COQ3_HUMAN
ID COQ3_HUMAN Reviewed; 369 AA.
AC Q9NZJ6; B3KPX0; Q5T061; Q6P4F0; Q8IXG6; Q96BG1; Q9H0N1;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Ubiquinone biosynthesis O-methyltransferase, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=3-demethylubiquinol 3-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE EC=2.1.1.64 {ECO:0000255|HAMAP-Rule:MF_03190};
DE AltName: Full=Polyprenyldihydroxybenzoate methyltransferase {ECO:0000255|HAMAP-Rule:MF_03190};
DE EC=2.1.1.114 {ECO:0000255|HAMAP-Rule:MF_03190};
DE Flags: Precursor;
GN Name=COQ3 {ECO:0000255|HAMAP-Rule:MF_03190}; ORFNames=UG0215E05;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-134; GLY-272 AND
RP HIS-329.
RC TISSUE=Fetal brain;
RA Xie Y., Mao Y.;
RT "Isolation of full-length cDNA clones from human fetal brain cDNA
RT library.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-329.
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-272 AND HIS-329.
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-134; GLY-272 AND
RP HIS-329.
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-369, CATALYTIC ACTIVITY, AND VARIANTS
RP GLY-272 AND HIS-329.
RX PubMed=10777520; DOI=10.1074/jbc.275.17.12381;
RA Jonassen T., Clarke C.F.;
RT "Isolation and functional expression of human COQ3, a gene encoding a
RT methyltransferase required for ubiquinone biosynthesis.";
RL J. Biol. Chem. 275:12381-12387(2000).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps
CC in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-
CC Rule:MF_03190}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxy-5-all-trans-polyprenylbenzoate + S-adenosyl-L-
CC methionine = 3-methoxy,4-hydroxy-5-all-trans-polyprenylbenzoate +
CC H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44452, Rhea:RHEA-
CC COMP:10930, Rhea:RHEA-COMP:10931, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64694,
CC ChEBI:CHEBI:84443; EC=2.1.1.114; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03190, ECO:0000269|PubMed:10777520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol
CC + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:44380, Rhea:RHEA-
CC COMP:9566, Rhea:RHEA-COMP:10914, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17976, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:84422; EC=2.1.1.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03190, ECO:0000269|PubMed:10777520};
CC -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- SUBUNIT: Component of a multi-subunit COQ enzyme complex, composed of
CC at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9. {ECO:0000255|HAMAP-
CC Rule:MF_03190}.
CC -!- INTERACTION:
CC Q9NZJ6; Q9Y3A0: COQ4; NbExp=4; IntAct=EBI-10897372, EBI-12284865;
CC Q9NZJ6; Q5HYK3: COQ5; NbExp=7; IntAct=EBI-10897372, EBI-12577722;
CC Q9NZJ6; Q9Y2Z9: COQ6; NbExp=4; IntAct=EBI-10897372, EBI-718148;
CC Q9NZJ6; Q99807: COQ7; NbExp=5; IntAct=EBI-10897372, EBI-11017131;
CC Q9NZJ6; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-10897372, EBI-11978907;
CC Q9NZJ6; Q9Y697: NFS1; NbExp=3; IntAct=EBI-10897372, EBI-1751791;
CC Q9NZJ6; P43378: PTPN9; NbExp=3; IntAct=EBI-10897372, EBI-742898;
CC Q9NZJ6; Q13596: SNX1; NbExp=3; IntAct=EBI-10897372, EBI-2822329;
CC Q9NZJ6; P49638: TTPA; NbExp=3; IntAct=EBI-10897372, EBI-10210710;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_03190}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03190}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. UbiG/COQ3 family. {ECO:0000255|HAMAP-Rule:MF_03190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF66826.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF351615; AAN76515.1; -; mRNA.
DR EMBL; AL136726; CAB66660.1; -; mRNA.
DR EMBL; AK056955; BAG51832.1; -; mRNA.
DR EMBL; AL513550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015634; AAH15634.2; -; mRNA.
DR EMBL; BC063463; AAH63463.1; -; mRNA.
DR EMBL; AF193016; AAF66826.1; ALT_FRAME; mRNA.
DR CCDS; CCDS5042.1; -.
DR RefSeq; NP_059117.3; NM_017421.3.
DR AlphaFoldDB; Q9NZJ6; -.
DR SMR; Q9NZJ6; -.
DR BioGRID; 119731; 52.
DR ComplexPortal; CPX-3642; CoQ biosynthetic complex.
DR IntAct; Q9NZJ6; 16.
DR STRING; 9606.ENSP00000254759; -.
DR GlyGen; Q9NZJ6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NZJ6; -.
DR PhosphoSitePlus; Q9NZJ6; -.
DR BioMuta; COQ3; -.
DR DMDM; 313104241; -.
DR EPD; Q9NZJ6; -.
DR jPOST; Q9NZJ6; -.
DR MassIVE; Q9NZJ6; -.
DR MaxQB; Q9NZJ6; -.
DR PaxDb; Q9NZJ6; -.
DR PeptideAtlas; Q9NZJ6; -.
DR PRIDE; Q9NZJ6; -.
DR ProteomicsDB; 83417; -.
DR Antibodypedia; 31993; 173 antibodies from 22 providers.
DR DNASU; 51805; -.
