FAS_BOVIN
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 03-AUG-2022, entry version 126.
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 PaxDb; Q71SP7; -.
DR PeptideAtlas; Q71SP7; -.
DR PRIDE; Q71SP7; -.
DR GeneID; 281152; -.
DR KEGG; bta:281152; -.
DR CTD; 2194; -.
DR eggNOG; KOG1202; Eukaryota.
DR InParanoid; Q71SP7; -.
DR OrthoDB; 19161at2759; -.
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:0008659; F:(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0008693; F:3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0047451; F:3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:UniProtKB-EC.
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:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.366.10; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 2.
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; 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; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
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 Pfam; PF00698; Acyl_transf_1; 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; PF00550; PP-binding; 1.
DR Pfam; PF14765; PS-DH; 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; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 2.
DR SUPFAM; SSF52151; SSF52151; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 1.
DR SUPFAM; SSF55048; SSF55048; 1.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 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 2123..2200
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 1..414
FT /note="Beta-ketoacyl synthase"
FT REGION 429..817
FT /note="Acyl and malonyl transferases"
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:PRU10022"
FT ACT_SITE 581
FT /note="For malonyltransferase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 878
FT /note="For beta-hydroxyacyl dehydratase activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
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
