ATNM_EMENI
ID ATNM_EMENI Reviewed; 2111 AA.
AC Q5AV07; A0A1U8QFM2; C8V3X8;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Fatty acid synthase beta subunit aflB {ECO:0000303|PubMed:26563584};
DE EC=2.3.1.86 {ECO:0000305|PubMed:26563584};
DE AltName: Full=Aspercryptin biosynthesis cluster protein M {ECO:0000303|PubMed:26563584};
DE Includes:
DE RecName: Full=3-hydroxyacyl-[acyl-carrier-protein] dehydratase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=4.2.1.59 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=Enoyl-[acyl-carrier-protein] reductase [NADH] {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=1.3.1.9 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] acetyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.38 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=[Acyl-carrier-protein] malonyltransferase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=2.3.1.39 {ECO:0000250|UniProtKB:Q8TGA1};
DE Includes:
DE RecName: Full=S-acyl fatty acid synthase thioesterase {ECO:0000250|UniProtKB:Q8TGA1};
DE EC=3.1.2.14 {ECO:0000250|UniProtKB:Q8TGA1};
GN Name=atnM {ECO:0000303|PubMed:26563584}; ORFNames=ANIA_07873;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [3]
RP IDENTIFICATION OF THE CLUSTER.
RX PubMed=23248299; DOI=10.1073/pnas.1205532110;
RA Andersen M.R., Nielsen J.B., Klitgaard A., Petersen L.M., Zachariasen M.,
RA Hansen T.J., Blicher L.H., Gotfredsen C.H., Larsen T.O., Nielsen K.F.,
RA Mortensen U.H.;
RT "Accurate prediction of secondary metabolite gene clusters in filamentous
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E99-E107(2013).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=27310134; DOI=10.1021/acschembio.6b00398;
RA Henke M.T., Soukup A.A., Goering A.W., McClure R.A., Thomson R.J.,
RA Keller N.P., Kelleher N.L.;
RT "New aspercryptins, lipopeptide natural products, revealed by HDAC
RT inhibition in Aspergillus nidulans.";
RL ACS Chem. Biol. 11:2117-2123(2016).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=26563584; DOI=10.1002/anie.201507097;
RA Chiang Y.M., Ahuja M., Oakley C.E., Entwistle R., Asokan A., Zutz C.,
RA Wang C.C., Oakley B.R.;
RT "Development of genetic dereplication strains in Aspergillus nidulans
RT results in the discovery of aspercryptin.";
RL Angew. Chem. Int. Ed. 55:1662-1665(2016).
CC -!- FUNCTION: Fatty acid synthase beta subunit; part of the gene cluster
CC that mediates the biosynthesis of aspercryptins, linear lipopeptides
CC built from six amino acids including 2 highly unusual and
CC nonproteogenic amino acids, 2-amino-octanoic acid (2aoa) and 2-amino-
CC dodecanol (2adol) (PubMed:23248299, PubMed:27310134, PubMed:26563584).
CC The core structure of aspercryptins is as follows: Ser/Ala-Thr-Ile/Val-
CC 2aoa-Asn-2adol (PubMed:27310134). The first step of aspercryptin
CC biosynthesis is the generation of the fatty acid precursors, octanoic
CC and dodecanoic acids, by the FAS subunits atnF and atnM
CC (PubMed:27310134, PubMed:26563584). The fatty acid precursors are
CC likely transformed into the corresponding alpha-amino fatty acids in
CC three steps (PubMed:27310134, PubMed:26563584). First, they are
CC hydroxylated by the cytochrome P450 monooxygenase atnE, then oxidized
CC to the corresponding alpha-keto acids by the NAD(P)-dependent
CC oxidoreductase atnD, and finally converted to the alpha-amino fatty
CC acids by the PLP-dependent aminotransferases atnH or atnJ
CC (PubMed:27310134, PubMed:26563584). the alpha-amino fatty acids, 2-
CC amino-octanoic and 2-amino-dodecanoic acids, are recognized, activated,
CC and covalently tethered to the NRPS atnA by its fourth and sixth
CC adenylation domains (PubMed:27310134). The second module of atnA is the
CC Thr module and contains an epimerase (E) domain responsible for the
CC epimerization of Thr to D-allo-Thr (PubMed:26563584). Additionally,
CC despite atnA having only one epimerase domain, the first amino acid of
CC aspercryptin A1 is D-Ser, suggesting that serine is either loaded
CC directly as D-Ser on the first module or that the epimerase domain in
CC the threonine module epimerizes both L-Ser and L-Thr (PubMed:27310134).
CC After condensation of the hexapeptide of aspercryptin, the C-terminal
CC reductase (TE) domain might be involved in the reductive release and
CC production of the aldehyde hexapeptide (PubMed:26563584). Further
CC reduction would generate aspercryptins (PubMed:27310134,
CC PubMed:26563584). The variety of aspercryptins produced reflects the
CC flexibiliy of the atnA NRPS, allowing incorporation of alanine instead
CC of serine, valine for isoleucine, and a C10 fatty amino alcohol instead
CC of the C12 version (PubMed:27310134). AtnB seems to be involved in the
CC selectivity for Ile versus Val by the third module (PubMed:26563584).
