ID   ODO2_MOUSE              Reviewed;         454 AA.
AC   Q9D2G2; Q3UEA0; Q4FK55; Q8CIE8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 177.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial {ECO:0000305};
DE            EC=2.3.1.61 {ECO:0000250|UniProtKB:P36957};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2;
DE            Short=OGDC-E2;
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE   AltName: Full=E2K;
DE   Flags: Precursor;
GN   Name=Dlst {ECO:0000312|MGI:MGI:1926170};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Heart, Oviduct, Testis, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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   [4]
RP   PROTEIN SEQUENCE OF 69-89; 288-308; 314-334 AND 355-346, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-268; LYS-273; LYS-274;
RP   LYS-278 AND LYS-308, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [7]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=36854377; DOI=10.1098/rsob.220363;
RA   Hevler J.F., Albanese P., Cabrera-Orefice A., Potter A., Jankevics A.,
RA   Misic J., Scheltema R.A., Brandt U., Arnold S., Heck A.J.R.;
RT   "MRPS36 provides a structural link in the eukaryotic 2-oxoglutarate
RT   dehydrogenase complex.";
RL   Open Biol. 13:220363-220363(2023).
CC   -!- FUNCTION: Dihydrolipoamide succinyltransferase (E2) component of the 2-
CC       oxoglutarate dehydrogenase complex (By similarity). The 2-oxoglutarate
CC       dehydrogenase complex catalyzes the overall conversion of 2-
CC       oxoglutarate to succinyl-CoA and CO(2) (By similarity). The 2-
CC       oxoglutarate dehydrogenase complex is mainly active in the
CC       mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex
CC       also localizes in the nucleus and is required for lysine succinylation
CC       of histones: associates with KAT2A on chromatin and provides succinyl-
CC       CoA to histone succinyltransferase KAT2A (By similarity).
CC       {ECO:0000250|UniProtKB:P36957, ECO:0000250|UniProtKB:Q9N0F1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC         succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC         COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC         ChEBI:CHEBI:83120; EC=2.3.1.61;
CC         Evidence={ECO:0000250|UniProtKB:P36957};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15215;
CC         Evidence={ECO:0000250|UniProtKB:P36957};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000250|UniProtKB:P11179};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000250|UniProtKB:P11179};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 6/6.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC       {ECO:0000250|UniProtKB:P36957}.
CC   -!- SUBUNIT: The 2-oxoglutarate dehydrogenase complex is composed of OGDH
CC       (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide
CC       succinyltransferase; E2), DLD (dihydrolipoamide dehydrogenase; E3) and
CC       the assembly factor KGD4 (PubMed:36854377). It contains multiple copies
CC       of the three enzymatic components (E1, E2 and E3). In the nucleus, the
CC       2-oxoglutarate dehydrogenase complex associates with KAT2A. Interacts
CC       with ABHD11; this interaction maintains the functional lipoylation of
CC       the 2-oxoglutarate dehydrogenase complex (By similarity).
CC       {ECO:0000250|UniProtKB:P36957, ECO:0000269|PubMed:36854377}.
CC   -!- INTERACTION:
CC       Q9D2G2; Q9QXS1: Plec; NbExp=2; IntAct=EBI-773210, EBI-774583;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P36957}. Nucleus {ECO:0000250|UniProtKB:P36957}.
CC       Note=Mainly localizes in the mitochondrion. A small fraction localizes
CC       to the nucleus, where the 2-oxoglutarate dehydrogenase complex is
CC       required for histone succinylation. {ECO:0000250|UniProtKB:P36957}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D2G2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D2G2-2; Sequence=VSP_025015, VSP_025016;
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AK019713; BAB31840.1; -; mRNA.
DR   EMBL; AK054053; BAC35637.1; -; mRNA.
DR   EMBL; AK149664; BAE29011.1; -; mRNA.
DR   EMBL; AK158877; BAE34709.1; -; mRNA.
DR   EMBL; AK168570; BAE40440.1; -; mRNA.
DR   EMBL; AK169943; BAE41472.1; -; mRNA.
DR   EMBL; CT010197; CAJ18405.1; -; mRNA.
DR   EMBL; BC006702; AAH06702.1; -; mRNA.
DR   EMBL; BC024066; AAH24066.1; -; mRNA.
DR   CCDS; CCDS26052.1; -. [Q9D2G2-1]
DR   RefSeq; NP_084501.1; NM_030225.4. [Q9D2G2-1]
DR   AlphaFoldDB; Q9D2G2; -.
DR   SMR; Q9D2G2; -.
DR   BioGRID; 219707; 35.
DR   IntAct; Q9D2G2; 62.
DR   MINT; Q9D2G2; -.
DR   STRING; 10090.ENSMUSP00000060346; -.
DR   ChEMBL; CHEMBL2176822; -.
DR   GlyGen; Q9D2G2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D2G2; -.
DR   MetOSite; Q9D2G2; -.
