ID   BL1S1_HUMAN             Reviewed;         153 AA.
AC   P78537; A1L4Q9; Q6NZ45;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 2.
DT   04-NOV-2026, entry version 180.
DE   RecName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 1;
DE            Short=BLOC-1 subunit 1;
DE   AltName: Full=GCN5-like protein 1 {ECO:0000303|PubMed:38281616};
DE   AltName: Full=Protein RT14;
DE   AltName: Full=Protein acetyltransferase BLOC1S1 {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000305|PubMed:38281616};
GN   Name=BLOC1S1;
GN   Synonyms=BLOS1, GCN5L1 {ECO:0000303|PubMed:38281616}, RT14;
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 2).
RC   TISSUE=Fetal brain;
RX   PubMed=8770567; DOI=10.1093/dnares/2.5.235;
RA   Watanabe T.K., Fujiwara T., Shinomiya H., Kuga Y., Hishigaki H.,
RA   Nakamura Y., Hirai Y.;
RT   "Molecular cloning of a novel human cDNA, RT14, containing a putative ORF
RT   highly conserved between human, fruit fly, and nematode.";
RL   DNA Res. 2:235-237(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 11-153 (ISOFORM 1).
RX   PubMed=8646881; DOI=10.1159/000134324;
RA   Inoue M., Isomura M., Ikegawa S., Fujiwara T., Shin S., Moriya H.,
RA   Nakamura Y.;
RT   "Isolation and characterization of a human cDNA clone (GCN5L1) homologous
RT   to GCN5, a yeast transcription activator.";
RL   Cytogenet. Cell Genet. 73:134-136(1996).
RN   [5]
RP   IDENTIFICATION IN THE BLOC-1 COMPLEX.
RX   PubMed=15102850; DOI=10.1074/jbc.m402513200;
RA   Starcevic M., Dell'Angelica E.C.;
RT   "Identification of snapin and three novel proteins (BLOS1, BLOS2, and
RT   BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related
RT   organelles complex-1 (BLOC-1).";
RL   J. Biol. Chem. 279:28393-28401(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=17182842; DOI=10.1091/mbc.e06-12-1066;
RA   Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C.,
RA   Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
RA   Dell'Angelica E.C., Raposo G., Marks M.S.;
RT   "BLOC-1 is required for cargo-specific sorting from vacuolar early
RT   endosomes toward lysosome-related organelles.";
RL   Mol. Biol. Cell 18:768-780(2007).
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   FUNCTION IN MITOCHONDRIAL PROTEIN ACETYLATION, FUNCTION IN AEROBIC
RP   RESPIRATION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP5F1A AND NDUFA9.
RX   PubMed=22309213; DOI=10.1042/bj20120118;
RA   Scott I., Webster B.R., Li J.H., Sack M.N.;
RT   "Identification of a molecular component of the mitochondrial acetyl
RT   transferase program; a novel role for GCN5L1.";
RL   Biochem. J. 443:655-661(2012).
RN   [9]
RP   IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
RP   COMPLEX.
RX   PubMed=22203680; DOI=10.1074/jbc.m111.325746;
RA   Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C.,
RA   Bonifacino J.S., Hurley J.H.;
RT   "Assembly and architecture of biogenesis of lysosome-related organelles
RT   complex-1 (BLOC-1).";
RL   J. Biol. Chem. 287:5882-5890(2012).
RN   [10]
RP   FUNCTION, IDENTIFICATION OF THE BORC COMPLEX, AND SUBCELLULAR LOCATION.
RX   PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011;
RA   Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.;
RT   "BORC, a multisubunit complex that regulates lysosome positioning.";
RL   Dev. Cell 33:176-188(2015).
RN   [11]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=38281616; DOI=10.1016/j.cellsig.2024.111065;
RA   Bugga P., Manning J.R., Mushala B.A.S., Stoner M.W., Sembrat J., Scott I.;
RT   "GCN5L1-mediated acetylation prevents Rictor degradation in cardiac cells
RT   after hypoxic stress.";
RL   Cell. Signal. 116:111065-111065(2024).
CC   -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC       for normal biogenesis of lysosome-related organelles (LRO), such as
CC       platelet dense granules and melanosomes (PubMed:17182842). In concert
CC       with the AP-3 complex, the BLOC-1 complex is required to target
CC       membrane protein cargos into vesicles assembled at cell bodies for
CC       delivery into neurites and nerve terminals (PubMed:17182842). The BLOC-
CC       1 complex, in association with SNARE proteins, is also proposed to be
CC       involved in neurite extension (PubMed:17182842). As part of the BORC
CC       complex may play a role in lysosomes movement and localization at the
CC       cell periphery (PubMed:25898167). Associated with the cytosolic face of
CC       lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to
CC       microtubule plus-end-directed kinesin motor (PubMed:25898167).
