COQ8_YEAST
ID COQ8_YEAST Reviewed; 501 AA.
AC P27697; D6VU29;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Atypical kinase COQ8, mitochondrial {ECO:0000250|UniProtKB:Q8NI60};
DE EC=2.7.-.- {ECO:0000250|UniProtKB:Q8NI60};
DE AltName: Full=Activity of bc1 complex protein 1;
DE AltName: Full=Coenzyme Q protein 8;
DE AltName: Full=Ubiquinone biosynthesis protein COQ8;
DE Flags: Precursor;
GN Name=COQ8; Synonyms=ABC1; OrderedLocusNames=YGL119W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=S9-12/50;
RX PubMed=1648478; DOI=10.1002/j.1460-2075.1991.tb07732.x;
RA Bousquet I., Dujardin G., Slonimski P.P.;
RT "ABC1, a novel yeast nuclear gene has a dual function in mitochondria: it
RT suppresses a cytochrome b mRNA translation defect and is essential for the
RT electron transfer in the bc 1 complex.";
RL EMBO J. 10:2023-2031(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION.
RX PubMed=9210471; DOI=10.1111/j.1432-1033.1997.t01-1-00103.x;
RA Brasseur G., Tron G., Dujardin G., Slonimski P.P., Brivet-Chevillotte P.;
RT "The nuclear ABC1 gene is essential for the correct conformation and
RT functioning of the cytochrome bc1 complex and the neighbouring complexes II
RT and IV in the mitochondrial respiratory chain.";
RL Eur. J. Biochem. 246:103-111(1997).
RN [5]
RP FUNCTION.
RX PubMed=9266513; DOI=10.1016/s0098-2997(97)00004-6;
RA Poon W.W., Do T.Q., Marbois B.N., Clarke C.F.;
RT "Sensitivity to treatment with polyunsaturated fatty acids is a general
RT characteristic of the ubiquinone-deficient yeast coq mutants.";
RL Mol. Aspects Med. 18:S121-S127(1997).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=10760477; DOI=10.1016/s1388-1981(00)00019-6;
RA Hsu A.Y., Do T.Q., Lee P.T., Clarke C.F.;
RT "Genetic evidence for a multi-subunit complex in the O-methyltransferase
RT steps of coenzyme Q biosynthesis.";
RL Biochim. Biophys. Acta 1484:287-297(2000).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11279158; DOI=10.1074/jbc.m100952200;
RA Do T.Q., Hsu A.Y., Jonassen T., Lee P.T., Clarke C.F.;
RT "A defect in coenzyme Q biosynthesis is responsible for the respiratory
RT deficiency in Saccharomyces cerevisiae abc1 mutants.";
RL J. Biol. Chem. 276:18161-18168(2001).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION.
RX PubMed=15063807; DOI=10.1016/j.bbrc.2004.03.096;
RA Hsieh E.J., Dinoso J.B., Clarke C.F.;
RT "A tRNA(TRP) gene mediates the suppression of cbs2-223 previously
RT attributed to ABC1/COQ8.";
RL Biochem. Biophys. Res. Commun. 317:648-653(2004).
RN [10]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=18801050; DOI=10.1111/j.1567-1364.2008.00436.x;
RA Tauche A., Krause-Buchholz U., Rodel G.;
RT "Ubiquinone biosynthesis in Saccharomyces cerevisiae: the molecular
RT organization of O-methylase Coq3p depends on Abc1p/Coq8p.";
RL FEMS Yeast Res. 8:1263-1275(2008).
RN [11]
RP FUNCTION.
RX PubMed=19002377; DOI=10.1007/s00018-008-8547-7;
RA Padilla S., Tran U.C., Jimenez-Hidalgo M., Lopez-Martin J.M.,
RA Martin-Montalvo A., Clarke C.F., Navas P., Santos-Ocana C.;
RT "Hydroxylation of demethoxy-Q6 constitutes a control point in yeast
RT coenzyme Q6 biosynthesis.";
RL Cell. Mol. Life Sci. 66:173-186(2009).
