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Database: UniProt
Entry: P12785
LinkDB: P12785
Original site: P12785 
ID   FAS_RAT                 Reviewed;        2505 AA.
AC   P12785; O09187; O09190; Q63577; Q64717;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   29-OCT-2014, entry version 148.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85;
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE              EC=2.3.1.38;
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE              EC=2.3.1.39;
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE              EC=2.3.1.41;
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE              EC=1.1.1.100;
DE   Includes:
DE     RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase;
DE              EC=4.2.1.59;
DE   Includes:
DE     RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE              EC=1.3.1.39;
DE   Includes:
DE     RecName: Full=Oleoyl-[acyl-carrier-protein] hydrolase;
DE              EC=3.1.2.14;
GN   Name=Fasn;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2717611; DOI=10.1073/pnas.86.9.3114;
RA   Amy C.M., Witkowski A., Naggert J., Williams B., Randhawa Z.,
RA   Smith S.;
RT   "Molecular cloning and sequencing of cDNAs encoding the entire rat
RT   fatty acid synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3114-3118(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=1339331;
RA   Beck K.F., Schreglmann R., Stathopulos I., Klein H., Hoch J.,
RA   Schweizer M.;
RT   "The fatty acid synthase (FAS) gene and its promoter in Rattus
RT   norvegicus.";
RL   DNA Seq. 2:359-386(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1736293; DOI=10.1073/pnas.89.3.1105;
RA   Amy C.M., Williams-Ahlf B., Naggert J., Smith S.;
RT   "Intron-exon organization of the gene for the multifunctional animal
RT   fatty acid synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1105-1108(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 75-2505.
RC   STRAIN=Sprague-Dawley; TISSUE=Mammary gland;
RX   PubMed=2915923; DOI=10.1093/nar/17.2.567;
RA   Schweizer M., Takabeyashi K., Beck K.F., Schreglmann R.;
RT   "Rat mammary gland fatty acid synthase: localization of the
RT   constituent domains and two functional polyadenylation/termination
RT   signals in the cDNA.";
RL   Nucleic Acids Res. 17:567-586(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1921-2324.
RC   TISSUE=Mammary gland;
RX   PubMed=3109907; DOI=10.1111/j.1432-1033.1987.tb11482.x;
RA   Witlowski A., Naggert J., Mikkelsen J., Smith S.;
RT   "Molecular cloning and sequencing of a cDNA encoding the acyl carrier
RT   protein and its flanking domains in the mammalian fatty acid
RT   synthetase.";
RL   Eur. J. Biochem. 165:601-606(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2085-2505.
RC   TISSUE=Mammary gland;
RX   PubMed=2891707;
RA   Naggert J., Witkowski A., Mikkelsen J., Smith S.;
RT   "Molecular cloning and sequencing of a cDNA encoding the thioesterase
RT   domain of the rat fatty acid synthetase.";
RL   J. Biol. Chem. 263:1146-1150(1988).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 2377-2413, AND INDUCTION.
RX   PubMed=2313386;
RA   Clarke S.D., Armstrong M.K., Jump D.B.;
RT   "Nutritional control of rat liver fatty acid synthase and S14 mRNA
RT   abundance.";
RL   J. Nutr. 120:218-224(1990).
RN   [8]
RP   STRUCTURE BY NMR OF 2114-2202.
RX   PubMed=12926246; DOI=10.1039/b208941f;
RA   Reed M.A.C., Schweizer M., Szafranska A.E., Arthur C., Nicholson T.P.,
RA   Cox R.J., Crosby J., Crump M.P., Simpson T.J.;
RT   "The type I rat fatty acid synthase ACP shows structural homology and
RT   analogous biochemical properties to type II ACPs.";
RL   Org. Biomol. Chem. 1:463-471(2003).
CC   -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-
CC       chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This
CC       multifunctional protein has 7 catalytic activities and an acyl
CC       carrier protein.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = a
CC       long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA +
CC       acetyl-[acyl-carrier-protein].
CC   -!- CATALYTIC ACTIVITY: Malonyl-CoA + an [acyl-carrier-protein] = CoA
CC       + a malonyl-[acyl-carrier-protein].