CC Moreover, type B, C and D aspercryptins have an additional N-terminal
CC cichorine, acetyl and propionyl group respectively (PubMed:27310134).
CC {ECO:0000269|PubMed:23248299, ECO:0000269|PubMed:26563584,
CC ECO:0000269|PubMed:27310134}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain
CC fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+);
CC Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:83139; EC=2.3.1.86;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
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:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] +
CC H(+) + NADH; Xref=Rhea:RHEA:10240, Rhea:RHEA-COMP:9925, Rhea:RHEA-
CC COMP:9926, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:78784, ChEBI:CHEBI:78785; EC=1.3.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000250|UniProtKB:Q8TGA1};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:26563584}.
CC -!- SUBUNIT: [Alpha(6)beta(6)] hexamers of two multifunctional subunits
CC (alpha and beta). {ECO:0000250|UniProtKB:P19097}.
CC -!- INDUCTION: Expression is positively regulated by the aspercryptin
CC cluser-specific transcription factor atnN (PubMed:27310134).
CC {ECO:0000269|PubMed:27310134}.
CC -!- DISRUPTION PHENOTYPE: Eliminates more than 99.5% of aspercryptin
CC production (PubMed:26563584). {ECO:0000269|PubMed:26563584}.
CC -!- SIMILARITY: Belongs to the fungal fatty acid synthetase subunit beta
CC family. {ECO:0000305}.
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DR EMBL; BN001302; CBF73431.1; -; Genomic_DNA.
DR EMBL; AACD01000135; EAA59527.1; -; Genomic_DNA.
DR RefSeq; XP_681142.1; XM_676050.1.
DR AlphaFoldDB; Q5AV07; -.
DR SMR; Q5AV07; -.
DR STRING; 162425.CADANIAP00003889; -.
DR EnsemblFungi; CBF73431; CBF73431; ANIA_07873.
DR EnsemblFungi; EAA59527; EAA59527; AN7873.2.
DR GeneID; 2868965; -.
DR KEGG; ani:AN7873.2; -.
DR VEuPathDB; FungiDB:AN7873; -.
DR eggNOG; ENOG502QQJX; Eukaryota.
DR HOGENOM; CLU_000114_5_0_1; -.
DR InParanoid; Q5AV07; -.
DR OMA; RVTHGMF; -.
DR OrthoDB; 8490at2759; -.
DR Proteomes; UP000000560; Chromosome II.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005835; C:fatty acid synthase complex; IBA:GO_Central.
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: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:0004318; F:enoyl-[acyl-carrier-protein] reductase (NADH) activity; IEA:UniProtKB-EC.
DR GO; GO:0016631; F:enoyl-[acyl-carrier-protein] reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IEA:UniProtKB-EC.
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:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 2.
DR Gene3D; 3.40.366.10; -; 3.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR016452; Fas1/AflB-like.
DR InterPro; IPR013565; Fas1/AflB-like_central.
DR InterPro; IPR040883; FAS_meander.
DR InterPro; IPR003965; Fatty_acid_synthase.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR039569; MaoC-like_dehydrat_N.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR032088; SAT.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF08354; DUF1729; 1.
DR Pfam; PF17951; FAS_meander; 1.
DR Pfam; PF13452; MaoC_dehydrat_N; 1.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR Pfam; PF16073; SAT; 1.
DR PIRSF; PIRSF005562; FAS_yeast_beta; 1.
DR PRINTS; PR01483; FASYNTHASE.
DR SMART; SM00827; PKS_AT; 1.
DR SUPFAM; SSF52151; SSF52151; 2.
DR SUPFAM; SSF54637; SSF54637; 2.
PE 2: Evidence at transcript level;
KW Hydrolase; Lyase; Multifunctional enzyme; NAD; NADP; Oxidoreductase;
KW Reference proteome; Transferase.
