STX16_HUMAN
ID STX16_HUMAN Reviewed; 325 AA.
AC O14662; A6NK32; A6NN69; A8MPP0; B7ZBN1; B7ZBN2; B7ZBN3; E1P5M0; E1P607;
AC O14661; O14663; O60517; Q5W084; Q5W086; Q5W087; Q5XKI6; Q6GMS8; Q9H0Z0;
AC Q9H1T7; Q9H1T8; Q9UIX5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Syntaxin-16;
DE Short=Syn16;
GN Name=STX16;
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] (ISOFORMS A; B; C AND D).
RC TISSUE=Brain;
RX PubMed=9587053; DOI=10.1016/s0171-9335(98)80116-7;
RA Simonsen A., Bremnes B., Ronning E., Aasland R., Stenmark H.;
RT "Syntaxin-16, a putative Golgi t-SNARE.";
RL Eur. J. Cell Biol. 75:223-231(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
RX PubMed=9464276; DOI=10.1006/bbrc.1997.8029;
RA Tang B.L., Low D.Y.H., Lee S.S., Tan A.E.H., Ho W.;
RT "Molecular cloning and localization of human syntaxin 16, a member of the
RT syntaxin family of SNARE proteins.";
RL Biochem. Biophys. Res. Commun. 242:673-679(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND E).
RC TISSUE=Kidney;
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 [LARGE SCALE MRNA] OF 1-251 (ISOFORM 6).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INVOLVEMENT IN PHP1B.
RX PubMed=14561710; DOI=10.1172/jci200319159;
RA Bastepe M., Froehlich L.F., Hendy G.N., Indridason O.S., Josse R.G.,
RA Koshiyama H., Koerkkoe J., Nakamoto J.M., Rosenbloom A.L., Slyper A.H.,
RA Sugimoto T., Tsatsoulis A., Crawford J.D., Jueppner H.;
RT "Autosomal dominant pseudohypoparathyroidism type Ib is associated with a
RT heterozygous microdeletion that likely disrupts a putative imprinting
RT control element of GNAS.";
RL J. Clin. Invest. 112:1255-1263(2003).
RN [8]
RP INVOLVEMENT IN PHP1B.
RX PubMed=15800843; DOI=10.1086/429932;
RA Linglart A., Gensure R.C., Olney R.C., Jueppner H., Bastepe M.;
RT "A novel STX16 deletion in autosomal dominant pseudohypoparathyroidism type
RT Ib redefines the boundaries of a cis-acting imprinting control element of
RT GNAS.";
RL Am. J. Hum. Genet. 76:804-814(2005).
RN [9]
RP FUNCTION, AND INTERACTION WITH GCC2.
RX PubMed=18195106; DOI=10.1083/jcb.200707136;
RA Ganley I.G., Espinosa E., Pfeffer S.R.;
RT "A syntaxin 10-SNARE complex distinguishes two distinct transport routes
RT from endosomes to the trans-Golgi in human cells.";
RL J. Cell Biol. 180:159-172(2008).
RN [10]
RP INTERACTION WITH BAIAP3.
RX PubMed=28626000; DOI=10.1083/jcb.201702099;
RA Zhang X., Jiang S., Mitok K.A., Li L., Attie A.D., Martin T.F.J.;
RT "BAIAP3, a C2 domain-containing Munc13 protein, controls the fate of dense-
RT core vesicles in neuroendocrine cells.";
RL J. Cell Biol. 216:2151-2166(2017).
CC -!- FUNCTION: SNARE involved in vesicular transport from the late endosomes
CC to the trans-Golgi network. {ECO:0000269|PubMed:18195106}.
CC -!- SUBUNIT: Interacts with GCC2 (PubMed:18195106). Interacts with BAIAP3;
CC this interaction is increased in the presence of calcium
CC (PubMed:28626000). {ECO:0000269|PubMed:18195106,
CC ECO:0000269|PubMed:28626000}.