RN [12]
RP SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF GLY-89; GLY-130;
RP ALA-197; LYS-216; ASP-229; ASP-346; ASN-348 AND GLY-475.
RX PubMed=21296186; DOI=10.1016/j.bbalip.2011.01.009;
RA Xie L.X., Hsieh E.J., Watanabe S., Allan C.M., Chen J.Y., Tran U.C.,
RA Clarke C.F.;
RT "Expression of the human atypical kinase ADCK3 rescues coenzyme Q
RT biosynthesis and phosphorylation of Coq polypeptides in yeast coq8
RT mutants.";
RL Biochim. Biophys. Acta 1811:348-360(2011).
RN [13]
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF LYS-134; GLN-137; ALA-197; SER-198;
RP LYS-216; GLU-269; ASP-346; ASN-351; ASP-365 AND ARG-471.
RX PubMed=25498144; DOI=10.1016/j.molcel.2014.11.002;
RA Stefely J.A., Reidenbach A.G., Ulbrich A., Oruganty K., Floyd B.J.,
RA Jochem A., Saunders J.M., Johnson I.E., Minogue C.E., Wrobel R.L.,
RA Barber G.E., Lee D., Li S., Kannan N., Coon J.J., Bingman C.A.,
RA Pagliarini D.J.;
RT "Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable
RT coenzyme Q biosynthesis.";
RL Mol. Cell 57:83-94(2015).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF LYS-134; ALA-197 AND ASP-365.
RX PubMed=27499294; DOI=10.1016/j.molcel.2016.06.030;
RA Stefely J.A., Licitra F., Laredj L., Reidenbach A.G., Kemmerer Z.A.,
RA Grangeray A., Jaeg-Ehret T., Minogue C.E., Ulbrich A., Hutchins P.D.,
RA Wilkerson E.M., Ruan Z., Aydin D., Hebert A.S., Guo X., Freiberger E.C.,
RA Reutenauer L., Jochem A., Chergova M., Johnson I.E., Lohman D.C.,
RA Rush M.J., Kwiecien N.W., Singh P.K., Schlagowski A.I., Floyd B.J.,
RA Forsman U., Sindelar P.J., Westphall M.S., Pierrel F., Zoll J.,
RA Dal Peraro M., Kannan N., Bingman C.A., Coon J.J., Isope P., Puccio H.,
RA Pagliarini D.J.;
RT "Cerebellar ataxia and coenzyme Q deficiency through loss of unorthodox
RT kinase activity.";
RL Mol. Cell 63:608-620(2016).
CC -!- FUNCTION: Atypical kinase involved in the biosynthesis of coenzyme Q,
CC also named ubiquinone, an essential lipid-soluble electron transporter
CC for aerobic cellular respiration (PubMed:27499294). Affects the
CC molecular organization and function of COQ3, possibly through kinase
CC activity towards COQ3, COQ5 and/or COQ7 (PubMed:11279158,
CC PubMed:15063807, PubMed:1648478, PubMed:18801050, PubMed:19002377,
CC PubMed:21296186, PubMed:9210471, PubMed:9266513, PubMed:25498144). Its
CC substrate specificity is unclear: does not show any protein kinase
CC activity (PubMed:27499294). Probably acts as a small molecule kinase,
CC possibly a lipid kinase that phosphorylates a prenyl lipid in the
CC ubiquinone biosynthesis pathway, as suggested by its ability to bind
CC coenzyme Q lipid intermediates (By similarity).
CC {ECO:0000250|UniProtKB:Q8NI60, ECO:0000269|PubMed:11279158,
CC ECO:0000269|PubMed:15063807, ECO:0000269|PubMed:1648478,
CC ECO:0000269|PubMed:18801050, ECO:0000269|PubMed:19002377,
CC ECO:0000269|PubMed:21296186, ECO:0000269|PubMed:25498144,
CC ECO:0000269|PubMed:27499294, ECO:0000269|PubMed:9210471,
CC ECO:0000269|PubMed:9266513}.