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
CC       carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
CC       [acyl-carrier-protein].
CC   -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
CC       NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
CC   -!- CATALYTIC ACTIVITY: A (3R)-3-hydroxyacyl-[acyl-carrier protein] =
CC       a trans-2-enoyl-[acyl-carrier protein] + H(2)O.
CC   -!- CATALYTIC ACTIVITY: An acyl-[acyl-carrier protein] + NADP(+) = a
CC       trans-2,3-dehydroacyl-[acyl-carrier protein] + NADPH.
CC   -!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-
CC       carrier-protein] + oleate.
CC   -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion.
CC   -!- INTERACTION:
CC       Self; NbExp=8; IntAct=EBI-493558, EBI-493558;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated in livers of rats fed on a high
CC       carbohydrate diet. {ECO:0000269|PubMed:2313386}.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00258}.
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DR   EMBL; M76767; AAA57219.1; -; mRNA.
DR   EMBL; X62888; CAA44679.1; -; mRNA.
DR   EMBL; X62889; CAA44680.1; -; Genomic_DNA.
DR   EMBL; M84761; AAA41145.1; -; Genomic_DNA.
DR   EMBL; X13415; CAA31780.1; -; mRNA.
DR   EMBL; X13527; CAA31882.1; -; mRNA.
DR   EMBL; J03514; AAA41144.1; -; mRNA.
DR   PIR; A30313; XYRTFA.
DR   RefSeq; NP_059028.1; NM_017332.1.
DR   UniGene; Rn.9486; -.
DR   PDB; 2PNG; NMR; -; A=2114-2202.
DR   PDBsum; 2PNG; -.
DR   ProteinModelPortal; P12785; -.
DR   SMR; P12785; 423-819, 2114-2202, 2216-2501.
DR   BioGrid; 248415; 2.
DR   DIP; DIP-33893N; -.
DR   MINT; MINT-4564064; -.
DR   BindingDB; P12785; -.
DR   ChEMBL; CHEMBL3783; -.
DR   PRIDE; P12785; -.
DR   Ensembl; ENSRNOT00000073321; ENSRNOP00000064445; ENSRNOG00000045636.
DR   GeneID; 50671; -.
DR   KEGG; rno:50671; -.
DR   CTD; 2194; -.
DR   RGD; 620665; Fasn.
DR   GeneTree; ENSGT00530000063309; -.
DR   HOVERGEN; HBG005640; -.
DR   InParanoid; P12785; -.
DR   KO; K00665; -.
DR   OMA; ATGQMAI; -.
DR   OrthoDB; EOG71K623; -.
DR   PhylomeDB; P12785; -.
DR   Reactome; REACT_198613; Activation of gene expression by SREBF (SREBP).
DR   SABIO-RK; P12785; -.
DR   EvolutionaryTrace; P12785; -.
DR   NextBio; 610498; -.
DR   PRO; PR:P12785; -.
DR   Genevestigator; P12785; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl.
DR   GO; GO:0042587; C:glycogen granule; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:InterPro.
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:0008144; F:drug binding; IDA:RGD.
DR   GO; GO:0047117; F:enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:InterPro.
DR   GO; GO:0004312; F:fatty acid synthase activity; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0070402; F:NADPH binding; IDA:RGD.
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:0044822; F:poly(A) RNA binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:RGD.
DR   GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IMP:RGD.
DR   GO; GO:0008610; P:lipid biosynthetic process; TAS:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 1.10.1470.20; -; 1.
DR   Gene3D; 3.40.366.10; -; 2.
DR   Gene3D; 3.40.47.10; -; 2.
DR   Gene3D; 3.40.50.150; -; 1.
DR   Gene3D; 3.40.50.1820; -; 2.
DR   Gene3D; 3.40.50.720; -; 2.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR023102; Fatty_acid_synthase_dom_2.
DR   InterPro; IPR011032; GroES-like.
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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020842; PKS/FAS_KR.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR029063; SAM-dependent_MTases-like.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00107; ADH_zinc_N; 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; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF52151; SSF52151; 2.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   SUPFAM; SSF55048; SSF55048; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Multifunctional enzyme;
KW   NAD; NADP; Oxidoreductase; Phosphopantetheine; Phosphoprotein;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN         1   2505       Fatty acid synthase.