DR Ensembl; ENST00000254759.8; ENSP00000254759.3; ENSG00000132423.12.
DR GeneID; 51805; -.
DR KEGG; hsa:51805; -.
DR MANE-Select; ENST00000254759.8; ENSP00000254759.3; NM_017421.4; NP_059117.3.
DR UCSC; uc003ppk.4; human.
DR CTD; 51805; -.
DR GeneCards; COQ3; -.
DR HGNC; HGNC:18175; COQ3.
DR HPA; ENSG00000132423; Tissue enhanced (tongue).
DR MIM; 605196; gene.
DR neXtProt; NX_Q9NZJ6; -.
DR OpenTargets; ENSG00000132423; -.
DR PharmGKB; PA134934287; -.
DR VEuPathDB; HostDB:ENSG00000132423; -.
DR eggNOG; KOG1270; Eukaryota.
DR GeneTree; ENSGT00390000007284; -.
DR InParanoid; Q9NZJ6; -.
DR OMA; RGTHDWE; -.
DR OrthoDB; 1542938at2759; -.
DR PhylomeDB; Q9NZJ6; -.
DR TreeFam; TF314553; -.
DR BioCyc; MetaCyc:HS05632-MON; -.
DR BRENDA; 2.1.1.114; 2681.
DR BRENDA; 2.1.1.222; 2681.
DR BRENDA; 2.1.1.64; 2681.
DR PathwayCommons; Q9NZJ6; -.
DR Reactome; R-HSA-2142789; Ubiquinol biosynthesis.
DR SignaLink; Q9NZJ6; -.
DR UniPathway; UPA00232; -.
DR BioGRID-ORCS; 51805; 60 hits in 1072 CRISPR screens.
DR ChiTaRS; COQ3; human.
DR GenomeRNAi; 51805; -.
DR Pharos; Q9NZJ6; Tbio.
DR PRO; PR:Q9NZJ6; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NZJ6; protein.
DR Bgee; ENSG00000132423; Expressed in biceps brachii and 185 other tissues.
DR ExpressionAtlas; Q9NZJ6; baseline and differential.
DR Genevisible; Q9NZJ6; HS.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0110142; C:ubiquinone biosynthesis complex; IPI:ComplexPortal.
DR GO; GO:0008425; F:2-polyprenyl-6-methoxy-1,4-benzoquinone methyltransferase activity; IEA:InterPro.
DR GO; GO:0044596; F:3-demethylubiquinol-10 3-O-methyltransferase activity; TAS:Reactome.
DR GO; GO:0008689; F:3-demethylubiquinone-9 3-O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0044595; F:decaprenyldihydroxybenzoate methyltransferase activity; TAS:Reactome.
DR GO; GO:0004395; F:hexaprenyldihydroxybenzoate methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008171; F:O-methyltransferase activity; IGI:UniProtKB.
DR GO; GO:0006071; P:glycerol metabolic process; IGI:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0010795; P:regulation of ubiquinone biosynthetic process; IEA:Ensembl.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IGI:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00472; UbiG; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR010233; UbiG_MeTrfase.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01983; UbiG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Membrane; Methyltransferase; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; Transit peptide; Ubiquinone biosynthesis.
FT TRANSIT 1..85
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT CHAIN 86..369
FT /note="Ubiquinone biosynthesis O-methyltransferase,
FT mitochondrial"
FT /id="PRO_0000035926"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT BINDING 222
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03190"
FT MOD_RES 143
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS4"
FT MOD_RES 149
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS4"
FT MOD_RES 196
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMS4"
FT VARIANT 134
FT /note="K -> E (in dbSNP:rs11548336)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_061925"
FT VARIANT 272
FT /note="S -> G (in dbSNP:rs6925344)"
FT /evidence="ECO:0000269|PubMed:10777520,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.1"
FT /id="VAR_020789"
FT VARIANT 329
FT /note="Y -> H (in dbSNP:rs4144164)"
FT /evidence="ECO:0000269|PubMed:10777520,
FT ECO:0000269|PubMed:11230166, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_020790"
FT CONFLICT 21
FT /note="G -> V (in Ref. 2; CAB66660)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="N -> D (in Ref. 2; CAB66660)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..289
FT /note="PET -> LEP (in Ref. 1; AAN76515)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="N -> D (in Ref. 1; AAN76515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 41054 MW; B257A099D6C06A2D CRC64;
MWSGRKLGSS GGWFLRVLGP GGCNTKAARP LISSAVYVKN QLSGTLQIKP GVFNEYRTIW
FKSYRTIFSC LNRIKSFRYP WARLYSTSQT TVDSGEVKTF LALAHKWWDE QGVYAPLHSM
NDLRVPFIRD NLLKTIPNHQ PGKPLLGMKI LDVGCGGGLL TEPLGRLGAS VIGIDPVDEN
IKTAQCHKSF DPVLDKRIEY RVCSLEEIVE ETAETFDAVV ASEVVEHVID LETFLQCCCQ
VLKPGGSLFI TTINKTQLSY ALGIVFSEQI ASIVPKGTHT WEKFVSPETL ESILESNGLS
VQTVVGMLYN PFSGYWHWSE NTSLNYAAYA VKSRVQEHPA SAEFVLKGET EELQANACTN
PAVHEKLKK