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000269|PubMed:25498144}.
CC -!- SUBUNIT: Forms homopolymers. Predominantly associated with a complex of
CC about 500 kDa. {ECO:0000269|PubMed:18801050}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11279158, ECO:0000269|PubMed:18801050,
CC ECO:0000269|PubMed:21296186}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11279158, ECO:0000269|PubMed:18801050,
CC ECO:0000269|PubMed:21296186}; Matrix side {ECO:0000269|PubMed:11279158,
CC ECO:0000269|PubMed:18801050, ECO:0000269|PubMed:21296186}.
CC -!- DOMAIN: Adopts an atypical protein kinase-like fold: while it adopts a
CC core fold similar to that of well-characterized protein kinase-like
CC domains. The KxGQ motif completely occludes the typical substrate
CC binding pocket. Nucleotide-binding opens the substrate binding pocket
CC and flips the active site from inside the hydrophobic core into a
CC catalytically competent, solvent-exposed posture.
CC {ECO:0000250|UniProtKB:Q8NI60}.
CC -!- DISRUPTION PHENOTYPE: Decreases COQ3 O-methyltransferase activity.
CC {ECO:0000269|PubMed:10760477}.
CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. ADCK protein
CC kinase family. {ECO:0000305}.
CC -!- CAUTION: Able to autophosphorylate in cis in vitro. This activity may
CC not be relevant in vivo and only reflects in vitro conditions. Probably
CC does not act as a protein kinase as it is unable to act in trans
CC (PubMed:27499294). {ECO:0000269|PubMed:27499294}.
CC -!- CAUTION: Was originally (PubMed:1648478) isolated as a multicopy
CC suppressor of a yeast strain harboring a mutation in a cytochrome b
CC translational activator (cbs2-223). But more recently it has been shown
CC (PubMed:15063807) that a tRNA(Trp) gene located downstream of COQ8
CC mediates suppression of the cbs2-223 mutation. The inability of COQ8 to
CC suppress the cbs2-223 allele in multicopy indicates it may not be a
CC chaperone as previously reported. {ECO:0000305|PubMed:15063807,
CC ECO:0000305|PubMed:1648478}.
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DR EMBL; X59027; CAA41759.1; -; Genomic_DNA.
DR EMBL; Z72641; CAA96827.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07990.1; -; Genomic_DNA.
DR PIR; S16711; S16711.
DR RefSeq; NP_011396.1; NM_001180984.1.
DR AlphaFoldDB; P27697; -.
DR SMR; P27697; -.
DR BioGRID; 33132; 127.
DR DIP; DIP-5113N; -.
DR IntAct; P27697; 4.
DR MINT; P27697; -.
DR STRING; 4932.YGL119W; -.
DR iPTMnet; P27697; -.
DR MaxQB; P27697; -.
DR PaxDb; P27697; -.
DR PRIDE; P27697; -.
DR DNASU; 852758; -.
DR EnsemblFungi; YGL119W_mRNA; YGL119W; YGL119W.
DR GeneID; 852758; -.
DR KEGG; sce:YGL119W; -.
DR SGD; S000003087; COQ8.
DR VEuPathDB; FungiDB:YGL119W; -.
DR eggNOG; KOG1234; Eukaryota.
DR GeneTree; ENSGT00940000169293; -.
DR HOGENOM; CLU_006533_9_0_1; -.
DR InParanoid; P27697; -.
DR OMA; QVERVMN; -.
DR BioCyc; YEAST:G3O-30616-MON; -.
DR UniPathway; UPA00232; -.
DR PRO; PR:P27697; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P27697; protein.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IDA:UniProtKB.
DR GO; GO:1901006; P:ubiquinone-6 biosynthetic process; IMP:SGD.
DR CDD; cd13970; ABC1_ADCK3; 1.
DR InterPro; IPR004147; ABC1_dom.
