ATG3_HUMAN
ID ATG3_HUMAN Reviewed; 314 AA.
AC Q9NT62; Q6PKC5; Q9H6L9;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Ubiquitin-like-conjugating enzyme ATG3;
DE EC=2.3.2.-;
DE AltName: Full=Autophagy-related protein 3;
DE Short=APG3-like;
DE Short=hApg3;
DE AltName: Full=Protein PC3-96;
GN Name=ATG3; Synonyms=APG3, APG3L;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MUTAGENESIS OF
RP CYS-264, SUBCELLULAR LOCATION, FUNCTION, ACTIVE SITE, AND INTERACTION WITH
RP ATG7 AND ATG12.
RC TISSUE=Brain;
RX PubMed=11825910; DOI=10.1074/jbc.m200385200;
RA Tanida I., Tanida-Miyake E., Komatsu M., Ueno T., Kominami E.;
RT "Human Apg3p/Aut1p homologue is an authentic E2 enzyme for multiple
RT substrates, GATE-16, GABARAP, and MAP-LC3, and facilitates the conjugation
RT of hApg12p to hApg5p.";
RL J. Biol. Chem. 277:13739-13744(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retina;
RA Wu B.X., Li Y., Laser M., Crosson C.E., Hazard E.S. III, Ma J.X.;
RT "Cloning and characterization of human PC3-96 gene.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Lymph;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-314 (ISOFORM 2).
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 [6]
RP FUNCTION, AND INTERACTION WITH THE ATG12-ATG5 CONJUGATE.
RX PubMed=12207896; DOI=10.1016/s0006-291x(02)02057-0;
RA Tanida I., Nishitani T., Nemoto T., Ueno T., Kominami E.;
RT "Mammalian Apg12p, but not the Apg12p.Apg5p conjugate, facilitates LC3
RT processing.";
RL Biochem. Biophys. Res. Commun. 296:1164-1170(2002).
RN [7]
RP FUNCTION.
RX PubMed=12890687; DOI=10.1074/jbc.m300550200;
RA Nemoto T., Tanida I., Tanida-Miyake E., Minematsu-Ikeguchi N., Yokota M.,
RA Ohsumi M., Ueno T., Kominami E.;
RT "The mouse APG10 homologue, an E2-like enzyme for Apg12p conjugation,
RT facilitates MAP-LC3 modification.";
RL J. Biol. Chem. 278:39517-39526(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP FUNCTION.
RX PubMed=16704426; DOI=10.1111/j.1742-4658.2006.05260.x;
RA Tanida I., Sou Y.S., Minematsu-Ikeguchi N., Ueno T., Kominami E.;
RT "Atg8L/Apg8L is the fourth mammalian modifier of mammalian Atg8 conjugation
RT mediated by human Atg4B, Atg7 and Atg3.";
RL FEBS J. 273:2553-2562(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH FNBP1L.
RX PubMed=19342671; DOI=10.4049/jimmunol.0803050;
RA Huett A., Ng A., Cao Z., Kuballa P., Komatsu M., Daly M.J., Podolsky D.K.,
RA Xavier R.J.;
RT "A novel hybrid yeast-human network analysis reveals an essential role for
RT FNBP1L in antibacterial autophagy.";
RL J. Immunol. 182:4917-4930(2009).
RN [13]
RP FUNCTION, AND INTERACTION WITH ATG12.
RX PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
RA Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
RA Debnath J.;
RT "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and cell
RT death.";
RL Cell 142:590-600(2010).
RN [14]
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 [15]
RP DOMAIN, AND CLEAVAGE BY CASP8.
RX PubMed=22644571; DOI=10.1007/s10495-012-0735-0;
RA Oral O., Oz-Arslan D., Itah Z., Naghavi A., Deveci R., Karacali S.,
RA Gozuacik D.;
RT "Cleavage of Atg3 protein by caspase-8 regulates autophagy during receptor-
RT activated cell death.";
RL Apoptosis 17:810-820(2012).
RN [16]
RP INTERACTION WITH ATG3 AND ATG12.