CC       {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:25898167}.
CC   -!- FUNCTION: Acts as a protein acetyltransferase (PubMed:22309213,
CC       PubMed:38281616). Negatively regulates aerobic respiration through
CC       mitochondrial protein lysine-acetylation (PubMed:22309213). May
CC       counteract the action of the deacetylase SIRT3 by acetylating and
CC       regulating proteins of the mitochondrial respiratory chain including
CC       ATP5F1A and NDUFA9 (PubMed:22309213). Acts as a regulator of mTORC2
CC       signaling in response to hypotoxic stress by mediating acetylation of
CC       RICTOR, thereby protecting RICTOR against ubiquitination and subsequent
CC       degradation by the proteasome (PubMed:38281616).
CC       {ECO:0000269|PubMed:22309213, ECO:0000269|PubMed:38281616}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein]
CC         + CoA + H(+); Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000305|PubMed:38281616};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC         Evidence={ECO:0000305|PubMed:38281616};
CC   -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC       complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
CC       BLOC1S5, BLOC1S6, DTNBP1/BLOC1S8 and SNAPIN/BLOC1S7 (PubMed:15102850,
CC       PubMed:22203680). Octamer composed of one copy each BLOC1S1, BLOC1S2,
CC       BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S8 and SNAPIN/BLOC1S7
CC       (PubMed:15102850, PubMed:22203680). The BLOC-1 complex associates with
CC       the AP-3 protein complex and membrane protein cargos (By similarity).
CC       Component of the BLOC-one-related complex (BORC) which is composed of
CC       BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN
CC       (PubMed:25898167). Interacts with ATP5F1A and NDUFA9; involved in their
CC       acetylation on lysine residues (PubMed:22309213). Interacts with KXD1
CC       (By similarity). {ECO:0000250|UniProtKB:O55102,
CC       ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:22203680,
CC       ECO:0000269|PubMed:22309213, ECO:0000269|PubMed:25898167}.
CC   -!- INTERACTION:
CC       P78537; P25705: ATP5F1A; NbExp=2; IntAct=EBI-348630, EBI-351437;
CC       P78537; Q6QNY1: BLOC1S2; NbExp=5; IntAct=EBI-348630, EBI-465872;
CC       P78537; Q9UL45: BLOC1S6; NbExp=20; IntAct=EBI-348630, EBI-465781;
CC       P78537; Q13561: DCTN2; NbExp=3; IntAct=EBI-348630, EBI-715074;
CC       P78537; Q9H4M3-2: FBXO44; NbExp=3; IntAct=EBI-348630, EBI-12104696;
CC       P78537; O14964: HGS; NbExp=3; IntAct=EBI-348630, EBI-740220;
CC       P78537; O15481: MAGEB4; NbExp=3; IntAct=EBI-348630, EBI-751857;
CC       P78537; Q16795: NDUFA9; NbExp=3; IntAct=EBI-348630, EBI-1045087;
CC       P78537; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-348630, EBI-12004298;
CC       P78537; O95295: SNAPIN; NbExp=8; IntAct=EBI-348630, EBI-296723;
CC       P78537; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-348630, EBI-739895;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space
CC       {ECO:0000269|PubMed:22309213}. Mitochondrion matrix
CC       {ECO:0000269|PubMed:22309213}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:22309213}. Lysosome membrane
CC       {ECO:0000305|PubMed:25898167}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=P78537-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P78537-2; Sequence=VSP_040954;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced by alternative initiation
CC       at Met-27 of isoform 1. A polymorphism at position 9 leads to the
CC       creation of a stop codon. Isoform 2 is the only form that exists in
CC       orthologs (except primates). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BLOC1S1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB37682.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D64007; BAA10887.1; -; mRNA.
DR   EMBL; AC009779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC130640; AAI30641.1; -; mRNA.
DR   EMBL; BC132795; AAI32796.1; -; mRNA.
DR   EMBL; S82447; AAB37682.1; ALT_INIT; mRNA.
DR   CCDS; CCDS8889.2; -. [P78537-1]
DR   PIR; JC4392; JC4392.
DR   RefSeq; NP_001478.2; NM_001487.4. [P78537-1]
DR   AlphaFoldDB; P78537; -.
DR   SMR; P78537; -.
DR   BioGRID; 108917; 53.
DR   ComplexPortal; CPX-1910; BLOC-1 complex.
DR   ComplexPortal; CPX-5029; BORC complex.
DR   CORUM; P78537; -.
DR   FunCoup; P78537; 489.
DR   IntAct; P78537; 41.