FT                                /FTId=PRO_0000180279.
FT   DOMAIN     2118   2174       Acyl carrier. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00258}.
FT   NP_BIND    1665   1682       NADP (ER).
FT   NP_BIND    1765   1780       NADP (KR).
FT   REGION        1    413       Beta-ketoacyl synthase.
FT   REGION      429    817       Acyl and malonyl transferases.
FT   REGION     1629   1857       Enoyl reductase.
FT   REGION     1858   2113       Beta-ketoacyl reductase.
FT   REGION     2202   2505       Thioesterase.
FT   ACT_SITE    161    161       For beta-ketoacyl synthase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE    581    581       For malonyltransferase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE    878    878       For beta-hydroxyacyl dehydratase
FT                                activity. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10022}.
FT   ACT_SITE   2302   2302       For thioesterase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   ACT_SITE   2475   2475       For thioesterase activity.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10022}.
FT   MOD_RES       1      1       N-acetylmethionine. {ECO:0000250}.
FT   MOD_RES      59     59       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES      70     70       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     207    207       Phosphoserine. {ECO:0000250}.
FT   MOD_RES     298    298       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     528    528       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     673    673       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     790    790       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES     993    993       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1276   1276       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1698   1698       N6-(pyridoxal phosphate)lysine;
FT                                alternate. {ECO:0000250}.
FT   MOD_RES    1698   1698       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES    1765   1765       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1841   1841       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    1989   1989       N6-acetyllysine. {ECO:0000250}.
FT   MOD_RES    2151   2151       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00258}.
FT   MOD_RES    2230   2230       Phosphoserine. {ECO:0000250}.
FT   MOD_RES    2385   2385       N6-acetyllysine. {ECO:0000250}.
FT   CONFLICT    184    184       I -> T (in Ref. 3; AAA41145).
FT                                {ECO:0000305}.
FT   CONFLICT    871    871       S -> P (in Ref. 4; CAA31780).
FT                                {ECO:0000305}.
FT   CONFLICT   2085   2085       C -> P (in Ref. 6; AAA41144).
FT                                {ECO:0000305}.
FT   CONFLICT   2106   2106       A -> V (in Ref. 1; AAA57219, 3; AAA41145
FT                                and 5; CAA31882). {ECO:0000305}.
FT   CONFLICT   2296   2296       Y -> H (in Ref. 1; AAA57219 and 5;
FT                                CAA31882). {ECO:0000305}.
FT   HELIX      2122   2124
FT   HELIX      2126   2130
FT   STRAND     2140   2142
FT   HELIX      2144   2147
FT   HELIX      2152   2164