CC -!- INTERACTION:
CC O14662; P50222: MEOX2; NbExp=3; IntAct=EBI-2853548, EBI-748397;
CC O14662; Q9H115: NAPB; NbExp=3; IntAct=EBI-2853548, EBI-3921185;
CC O14662; Q12846: STX4; NbExp=3; IntAct=EBI-2853548, EBI-744942;
CC O14662; O95183: VAMP5; NbExp=4; IntAct=EBI-2853548, EBI-10191195;
CC O14662-5; P05067: APP; NbExp=3; IntAct=EBI-9089968, EBI-77613;
CC O14662-5; P42858: HTT; NbExp=15; IntAct=EBI-9089968, EBI-466029;
CC O14662-5; Q9H115: NAPB; NbExp=3; IntAct=EBI-9089968, EBI-3921185;
CC O14662-5; O95721: SNAP29; NbExp=3; IntAct=EBI-9089968, EBI-490676;
CC O14662-5; Q16623: STX1A; NbExp=3; IntAct=EBI-9089968, EBI-712466;
CC O14662-5; P32856-2: STX2; NbExp=3; IntAct=EBI-9089968, EBI-11956649;
CC O14662-5; Q12846: STX4; NbExp=3; IntAct=EBI-9089968, EBI-744942;
CC O14662-5; O75379: VAMP4; NbExp=3; IntAct=EBI-9089968, EBI-744953;
CC O14662-5; O95183: VAMP5; NbExp=3; IntAct=EBI-9089968, EBI-10191195;
CC O14662-5; Q9NRW7: VPS45; NbExp=3; IntAct=EBI-9089968, EBI-1782543;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type IV
CC membrane protein.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=B;
CC IsoId=O14662-1; Sequence=Displayed;
CC Name=A;
CC IsoId=O14662-2; Sequence=VSP_006348;
CC Name=C;
CC IsoId=O14662-3; Sequence=VSP_006349, VSP_006350, VSP_006351;
CC Name=D;
CC IsoId=O14662-4; Sequence=VSP_006349;
CC Name=E;
CC IsoId=O14662-5; Sequence=VSP_043849;
CC Name=6;
CC IsoId=O14662-6; Sequence=VSP_045073;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Pseudohypoparathyroidism 1B (PHP1B) [MIM:603233]: A disorder
CC characterized by end-organ resistance to parathyroid hormone,
CC hypocalcemia and hyperphosphatemia. Patients affected with PHP1B lack
CC developmental defects characteristic of Albright hereditary
CC osteodystrophy, and typically show no other endocrine abnormalities
CC besides resistance to PTH. {ECO:0000269|PubMed:14561710,
CC ECO:0000269|PubMed:15800843}. Note=The gene represented in this entry
CC is involved in disease pathogenesis. Microdeletions involving STX16 can
CC cause loss of methylation at exon A/B of GNAS, resulting in PHP1B.
CC -!- MISCELLANEOUS: [Isoform C]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB69282.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB69283.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC05647.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF008936; AAB69283.1; ALT_FRAME; mRNA.
DR EMBL; AF008935; AAB69282.1; ALT_FRAME; mRNA.
DR EMBL; AF008937; AAB69284.1; -; mRNA.
DR EMBL; AF038897; AAC05647.1; ALT_FRAME; mRNA.
DR EMBL; AL139349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL050327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75481.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75482.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75484.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75485.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75486.1; -; Genomic_DNA.
DR EMBL; BC019042; AAH19042.1; -; mRNA.
DR EMBL; BC073876; AAH73876.1; -; mRNA.
DR EMBL; BX396221; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13468.1; -. [O14662-1]
DR CCDS; CCDS13469.1; -. [O14662-2]
DR CCDS; CCDS46619.1; -. [O14662-5]
DR CCDS; CCDS46620.1; -. [O14662-4]
DR CCDS; CCDS56199.1; -. [O14662-6]
DR PIR; JC5927; JC5927.
DR RefSeq; NP_001001433.1; NM_001001433.2. [O14662-1]
DR RefSeq; NP_001128244.1; NM_001134772.2. [O14662-5]
DR RefSeq; NP_001128245.1; NM_001134773.2. [O14662-4]
DR RefSeq; NP_001191797.1; NM_001204868.1. [O14662-6]
DR RefSeq; NP_003754.2; NM_003763.5. [O14662-2]
DR AlphaFoldDB; O14662; -.
DR SMR; O14662; -.
DR BioGRID; 114223; 61.
DR CORUM; O14662; -.
DR DIP; DIP-57570N; -.
DR IntAct; O14662; 28.
DR MINT; O14662; -.
DR STRING; 9606.ENSP00000360183; -.
DR iPTMnet; O14662; -.
DR PhosphoSitePlus; O14662; -.
DR BioMuta; STX16; -.
DR EPD; O14662; -.
DR jPOST; O14662; -.
DR MassIVE; O14662; -.
DR MaxQB; O14662; -.
DR PaxDb; O14662; -.
DR PeptideAtlas; O14662; -.
DR PRIDE; O14662; -.
DR ProteomicsDB; 15209; -.
DR ProteomicsDB; 48155; -. [O14662-1]
DR ProteomicsDB; 48156; -. [O14662-2]
DR ProteomicsDB; 48157; -. [O14662-3]
DR ProteomicsDB; 48158; -. [O14662-4]
DR ProteomicsDB; 48159; -. [O14662-5]
DR Antibodypedia; 29123; 169 antibodies from 27 providers.
DR DNASU; 8675; -.
