; Xref=Rhea:RHEA:41852, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9637, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78463, ChEBI:CHEBI:78464;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41853;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxodecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41856, Rhea:RHEA-COMP:9637,
CC         Rhea:RHEA-COMP:9638, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78464, ChEBI:CHEBI:78466;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41857;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydecanoyl-[ACP] = (2E)-decenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41860, Rhea:RHEA-COMP:9638, Rhea:RHEA-COMP:9639,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78466, ChEBI:CHEBI:78467;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41861;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-decenoyl-[ACP] + H(+) + NADPH = decanoyl-[ACP] + NADP(+);
CC         Xref=Rhea:RHEA:41864, Rhea:RHEA-COMP:9639, Rhea:RHEA-COMP:9640,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78467, ChEBI:CHEBI:78468;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41865;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=decanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxododecanoyl-[ACP]
CC         + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41868, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9641, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78468, ChEBI:CHEBI:78469;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41869;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxododecanoyl-[ACP] + H(+) + NADPH = (3R)-hydroxydodecanoyl-
CC         [ACP] + NADP(+); Xref=Rhea:RHEA:41872, Rhea:RHEA-COMP:9641,
CC         Rhea:RHEA-COMP:9642, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78469, ChEBI:CHEBI:78470;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41873;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxydodecanoyl-[ACP] = (2E)-dodecenoyl-[ACP] + H2O;
CC         Xref=Rhea:RHEA:41876, Rhea:RHEA-COMP:9642, Rhea:RHEA-COMP:9643,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78470, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41877;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-dodecenoyl-[ACP] + H(+) + NADPH = dodecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41880, Rhea:RHEA-COMP:9643, Rhea:RHEA-
CC         COMP:9644, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78472;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41881;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-[ACP] + H(+) + malonyl-[ACP] = 3-oxotetradecanoyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41884, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:65264, ChEBI:CHEBI:78449, ChEBI:CHEBI:78473;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41885;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxotetradecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxytetradecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41888,
CC         Rhea:RHEA-COMP:9645, Rhea:RHEA-COMP:9646, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78473,
CC         ChEBI:CHEBI:78474; Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41889;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxytetradecanoyl-[ACP] = (2E)-tetradecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41892, Rhea:RHEA-COMP:9646, Rhea:RHEA-COMP:9647,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78474, ChEBI:CHEBI:78475;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41893;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-tetradecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC         tetradecanoyl-[ACP]; Xref=Rhea:RHEA:41896, Rhea:RHEA-COMP:9647,
CC         Rhea:RHEA-COMP:9648, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78475, ChEBI:CHEBI:78477;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41897;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + malonyl-[ACP] + tetradecanoyl-[ACP] = 3-
CC         oxohexadecanoyl-[ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41900,
CC         Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9648, Rhea:RHEA-COMP:9649,
CC         Rhea:RHEA-COMP:9685, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78449, ChEBI:CHEBI:78477,
CC         ChEBI:CHEBI:78478; Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41901;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxohexadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxyhexadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41904, Rhea:RHEA-
CC         COMP:9649, Rhea:RHEA-COMP:9650, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78478, ChEBI:CHEBI:78480;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41905;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyhexadecanoyl-[ACP] = (2E)-hexadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41908, Rhea:RHEA-COMP:9650, Rhea:RHEA-COMP:9651,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78480, ChEBI:CHEBI:78481;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41909;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-hexadecenoyl-[ACP] + H(+) + NADPH = hexadecanoyl-[ACP] +