RX PubMed=22170151; DOI=10.4161/auto.8.1.18339;
RA Tanida I., Yamasaki M., Komatsu M., Ueno T.;
RT "The FAP motif within human ATG7, an autophagy-related E1-like enzyme, is
RT essential for the E2-substrate reaction of LC3 lipidation.";
RL Autophagy 8:88-97(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: E2 conjugating enzyme required for the cytoplasm to vacuole
CC transport (Cvt), autophagy, and mitochondrial homeostasis. Responsible
CC for the E2-like covalent binding of phosphatidylethanolamine to the C-
CC terminal Gly of ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2 or
CC MAP1LC3A). The ATG12-ATG5 conjugate plays a role of an E3 and promotes
CC the transfer of ATG8-like proteins from ATG3 to
CC phosphatidylethanolamine (PE). This step is required for the membrane
CC association of ATG8-like proteins. The formation of the ATG8-
CC phosphatidylethanolamine conjugates is essential for autophagy and for
CC the cytoplasm to vacuole transport (Cvt). Preferred substrate is
CC MAP1LC3A. Also acts as an autocatalytic E2-like enzyme, catalyzing the
CC conjugation of ATG12 to itself, ATG12 conjugation to ATG3 playing a
CC role in mitochondrial homeostasis but not in autophagy. ATG7 (E1-like
CC enzyme) facilitates this reaction by forming an E1-E2 complex with
CC ATG3. Promotes primary ciliogenesis by removing OFD1 from centriolar
CC satellites via the autophagic pathway. {ECO:0000269|PubMed:11825910,
CC ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:12890687,
CC ECO:0000269|PubMed:16704426, ECO:0000269|PubMed:20723759}.
CC -!- SUBUNIT: Interacts with ATG7 and ATG12. The complex, composed of ATG3
CC and ATG7, plays a role in the conjugation of ATG12 to ATG5. Interacts
CC with FNBP1L. {ECO:0000269|PubMed:11825910, ECO:0000269|PubMed:12207896,
CC ECO:0000269|PubMed:19342671, ECO:0000269|PubMed:20723759,
CC ECO:0000269|PubMed:22170151}.
CC -!- INTERACTION:
CC Q9NT62; O94817: ATG12; NbExp=6; IntAct=EBI-988094, EBI-746742;
CC Q9NT62; O95166: GABARAP; NbExp=5; IntAct=EBI-988094, EBI-712001;
CC Q9NT62; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-988094, EBI-746969;
CC Q9NT62; P60520: GABARAPL2; NbExp=5; IntAct=EBI-988094, EBI-720116;
CC Q9NT62; P62879: GNB2; NbExp=3; IntAct=EBI-988094, EBI-356942;
CC Q9NT62; Q9GZQ8: MAP1LC3B; NbExp=7; IntAct=EBI-988094, EBI-373144;
CC Q9NT62; Q70IA6: MOB2; NbExp=3; IntAct=EBI-988094, EBI-2558739;
CC Q9NT62; Q7Z6L1: TECPR1; NbExp=3; IntAct=EBI-988094, EBI-2946676;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11825910}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NT62-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NT62-2; Sequence=VSP_013037;
CC -!- TISSUE SPECIFICITY: Widely expressed, with a highest expression in
CC heart, skeletal muscle, kidney, liver and placenta.
CC {ECO:0000269|PubMed:11825910}.
CC -!- PTM: Conjugated to ATG12 at Lys-243. ATG12-conjugation plays a role in
CC regulation of mitochondrial homeostasis and cell death, while it is not
CC involved in PE-conjugation to ATG8-like proteins and autophagy.
CC -!- PTM: Cleaved by CASP8 upon death ligand binding such as tumor necrosis
CC factor-alpha. CASP8 cleavage blocks survival-related autophagy and
CC favors apoptosis. {ECO:0000269|PubMed:22644571}.
CC -!- SIMILARITY: Belongs to the ATG3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH02830.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15237.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAH02830.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB079384; BAB90843.1; -; mRNA.
DR EMBL; AF202092; AAG35611.1; -; mRNA.
DR EMBL; AL137515; CAB70781.1; -; mRNA.
DR EMBL; BC002830; AAH02830.1; ALT_FRAME; mRNA.
DR EMBL; BC024221; AAH24221.1; -; mRNA.
DR EMBL; AK025778; BAB15237.1; ALT_INIT; mRNA.
DR CCDS; CCDS2966.1; -. [Q9NT62-1]
DR CCDS; CCDS63721.1; -. [Q9NT62-2]
DR PIR; T46276; T46276.
DR RefSeq; NP_001265641.1; NM_001278712.1. [Q9NT62-2]
DR RefSeq; NP_071933.2; NM_022488.4. [Q9NT62-1]
DR PDB; 4NAW; X-ray; 2.20 A; D/H/L/P=140-170.
DR PDBsum; 4NAW; -.
DR AlphaFoldDB; Q9NT62; -.
DR SMR; Q9NT62; -.
DR BioGRID; 122171; 263.
DR DIP; DIP-35052N; -.
DR IntAct; Q9NT62; 37.
DR STRING; 9606.ENSP00000283290; -.
DR TCDB; 9.A.15.2.1; the autophagy-related phagophore-formation transporter (apt) family.
DR GlyGen; Q9NT62; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NT62; -.
DR PhosphoSitePlus; Q9NT62; -.
DR SwissPalm; Q9NT62; -.
DR BioMuta; ATG3; -.
DR DMDM; 61212142; -.
DR EPD; Q9NT62; -.
DR jPOST; Q9NT62; -.
DR MassIVE; Q9NT62; -.