DR Ensembl; ENST00000355957.9; ENSP00000348229.5; ENSG00000124222.22. [O14662-4]
DR Ensembl; ENST00000358029.8; ENSP00000350723.4; ENSG00000124222.22. [O14662-5]
DR Ensembl; ENST00000359617.8; ENSP00000352634.4; ENSG00000124222.22. [O14662-6]
DR Ensembl; ENST00000361830.7; ENSP00000354445.4; ENSG00000124222.22. [O14662-6]
DR Ensembl; ENST00000371132.8; ENSP00000360173.4; ENSG00000124222.22. [O14662-2]
DR Ensembl; ENST00000371141.8; ENSP00000360183.4; ENSG00000124222.22. [O14662-1]
DR Ensembl; ENST00000467096.5; ENSP00000434369.1; ENSG00000124222.22. [O14662-3]
DR GeneID; 8675; -.
DR KEGG; hsa:8675; -.
DR MANE-Select; ENST00000371141.8; ENSP00000360183.4; NM_001001433.3; NP_001001433.1.
DR UCSC; uc002xzi.4; human. [O14662-1]
DR CTD; 8675; -.
DR DisGeNET; 8675; -.
DR GeneCards; STX16; -.
DR GeneReviews; STX16; -.
DR HGNC; HGNC:11431; STX16.
DR HPA; ENSG00000124222; Low tissue specificity.
DR MalaCards; STX16; -.
DR MIM; 603233; phenotype.
DR MIM; 603666; gene.
DR neXtProt; NX_O14662; -.
DR OpenTargets; ENSG00000124222; -.
DR Orphanet; 94089; Pseudohypoparathyroidism type 1B.
DR PharmGKB; PA36231; -.
DR VEuPathDB; HostDB:ENSG00000124222; -.
DR eggNOG; KOG0809; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_038177_3_0_1; -.
DR InParanoid; O14662; -.
DR OMA; QTMIIDQ; -.
DR OrthoDB; 1182451at2759; -.
DR PhylomeDB; O14662; -.
DR TreeFam; TF314090; -.
DR PathwayCommons; O14662; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; O14662; -.
DR SIGNOR; O14662; -.
DR BioGRID-ORCS; 8675; 12 hits in 1081 CRISPR screens.
DR GeneWiki; STX16; -.
DR GenomeRNAi; 8675; -.
DR Pharos; O14662; Tbio.
DR PRO; PR:O14662; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O14662; protein.
DR Bgee; ENSG00000124222; Expressed in right uterine tube and 205 other tissues.
DR ExpressionAtlas; O14662; baseline and differential.
DR Genevisible; O14662; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC-UCL.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0090161; P:Golgi ribbon formation; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:UniProtKB.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028673; STX16.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR006011; Syntaxin_N.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF83; PTHR19957:SF83; 1.
DR Pfam; PF05739; SNARE; 1.
DR Pfam; PF00804; Syntaxin; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..325
FT /note="Syntaxin-16"
FT /id="PRO_0000210226"
FT TOPO_DOM 1..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..325
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 230..292
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVI5"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_045073"
FT VAR_SEQ 28..48
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9587053"
FT /id="VSP_006348"
FT VAR_SEQ 28..44
FT /note="Missing (in isoform C and isoform D)"
FT /evidence="ECO:0000303|PubMed:9464276,
FT ECO:0000303|PubMed:9587053"
FT /id="VSP_006349"
FT VAR_SEQ 45..48
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043849"
FT VAR_SEQ 132
FT /note="L -> A (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9587053"
FT /id="VSP_006350"
FT VAR_SEQ 133..325
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:9587053"
FT /id="VSP_006351"
FT CONFLICT 99
FT /note="L -> S (in Ref. 1; AAB69282/AAB69283)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="A -> E (in Ref. 1; AAC05647)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="I -> M (in Ref. 1; AAB69282/AAB69283)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 37031 MW; 65F566541A042C3C CRC64;
MATRRLTDAF LLLRNNSIQN RQLLAEQVSS HITSSPLHSR SIAAELDELA DDRMALVSGI
SLDPEAAIGV TKRPPPKWVD GVDEIQYDVG RIKQKMKELA SLHDKHLNRP TLDDSSEEEH
AIEITTQEIT QLFHRCQRAV QALPSRARAC SEQEGRLLGN VVASLAQALQ ELSTSFRHAQ
SGYLKRMKNR EERSQHFFDT SVPLMDDGDD NTLYHRGFTE DQLVLVEQNT LMVEEREREI
RQIVQSISDL NEIFRDLGAM IVEQGTVLDR IDYNVEQSCI KTEDGLKQLH KAEQYQKKNR
KMLVILILFV IIIVLIVVLV GVKSR