CC         NADP(+); Xref=Rhea:RHEA:41912, Rhea:RHEA-COMP:9651, Rhea:RHEA-
CC         COMP:9652, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:78481, ChEBI:CHEBI:78483;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41913;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hexadecanoyl-[ACP] + malonyl-[ACP] = 3-oxooctadecanoyl-
CC         [ACP] + CO2 + holo-[ACP]; Xref=Rhea:RHEA:41916, Rhea:RHEA-COMP:9623,
CC         Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9653, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:64479,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78483, ChEBI:CHEBI:78487;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41917;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-oxooctadecanoyl-[ACP] + H(+) + NADPH = (3R)-
CC         hydroxyoctadecanoyl-[ACP] + NADP(+); Xref=Rhea:RHEA:41920, Rhea:RHEA-
CC         COMP:9653, Rhea:RHEA-COMP:9654, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78487, ChEBI:CHEBI:78488;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41921;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3R)-hydroxyoctadecanoyl-[ACP] = (2E)-octadecenoyl-[ACP] +
CC         H2O; Xref=Rhea:RHEA:41924, Rhea:RHEA-COMP:9654, Rhea:RHEA-COMP:9655,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:78488, ChEBI:CHEBI:78489;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41925;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-octadecenoyl-[ACP] + H(+) + NADPH = NADP(+) +
CC         octadecanoyl-[ACP]; Xref=Rhea:RHEA:41928, Rhea:RHEA-COMP:9655,
CC         Rhea:RHEA-COMP:9656, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:78489, ChEBI:CHEBI:78495;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41929;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] +
CC         tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-
CC         COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78477; EC=3.1.2.14;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC         Evidence={ECO:0000305|PubMed:16772574};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + octadecanoyl-[ACP] = H(+) + holo-[ACP] + octadecanoate;
CC         Xref=Rhea:RHEA:63204, Rhea:RHEA-COMP:9656, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78495;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63205;
CC         Evidence={ECO:0000250|UniProtKB:P49327};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000269|PubMed:16772574}.
CC   -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion (By
CC       similarity). Interacts with CEACAM1; this interaction is insulin and
CC       phosphorylation-dependent; reduces fatty-acid synthase activity (By
CC       similarity). {ECO:0000250|UniProtKB:P12785,
CC       ECO:0000250|UniProtKB:P49327}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000250}.
CC   -!- PTM: S-nitrosylation of Fatty acid synthase at cysteine residues Cys-
CC       1473 or Cys-2093 is important for the enzyme dimerization. In
CC       adipocytes, S-nitrosylation of Fatty acid synthase occurs under
CC       physiological conditions and gradually increases during adipogenesis.
CC       {ECO:0000250|UniProtKB:P49327}.
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DR   EMBL; AF285607; AAR19788.1; -; Genomic_DNA.
DR   EMBL; AY343889; AAR17600.1; -; mRNA.
DR   RefSeq; NP_001012687.1; NM_001012669.1.
DR   AlphaFoldDB; Q71SP7; -.
DR   SMR; Q71SP7; -.
DR   STRING; 9913.ENSBTAP00000021260; -.
DR   ESTHER; bovin-fas; Thioesterase.
DR   iPTMnet; Q71SP7; -.
DR   SwissPalm; Q71SP7; -.
DR   PaxDb; 9913-ENSBTAP00000021260; -.
DR   PeptideAtlas; Q71SP7; -.
DR   GeneID; 281152; -.
DR   KEGG; bta:281152; -.
DR   CTD; 2194; -.
DR   eggNOG; KOG1202; Eukaryota.
DR   InParanoid; Q71SP7; -.
DR   OrthoDB; 3378513at2759; -.
DR   BRENDA; 2.3.1.85; 908.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008693; F:(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0047451; F:(3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0047450; F:(3R)-hydroxybutanoyl-[acyl-carrier-protein] hydratase activity; IEA:RHEA.
DR   GO; GO:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004317; F:(3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:RHEA.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR   GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA.
DR   GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd05195; enoyl_red; 1.
DR   CDD; cd08954; KR_1_FAS_SDR_x; 2.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR049391; FAS_pseudo-KR.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF7; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF13602; ADH_zinc_N_2; 1.
DR   Pfam; PF21149; FAS_pseudo-KR; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
DR   PROSITE; PS52019; PKS_MFAS_DH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Hydrolase; Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Lyase;
KW   Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine;
KW   Phosphoprotein; Pyridoxal phosphate; Reference proteome; S-nitrosylation;
KW   Transferase; Ubl conjugation.