FT   HELIX      2171   2174
FT   HELIX      2180   2184
FT   STRAND     2188   2190
FT   STRAND     2192   2194
SQ   SEQUENCE   2505 AA;  272650 MW;  5810EC13D37F3114 CRC64;
     MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF
     DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL
     SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC
     PAAIVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGN GYCRAEAVVA VLLTKKSLAR
     RVYATILNAG TNTDGCKEQG VTFPSGEAQE QLIRSLYQPG GVAPESLEYI EAHGTGTKVG
     DPQELNGITR SLCAFRQSPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEN GVWAPNLHFH
     NPNPEIPALL DGRLQVVDRP LPVRGGIVGI NSFGFGGANV HVILQPNTQQ APAPAPHAAL
     PHLLHASGRT MEAVQGLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGHVQ
     EVQQVPASQR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEALKPL GVKVSDLLLS
     TDEHTFDDIV HSFVSLTAIQ IALIDLLTSM GLKPDGIIGH SLGEVACGYA DGCLSQREAV
     LAAYWRGQCI KDANLPAGSM AAVGLSWEEC KQRCPPGVVP ACHNSEDTVT ISGPQAAVNE
     FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA
     QWQSSLARTS SAEYNVNNLV SPVLFQEALW HVPEHAVVLE IAPHALLQAV LKRGVKPSCT
     IIPLMKRDHK DNLEFFLTNL GKVHLTGIDI NPNALFPPVE FPVPRGTPLI SPHIKWDHSQ
     TWDIPVAEDF PNGSSSSSAT VYNIDASSES SDHYLVDHCI DGRVLFPGTG YLYLVWKTLA
     RSLSLSLEET PVVFENVTFH QATILPRTGT VPLEVRLLEA SHAFEVSDSG NLIVSGKVYQ
     WEDPDSKLFD HPEVPIPAES ESVSRLTQGE VYKELRLRGY DYGPHFQGVY EATLEGEQGK
     LLWKDNWVTF MDTMLQISIL GFSKQSLQLP TRVTAIYIDP ATHLQKVYML EGDTQVADVT
     TSRCLGVTVS GGVYISRLQT TATSRRQQEQ LVPTLEKFVF TPHVEPECLS ESAILQKELQ
     LCKGLAKALQ TKATQQGLKM TVPGLEDLPQ HGLPRLLAAA CQLQLNGNLQ LELGEVLARE
     RLLLPEDPLI SGLLNSQALK ACIDTALENL STLKMKVVEV LAGEGHLYSH ISALLNTQPM
     LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWDPSGPAPT NLGALDLVVC NCALATLGDP
     ALALDNMVAA LKDGGFLLMH TVLKGHALGE TLACLPSEVQ PGPSFLSQEE WESLFSRKAL
     HLVGLKKSFY GTALFLCRRL SPQDKPIFLP VEDTSFQWVD SLKSILATSS SQPVWLTAMN
     CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SSTSHVPKLD PGSSELQKVL ESDLVMNVYR
     DGAWGAFRHF QLEQDKPEEQ TAHAFVNVLT RGDLASIRWV SSPLKHMQPP SSSGAQLCTV
     YYASLNFRDI MLATGKLSPD AIPGKWASRD CMLGMEFSGR DKCGRRVMGL VPAEGLATSV
     LLSPDFLWDV PSSWTLEEAA SVPVVYTTAY YSLVVRGRIQ HGETVLIHSG SGGVGQAAIS
     IALSLGCRVF TTVGSAEKRA YLQARFPQLD DTSFANSRDT SFEQHVLLHT GGKGVDLVLN
     SLAEEKLQAS VRCLAQHGRF LEIGKFDLSN NHPLGMAIFL KNVTFHGILL DALFEGANDS
     WREVAELLKA GIRDGVVKPL KCTVFPKAQV EDAFRYMAQG KHIGKVLVQV REEEPEAMLP
     GAQPTLISAI SKTFCPEHKS YIITGGLGGF GLELARWLVL RGAQRLVLTS RSGIRTGYQA
     KHVREWRRQG IHVLVSTSNV SSLEGARALI AEATKLGPVG GVFNLAMVLR DAMLENQTPE
     LFQDVNKPKY NGTLNLDRAT REACPELDYF VAFSSVSCGR GNAGQSNYGF ANSTMERICE
     QRRHDGLPGL AVQWGAIGDV GIILEAMGTN DTVVGGTLPQ RISSCMEVLD LFLNQPHAVL
     SSFVLAEKKA VAHGDGEAQR DLVKAVAHIL GIRDLAGINL DSSLADLGLD SLMGVEVRQI
     LEREHDLVLP IREVRQLTLR KLQEMSSKAG SDTELAAPKS KNDTSLKQAQ LNLSILLVNP
     EGPTLTRLNS VQSSERPLFL VHPIEGSITV FHSLAAKLSV PTYGLQCTQA APLDSIPNLA
     AYYIDCIKQV QPEGPYRVAG YSFGACVAFE MCSQLQAQQG PAPAHNNLFL FDGSHTYVLA
     YTQSYRAKLT PGCEAEAEAE AICFFIKQFV DAEHSKVLEA LLPLKSLEDR VAAAVDLITR
     SHQSLDRRDL SFAAVSFYYK LRAADQYKPK AKYHGNVILL RAKTGGTYGE DLGADYNLSQ
     VCDGKVSVHI IEGDHRTLLE GRGLESIINI IHSSLAEPRV SVREG
//
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