FT CHAIN 1..2111
FT /note="Fatty acid synthase beta subunit aflB"
FT /id="PRO_0000444130"
FT DOMAIN 1606..1708
FT /note="MaoC-like"
FT /evidence="ECO:0000255"
FT REGION 200..565
FT /note="Acetyltransferase (AT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 618..863
FT /note="Enoyl reductase (ER) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 1195..1688
FT /note="Dehydratase (DH) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1"
FT REGION 1727..2091
FT /note="Malonyl/palmitoyl transferase (MT/PT) domain"
FT /evidence="ECO:0000250|UniProtKB:Q8TGA1, ECO:0000255"
SQ SEQUENCE 2111 AA; 232678 MW; C8292622D4E784B1 CRC64;
MFNFPHPAID LASRMKSSPL MAGGSSSASS EDLFSPPMME DLDTPMTEYP MGSPPRMPYR
GEDIEIAFLR SEASIKKSSL FNDKFAATLD DLSARPIDSA SLIGKLQSMT RSVREILDSG
DQLVHEDGPQ EILKQFVRVV NKHLCQDEDI HTVLAPLALE PEEKFHIIQT YYQAISMTQF
VSPKWTSSLL SDALCRRANI VTVFNGQGVE GYFSELQHLY DTYGGLLAEP LYALSKQLKG
LASDVRAQDM YPHGLDVIGW LENPEARPST DYLLSAPVSQ PLIGLVQLLN YAITCKILNK
SPGEFARHLS GSAGHSQGIV VAAMLATVVS WPTFFDAAST ALQVLFWIGC RSQQCYPSHS
IPPSLVDQSE RLSPMLSVKG ASRESLLKYL DEHNRHLPPA QQGSLALING RQQFVVAGNP
LSLYAFANKL RAASNNSSTT NTARVPFSQR PLLITARFLP ISVPFHTSLL EDAEAQILED
LRSVHVPGNS LLFPVLRTDN GADLREFDNL VPELVHMVVC GVVDWDRATR FPTATHLLDF
GPGRETGIGA LLASTKAGTA ARVILSTTLT GPSKKTLGYM PELLSRRRPV VYNTSWEQDF
APRLVRVGDD ILLDTKFSRA LGLPPVMVAG MTPTTVSPDF VAEVINANYH IEIAGGGYHD
AAGMRSALTR LVNLIPAGRG ITVNLIYANP RAMGWQIPLL VQLRQEGLPI TGLTIGAGVP
SPDIASEYIR DLGLSHISFK PGSKEAIDNV LRIAESNPGF PIILQWTGGR AGGHHSYEDF
HEPILDRYAQ IRAYPNLILV AGSGFGGSDD TIPYITGSWS KKLGYAAMPF DGVLVGSRVM
TAKEARTSPA VKQAIVDTPG VPDSQWEGTY KKATGGIITV KSEMGEPIHK LATRGVLLWA
ELDKEVFSLP AAQQVQELQR RKGSLMKRLN ADFQKVWFGI DQQGNPVEIS EMTYAEVLTR
AVDLLYLKDQ QAWIDPSYRS FVADFIRCVE NRLSARQPRP RAVFQSALQL DRPQVFLSEF
LQAYPAALED VIVREDEDQL VKLYKQPGRK PLPFIVALDE SFEYWFKKDS LWQSERLEAV
TNQDVGRICI LHGPVAAQYT KVANEPVKQI LDNIHKPHVQ AILKQQYAGD TSRVPTLDYL
YSAGAVSPML SPQDELLLPH VKHSRSYDPP TLAYDLEGPE ENLPTEKQWL ALIGGTKPSW
RKALLTLNEI VQGKMLVENP IKGLFAPRAG LSVRIIQAGR PQKTVILMRQ KSSQGQEKDE
ATVEIRALST SEIMLTLRAP MTGGSAGNPP VDLVLYFTYK PTYGNNPIHE VMGTRNQRIS
RFYEQLWVGN AGDEGTSLQK SADDVQVLTR EAILNFTKAI DNRNSAYNGK KNSKLLAPLD
MAIVVAWKPL MRCLFTDAVN GDILKLLHLK NDFRVIDNAS PMREGDVLSS TAAIESIRIR
PDSGKVVRAV ATIFKKGTPI ITVASEFILQ GRYEDYHNTF ETKEEQVYKL PLKSKRDVVL
LASKPWFRIA AADLSLDDHL DDELTFRLKS SYHFRDANTY SQIETCGTVS CAVGNKDMTI
GTVMFKSNSH FLKNPVIDFL TRRGFAYDEV KQLPNAVPLA ADVRIEMPTS SDQYAAASGD
SNPIHLSRAF ARYAGHNEGR VIHGMQTSGL VRGVVELHAA GNDPRRMKAW SASFKGKVSP
GETLLVDISH TGMNNGRLIV VATARSESSS VEVFRATAEV AQKPGAYLFT GQGSQKPAMG
MDLYETSQAA RDVWHTAEQF FVNTYGISIL EIVRNNPKEY TVHFGGSRGK AIRENYISLD
FEVVNEQGEI ESVRAFQEIT PSSRSFTYTS SGGLLHETIF TQPALVVMEL ARFHDMRARG
LINEDSCYAG HSLGEYAALA AMGEVFTVEG VTAAVFYRGL TMQKSIELDR SGRDYSMVAA
NPSRVSKNLS ESDLCAIVDS IEAATGGLCE IVNFNVESTQ YVCAGDLRSL DCLAGVLDSL
VAHPEHLTSL ETLNASVPAI VASCLAQTDK KPTPLVLQRG KATIPLKVNV PFHSSLLRPG
ADTFRRALRK AIPEHMVRPE KLIGRYIPNL TAMPFELSKG YFENVLAISE SPFVREILER
WDDNNVAVAV C