FT   CHAIN           1..2513
FT                   /note="Fatty acid synthase"
FT                   /id="PRO_0000180274"
FT   DOMAIN          1..406
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   DOMAIN          845..1107
FT                   /note="PKS/mFAS DH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   DOMAIN          2123..2200
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   REGION          429..817
FT                   /note="Acyl and malonyl transferases"
FT   REGION          845..976
FT                   /note="N-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          986..1107
FT                   /note="C-terminal hotdog fold"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   REGION          1637..1865
FT                   /note="Enoyl reductase"
FT   REGION          1866..2119
FT                   /note="Beta-ketoacyl reductase"
FT   REGION          2209..2513
FT                   /note="Thioesterase"
FT   ACT_SITE        161
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        293
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        331
FT                   /note="For beta-ketoacyl synthase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01348"
FT   ACT_SITE        581
FT                   /note="For malonyltransferase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        878
FT                   /note="Proton acceptor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        1035
FT                   /note="Proton donor; for dehydratase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01363"
FT   ACT_SITE        2310
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   ACT_SITE        2483
FT                   /note="For thioesterase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   BINDING         647..648
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   BINDING         671
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   BINDING         773
FT                   /ligand="an acyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:58342"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   BINDING         1673..1690
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="1"
FT                   /ligand_note="for enoyl reductase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         1888..1903
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /ligand_label="2"
FT                   /ligand_note="for ketoreductase activity"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         63
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         70
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         207
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         298
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         528
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         673
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         725
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   MOD_RES         996
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   MOD_RES         1414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         1473
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         1596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P19096"
FT   MOD_RES         1706
FT                   /note="N6-(pyridoxal phosphate)lysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1706
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         1773
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         1849
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         1997