DR   PhosphoSitePlus; Q9D2G2; -.
DR   SwissPalm; Q9D2G2; -.
DR   REPRODUCTION-2DPAGE; Q9D2G2; -.
DR   EPD; Q9D2G2; -.
DR   jPOST; Q9D2G2; -.
DR   MaxQB; Q9D2G2; -.
DR   PaxDb; 10090-ENSMUSP00000060346; -.
DR   PeptideAtlas; Q9D2G2; -.
DR   ProteomicsDB; 293493; -. [Q9D2G2-1]
DR   ProteomicsDB; 293494; -. [Q9D2G2-2]
DR   Pumba; Q9D2G2; -.
DR   TopDownProteomics; Q9D2G2-1; -. [Q9D2G2-1]
DR   TopDownProteomics; Q9D2G2-2; -. [Q9D2G2-2]
DR   Antibodypedia; 45; 224 antibodies from 29 providers.
DR   DNASU; 78920; -.
DR   Ensembl; ENSMUST00000053811.10; ENSMUSP00000060346.9; ENSMUSG00000004789.11. [Q9D2G2-1]
DR   Ensembl; ENSMUST00000221357.2; ENSMUSP00000152664.2; ENSMUSG00000004789.11. [Q9D2G2-1]
DR   GeneID; 78920; -.
DR   KEGG; mmu:78920; -.
DR   UCSC; uc007ogj.2; mouse. [Q9D2G2-1]
DR   AGR; MGI:1926170; -.
DR   CTD; 1743; -.
DR   MGI; MGI:1926170; Dlst.
DR   VEuPathDB; HostDB:ENSMUSG00000004789; -.
DR   eggNOG; KOG0559; Eukaryota.
DR   GeneTree; ENSGT00930000151014; -.
DR   HOGENOM; CLU_016733_0_0_1; -.
DR   InParanoid; Q9D2G2; -.
DR   OMA; MKVPSPG; -.
DR   OrthoDB; 672at2759; -.
DR   PhylomeDB; Q9D2G2; -.
DR   TreeFam; TF314164; -.
DR   BRENDA; 2.3.1.61; 3474.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-MMU-71064; Lysine catabolism.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   UniPathway; UPA00223; -.
DR   UniPathway; UPA00868; UER00840.
DR   BioGRID-ORCS; 78920; 26 hits in 83 CRISPR screens.
DR   ChiTaRS; Dlst; mouse.
DR   PRO; PR:Q9D2G2; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q9D2G2; Protein.
DR   Bgee; ENSMUSG00000004789; Expressed in heart right ventricle and 302 other cell types or tissues.
DR   ExpressionAtlas; Q9D2G2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IMP:MGI.
DR   GO; GO:0016746; F:acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB.
DR   CDD; cd06849; lipoyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   NCBIfam; TIGR01347; sucB; 1.
DR   PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   UCD-2DPAGE; Q9D2G2; -.
DR   Genevisible; Q9D2G2; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Alternative splicing;
KW   Direct protein sequencing; Lipoyl; Mitochondrion; Nucleus; Phosphoprotein;
KW   Reference proteome; Transferase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT         1..68
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           69..454
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex,
FT                   mitochondrial"
FT                   /id="PRO_0000020473"
FT   DOMAIN          71..145
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   REGION          147..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..198
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        425
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0F1"
FT   ACT_SITE        429
FT                   /evidence="ECO:0000250|UniProtKB:Q9N0F1"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         111
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   MOD_RES         155
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         268
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         273
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         274
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         278
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         308
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   VAR_SEQ         1..253
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025015"
FT   VAR_SEQ         254..257
FT                   /note="EVDM -> MTSL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_025016"
FT   CONFLICT        276
FT                   /note="N -> S (in Ref. 1; BAE29011)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   454 AA;  48995 MW;  9CB31698D185442A CRC64;
     MLSRSRCVSR AFSRSLSAFQ KGNCPLGRRS LPGVSLCRGP GYPDNRKMVI NSGSVFRVRF
     FQTTAVCKND VITVQTPAFA ESVTEGDVRW EKAVGDAVAE DEVVCEIETD KTSVQVPSPA
     NGIIEALLVP DGGKVEGGTP LFTLRKTGAA PAKAKPAETP APAHKAEPAA PAAPPPPAAP
     VLTQMPPVPS PSQPPSSKPV SAIKPTAAPP LAEAGAAKGL RSEHREKMNR MRQRIAQRLK
     EAQNTCAMLT TFNEVDMSNI QEMRARHKDA FLKKHNLKLG FMSAFVKASA FALQEQPVVN
     AVIDDATKEV VYRDYIDISV AVATPRGLVV PVIRNVETMN YADIERTINE LGEKARKNEL
     AIEDMDGGTF TISNGGVFGS LFGTPIINPP QSAILGMHAI FDRPVAVGGK VEVRPMMYVA
     LTYDHRLIDG REAVTFLRKI KAAVEDPRVL LLDL
//