DR   NDEx; IQUERY-CP-BLOC1S1; 2 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000447537; -.
DR   iPTMnet; P78537; -.
DR   PhosphoSitePlus; P78537; -.
DR   BioMuta; BLOC1S1; -.
DR   DMDM; 332278161; -.
DR   jPOST; P78537; -.
DR   MassIVE; P78537; -.
DR   PaxDb; 9606-ENSP00000447537; -.
DR   PeptideAtlas; P78537; -.
DR   ProteomicsDB; 57639; -. [P78537-1]
DR   ProteomicsDB; 57640; -. [P78537-2]
DR   Pumba; P78537; -.
DR   Antibodypedia; 15519; 97 antibodies from 20 providers.
DR   DNASU; 2647; -.
DR   Ensembl; ENST00000548925.6; ENSP00000447537.1; ENSG00000135441.9. [P78537-1]
DR   GeneID; 2647; -.
DR   KEGG; hsa:2647; -.
DR   MANE-Select; ENST00000548925.6; ENSP00000447537.1; NM_001487.4; NP_001478.2.
DR   UCSC; uc001shi.5; human. [P78537-1]
DR   AGR; HGNC:4200; -.
DR   ClinPGx; PA28617; -.
DR   CTD; 2647; -.
DR   DisGeNET; 2647; -.
DR   GeneCards; BLOC1S1; -.
DR   HGNC; HGNC:4200; BLOC1S1.
DR   HPA; ENSG00000135441; Low tissue specificity.
DR   MIM; 601444; gene.
DR   OpenTargets; ENSG00000135441; -.
DR   VEuPathDB; HostDB:ENSG00000135441; -.
DR   eggNOG; KOG3390; Eukaryota.
DR   GeneTree; ENSGT00390000002689; -.
DR   HOGENOM; CLU_115602_3_0_1; -.
DR   InParanoid; P78537; -.
DR   OMA; AATCLMG; -.
DR   OrthoDB; 20018at2759; -.
DR   PAN-GO; P78537; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; P78537; -.
DR   PathwayCommons; P78537; -.
DR   Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR   SignaLink; P78537; -.
DR   SIGNOR; P78537; -.
DR   Agora; ENSG00000135441; Agora Nominated Target for Alzheimer's Disease.
DR   BioGRID-ORCS; 2647; 18 hits in 1146 CRISPR screens.
DR   GeneWiki; BLOC1S1; -.
DR   GenomeRNAi; 2647; -.
DR   Pharos; P78537; Tbio.
DR   PRO; PR:P78537; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P78537; protein.
DR   Bgee; ENSG00000135441; Expressed in mucosa of transverse colon and 100 other cell types or tissues.
DR   ExpressionAtlas; P78537; baseline and differential.
DR   GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR   GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR   GO; GO:0099078; C:BORC complex; IDA:UniProtKB.
DR   GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR   GO; GO:0005576; C:extracellular region; HDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0061733; F:protein-lysine-acetyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; IMP:UniProtKB.
DR   GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR   GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR   GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0072384; P:organelle transport along microtubule; NAS:ComplexPortal.
DR   GO; GO:0060155; P:platelet dense granule organization; NAS:UniProtKB.
DR   GO; GO:0051036; P:regulation of endosome size; NAS:ComplexPortal.
DR   GO; GO:0062196; P:regulation of lysosome size; NAS:ComplexPortal.
DR   InterPro; IPR009395; BLOC1S1.
DR   PANTHER; PTHR13073:SF0; BIOGENESIS OF LYSOSOME-RELATED ORGANELLES COMPLEX 1 SUBUNIT 1; 1.
DR   PANTHER; PTHR13073; BLOC-1 COMPLEX SUBUNIT 1; 1.
DR   Pfam; PF06320; GCN5L1; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Coiled coil; Cytoplasm; Lysosome; Membrane;
KW   Mitochondrion; Proteomics identification; Reference proteome; Transferase.
FT   CHAIN           1..153
FT                   /note="Biogenesis of lysosome-related organelles complex 1
FT                   subunit 1"
FT                   /id="PRO_0000156331"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          27..59
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..11
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..28
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:8770567"
FT                   /id="VSP_040954"
SQ   SEQUENCE   153 AA;  17263 MW;  B7D1FE64F242B25A CRC64;
     MAPGSRGERS SFRSRRGPGV PSPQPDVTML SRLLKEHQAK QNERKELQEK RRREAITAAT
     CLTEALVDHL NVGVAQAYMN QRKLDHEVKT LQVQAAQFAK QTGQWIGMVE NFNQALKEIG
     DVENWARSIE LDMRTIATAL EYVYKGQLQS APS
//