DR MaxQB; Q9NT62; -.
DR PaxDb; Q9NT62; -.
DR PeptideAtlas; Q9NT62; -.
DR PRIDE; Q9NT62; -.
DR ProteomicsDB; 82601; -. [Q9NT62-1]
DR ProteomicsDB; 82602; -. [Q9NT62-2]
DR Antibodypedia; 32502; 751 antibodies from 39 providers.
DR DNASU; 64422; -.
DR Ensembl; ENST00000283290.10; ENSP00000283290.5; ENSG00000144848.11. [Q9NT62-1]
DR Ensembl; ENST00000402314.6; ENSP00000385943.2; ENSG00000144848.11. [Q9NT62-2]
DR GeneID; 64422; -.
DR KEGG; hsa:64422; -.
DR MANE-Select; ENST00000283290.10; ENSP00000283290.5; NM_022488.5; NP_071933.2.
DR UCSC; uc003dzc.5; human. [Q9NT62-1]
DR CTD; 64422; -.
DR DisGeNET; 64422; -.
DR GeneCards; ATG3; -.
DR HGNC; HGNC:20962; ATG3.
DR HPA; ENSG00000144848; Low tissue specificity.
DR MIM; 609606; gene.
DR neXtProt; NX_Q9NT62; -.
DR OpenTargets; ENSG00000144848; -.
DR PharmGKB; PA134883444; -.
DR VEuPathDB; HostDB:ENSG00000144848; -.
DR eggNOG; KOG2981; Eukaryota.
DR GeneTree; ENSGT00390000010308; -.
DR HOGENOM; CLU_027518_0_0_1; -.
DR InParanoid; Q9NT62; -.
DR OMA; YDKYYQV; -.
DR OrthoDB; 1432328at2759; -.
DR PhylomeDB; Q9NT62; -.
DR TreeFam; TF105903; -.
DR PathwayCommons; Q9NT62; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SignaLink; Q9NT62; -.
DR SIGNOR; Q9NT62; -.
DR BioGRID-ORCS; 64422; 37 hits in 1087 CRISPR screens.
DR ChiTaRS; ATG3; human.
DR GenomeRNAi; 64422; -.
DR Pharos; Q9NT62; Tbio.
DR PRO; PR:Q9NT62; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NT62; protein.
DR Bgee; ENSG00000144848; Expressed in monocyte and 210 other tissues.
DR ExpressionAtlas; Q9NT62; baseline and differential.
DR Genevisible; Q9NT62; HS.
DR GO; GO:0000153; C:cytoplasmic ubiquitin ligase complex; IPI:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0019777; F:Atg12 transferase activity; ISS:UniProtKB.
DR GO; GO:0019776; F:Atg8 ligase activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0019787; F:ubiquitin-like protein transferase activity; IDA:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
DR DisProt; DP01720; -.
DR InterPro; IPR007135; Atg3/Atg10.
DR PANTHER; PTHR12866; PTHR12866; 1.
DR Pfam; PF03987; Autophagy_act_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Cytoplasm;
KW Isopeptide bond; Protein transport; Reference proteome; Transferase;
KW Transport; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..314
FT /note="Ubiquitin-like-conjugating enzyme ATG3"
FT /id="PRO_0000213569"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 166..169
FT /note="Caspase cleavage motif LETD"
FT ACT_SITE 264
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305|PubMed:11825910"
FT SITE 169..170
FT /note="Cleavage; by CASP8"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CROSSLNK 243
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ATG12)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 290..314
FT /note="LLIFLKFVQAVIPTIEYDYTRHFTM -> PSLYVRLVAKWLLTIFFLRNLV
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_013037"
FT MUTAGEN 264
FT /note="C->S: Instead of the formation of an intermediate
FT complex with a thiol ester bond between ATG3 (E2-like
FT enzyme) and GABARAPL1/APG8L (substrate), a stable complex
FT with an O-ester bond is formed."
FT /evidence="ECO:0000269|PubMed:11825910"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:4NAW"
SQ SEQUENCE 314 AA; 35864 MW; 40EFE88DB5FE3EAB CRC64;
MQNVINTVKG KALEVAEYLT PVLKESKFKE TGVITPEEFV AAGDHLVHHC PTWQWATGEE
LKVKAYLPTG KQFLVTKNVP CYKRCKQMEY SDELEAIIEE DDGDGGWVDT YHNTGITGIT
EAVKEITLEN KDNIRLQDCS ALCEEEEDED EGEAADMEEY EESGLLETDE ATLDTRKIVE
ACKAKTDAGG EDAILQTRTY DLYITYDKYY QTPRLWLFGY DEQRQPLTVE HMYEDISQDH
VKKTVTIENH PHLPPPPMCS VHPCRHAEVM KKIIETVAEG GGELGVHMYL LIFLKFVQAV
IPTIEYDYTR HFTM