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         2093
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         2158
FT                   /note="O-(pantetheine 4'-phosphoryl)serine; alternate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         2158
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P12785"
FT   MOD_RES         2206
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         2217
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   MOD_RES         2238
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
FT   CROSSLNK        2451
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P49327"
SQ   SEQUENCE   2513 AA;  274554 MW;  D75B09DB855DFDAB CRC64;
     MEEVVITGMS GKLPESENLE EFWANLIGGV DMVTDDDRRW KAGLYGLPRR SGKLKDLSRF
     DASFFGVHPK QAHNMDPQLR LLLEVTYEAI VDAGINPASI RGTNTGVWVG VSGSEASEAL
     SRDPETLVGY SMVGCQRAML ANRLSFFFDF KGPSITLDTA CSSSLLALQR AYQAIQRGEC
     AMAIVGGVNI RLKPNTSVQF MKLGMLSPEG TCKFFDASGN GYCRAKAVMA ILLTKKSLAR
     RVYATILNAG TNTDGCKEKG VTFPSGEAQE QLISSLYKPA GLDPETLEYV EAHGTGTKVG
     DPQELNGIVQ ALCGTRQSPL RIGSTKSNMG HPEPASGLAA LAKVLLSLEH GLWAPNLHFH
     NPNPKIPALQ DGRLQVVDRP LPVLGGNVGI NSFGFGGSNV HVILQPNSQP LPPPAPHAAL
     PRLLRASGRT LEGVQGLLEL GLQHSQNLAF VSMLNDIATP SPAAMPFRGY AVLGSQGGSQ
     KVQQVLAGKR PLWFICSGMG TQWRGMGLSL MRLSRFRDSI LRSDEAVKPL GLQVSQLLLS
     TDEAIFDDMV ISFVSLTAIQ IALIDLLTSM GLQPDGIIGH SLGEVACGYA DGCISQEEAI
     LSAYWRGQCI KEANIPPGAM AAVGLTWEEC KQRCPPGIVP ACHNCIDTVT ISGPQASMLE
     FVQQLKQEGV FAKEVRTGGM AFHSYFMDAI APMLLQQLKK VIREPQPRSP RWLSTSIPET
     QWQESLARTF SAEYNVNNLV SPVLFQEALW RVPEDAVVLE IAPHALLQAV LKRGLKSSCT
     IIPLMKKDHR DNLEFFLSNV GQLYLTGIDV NPNGLFPPVE FPAPRGTPLI SPHIKWDHSQ
     TWDVPTAEDF PSGSSSSSAT IYKIDINPES PDHYLVDHCI DGRIIFPGTG YLCLVWKTLA
     RALDQNMEHT PVVFEDVTLH QAVILPKTGI VLLKVRLLEA SCTFEVSENG NLIASGKVYQ
     WEDPNPKLFD NRYGPDPATP VDPTTAIHLS RGDVYKELQL QGFNYGPYFQ GILEASSEGN
     TGQLLWKDNW VTFMDTMLQM SILAPSKRSL RLPTRITAIY IHPATHQQKL YTLQDKTQVA
     DVVINRCLDT TVAGGIYISR IHTSVAPRHQ QEQLVPILEK FCFTPHVETG CLAGNLALQE
     ELQLCVGLAQ ALQTRVAQQG IKMVVPGLDG AQAPQEAPQQ GLPRLLATAC QLQLNGNLQM
     EMGQILAQER ALLCDDPLLS GLLNSPALKA CVTLALENMT SLKMKVVLAG DGQLYSRIPT
     LLNTQPLLEL DYTATDRHPQ ALEAAQAKLQ QLDITQGQWD PSDPAPSNLG GANLVVCNYA
     LASLGDPATA VGNMVAALKE GGFLLLHTLL RGHPLGETVT FLTCPEPQQG QRHLLSQDEW
     ERLFAGASLH LVALKKSFYG SVLFLCRRLA PLDSPIFLPV EDTSFQWVDS LKNILADSSS
     RAVWLMAVGC TTSGVVGLVN CLRKEPDGHR IRCVLVSNLN STSPIPETDP KSLELQKVLQ
     SDLVMNVYRD GAWGAFRHFP LEQDKPEEQT EHAFINVLTR GDLSSIRWVC SPLRHSQPTA
     PGFQLCTIYY ASLNFKRNHA GHGQAVPRRH PRNWASRNCL LGMEFSGRDA SGKRVMGLVP
     AEGLATSTLV PQSFLWDVPS NWTLEEAASV PVVYSTAYYA LMVRGRMQPG ETVLIHSGSG
     GVGQAAIAIA LSLGCRVFPL VGSAEKRAYL QSRFPQLNET SFANSRDTSF EQHVLWHTAG
     KGADLVLNSL AEEKLQASVR CLAQHGRFLE IGKFDLSKNH PLGMAIFLKN VTFHGILLDS
     LFEENNTMWQ EVSTLLKAGI RKGVVQPLKR TVFPRTQAED AFRYMAQGKH IGKVVIQVRE
     EEQEAVLHGT KPTQMVALCK TFCPAHKSYI ITGGLGGFGL ELAHWLVERG AQKLVLTSRS
     GIRTGYQARQ VHEWRRQGVQ VLVSTSDVST LDGTRSLITE AAQLGPVGGI FNLAVVLRDA
     MLDNQTPEFF QDVNKPKYNG TLNLDRVTRE ACPELDYFEV FSSVSCGRGN AGQTNYGFAN
     STMERICEKR RHDGLPGLAV QWGAIADVGL LMELKGTKDK AIGGTLPQRI TSCMEVLDLF
     LNQPHPVLSS FVLAEKATSR GPSGSHQDLV KAVTHILGIR DLATVNLDSS LSDLGLDSLM
     GVEVRQMLER EHNLLLSMRE IRQLTIHKLQ EISAQAGTAD ELTDSTPKFG SPAQSHTQLN
     LSTLLVNPEG PTLTRLNSVQ SSERPLFLVH PIEGSTTVFH SLATKLSIPT YGLQCTGAAP
     LDSIQSLATY YIECIRQVQP EGNYRIAGYS YGACVAFEMC SQLQAQQNAG PTNNSLFLFD
     GSHTFVMAYT QSYRAKLNPG CEAEAEAEAM CFFMQQFTEA EHSRVLEALL PLGDLEARVA
     ATVELIVQSH AGLDRHALSF AARSFYHKLR AAEEYTPRAT YHGNVTLLRA KMGSAYQEGL
     GADYNLSQVC DGKVSVHIIE GDHRTLLEGS GLESILSIIH SSLAEPRVSV REG
//