DR InterPro; IPR034646; ADCK3_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF03109; ABC1; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotide-binding; Reference proteome; Transferase; Transit peptide;
KW Ubiquinone biosynthesis.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..501
FT /note="Atypical kinase COQ8, mitochondrial"
FT /id="PRO_0000000260"
FT DOMAIN 188..501
FT /note="Protein kinase"
FT REGION 41..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 134..137
FT /note="KxGQ motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MOTIF 195..198
FT /note="AAAS motif"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT COMPBIAS 43..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 346
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 303..306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT BINDING 365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q8NI60"
FT MUTAGEN 89
FT /note="G->D: In coq8-2; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 130
FT /note="G->D: In coq8-5; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8. Impairs coenzyme Q6 biosynthesis."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 134
FT /note="K->A,H,R,S: Abolishes coenzyme Q biosynthesis. Able
FT to autophosphorylate in cis."
FT /evidence="ECO:0000269|PubMed:25498144,
FT ECO:0000269|PubMed:27499294"
FT MUTAGEN 137
FT /note="Q->E: Abolishes coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 197
FT /note="A->G,S: Abolishes coenzyme Q biosynthesis. Able to
FT autophosphorylate in cis."
FT /evidence="ECO:0000269|PubMed:25498144,
FT ECO:0000269|PubMed:27499294"
FT MUTAGEN 197
FT /note="A->V: In coq8-3; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8. Impairs coenzyme Q6 biosynthesis."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 198
FT /note="S->A: Decreased coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 216
FT /note="K->A: Impairs coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 216
FT /note="K->R: Abolishes coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 229
FT /note="D->N: In coq8-6; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 269
FT /note="E->Q: Abolishes coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 346
FT /note="D->N: Abolishes coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 346
FT /note="D->N: In coq8-2; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 348
FT /note="N->Y: In coq8-4; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8."
FT /evidence="ECO:0000269|PubMed:21296186"
FT MUTAGEN 351
FT /note="N->A: Abolishes coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 365
FT /note="D->N: Abolishes coenzyme Q biosynthesis. Enhanced
FT autophosphorylation in cis."
FT /evidence="ECO:0000269|PubMed:25498144,
FT ECO:0000269|PubMed:27499294"
FT MUTAGEN 471
FT /note="R->E: Abolishes coenzyme Q biosynthesis."
FT /evidence="ECO:0000269|PubMed:25498144"
FT MUTAGEN 475
FT /note="G->N: In coq8-8; impairs growth on ethanol and/or
FT glycerol as a carbon source, but retains steady-state
FT levels of COQ8."
FT /evidence="ECO:0000269|PubMed:21296186"
SQ SEQUENCE 501 AA; 56742 MW; C91D1EEE5A7ACC9C CRC64;
MVTNMVKLRN LRRLYCSSRL LRTIQNGRIS SVSSISLSKK YTTKSAKEGE ENVERKHEEE
KKDTLKSSSV PTSRISRLFH YGSLAAGVGM NAAAKGISEV AKGNSPTWKS LILSDSNIDR
ITNKFSKMRG VALKIGQLLS FQDEKVLPKE LYEILSRVQN SANHMPQRQL EKVMAKELGA
NWKTKFSKFD KIPMAAASIG QVHAAELPSG QRVVVKIQYP GVKESIDSDL NSLLMLLTAS
SLLPKGLFLD KTIANARTEL KWECDYNREA RALQKFEALL KDDPAFEVPH VFPEYTTDNI
ITMTRMEGTE IMKLPKASQE TKNFISENIM RLCLEEIATF KYMQTDPNWA NFLYNGRTKK
IELLDFGASR PFAEDFILKY RKLLTYATLR DRKGAYEMSV QLGYLTGLES QSMKDAHVDS
VLTLGEPFRG DVDKSFDFKD QTVSDRIRGN IGLMLNERLC PPPEETYSLH RKFSGIFLLC
ARMGASVHCA KLFKEIFAYK V
