ID RB39B_HUMAN Reviewed; 213 AA. AC Q96DA2; Q5JT79; Q8NEX3; DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 12-SEP-2018, entry version 151. DE RecName: Full=Ras-related protein Rab-39B; GN Name=RAB39B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal brain; RX PubMed=12438742; DOI=10.1159/000064047; RA Cheng H., Ma Y., Ni X., Jiang M., Guo L., Ying K., Xie Y., Mao Y.; RT "Isolation and characterization of a human novel RAB (RAB39B) gene."; RL Cytogenet. Genome Res. 97:72-75(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Pancreas; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN MRX72. RX PubMed=20159109; DOI=10.1016/j.ajhg.2010.01.011; RA Giannandrea M., Bianchi V., Mignogna M.L., Sirri A., Carrabino S., RA D'Elia E., Vecellio M., Russo S., Cogliati F., Larizza L., RA Ropers H.H., Tzschach A., Kalscheuer V., Oehl-Jaschkowitz B., RA Skinner C., Schwartz C.E., Gecz J., Van Esch H., Raynaud M., RA Chelly J., de Brouwer A.P., Toniolo D., D'Adamo P.; RT "Mutations in the small GTPase gene RAB39B are responsible for X- RT linked mental retardation associated with autism, epilepsy, and RT macrocephaly."; RL Am. J. Hum. Genet. 86:185-195(2010). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=24349490; DOI=10.1371/journal.pone.0083324; RA Seto S., Sugaya K., Tsujimura K., Nagata T., Horii T., Koide Y.; RT "Rab39a interacts with phosphatidylinositol 3-kinase and negatively RT regulates autophagy induced by lipopolysaccharide stimulation in RT macrophages."; RL PLoS ONE 8:E83324-E83324(2013). RN [7] RP INTERACTION WITH PICK1. RX PubMed=25784538; DOI=10.1038/ncomms7504; RA Mignogna M.L., Giannandrea M., Gurgone A., Fanelli F., Raimondi F., RA Mapelli L., Bassani S., Fang H., Van Anken E., Alessio M., RA Passafaro M., Gatti S., Esteban J.A., Huganir R., D'Adamo P.; RT "The intellectual disability protein RAB39B selectively regulates RT GluA2 trafficking to determine synaptic AMPAR composition."; RL Nat. Commun. 6:6504-6504(2015). RN [8] RP INVOLVEMENT IN WSMN, VARIANT WSMN LYS-168, AND CHARACTERIZATION OF RP VARIANT WSMN LYS-168. RX PubMed=25434005; DOI=10.1016/j.ajhg.2014.10.015; RA Wilson G.R., Sim J.C., McLean C., Giannandrea M., Galea C.A., RA Riseley J.R., Stephenson S.E., Fitzpatrick E., Haas S.A., Pope K., RA Hogan K.J., Gregg R.G., Bromhead C.J., Wargowski D.S., Lawrence C.H., RA James P.A., Churchyard A., Gao Y., Phelan D.G., Gillies G., Salce N., RA Stanford L., Marsh A.P., Mignogna M.L., Hayflick S.J., Leventer R.J., RA Delatycki M.B., Mellick G.D., Kalscheuer V.M., D'Adamo P., Bahlo M., RA Amor D.J., Lockhart P.J.; RT "Mutations in RAB39B cause X-linked intellectual disability and early- RT onset Parkinson disease with alpha-synuclein pathology."; RL Am. J. Hum. Genet. 95:729-735(2014). RN [9] RP FUNCTION, AND MUTAGENESIS OF SER-22 AND GLN-68. RX PubMed=27103069; DOI=10.15252/embj.201593350; RA Sellier C., Campanari M.L., Julie Corbier C., Gaucherot A., RA Kolb-Cheynel I., Oulad-Abdelghani M., Ruffenach F., Page A., Ciura S., RA Kabashi E., Charlet-Berguerand N.; RT "Loss of C9ORF72 impairs autophagy and synergizes with polyQ Ataxin-2 RT to induce motor neuron dysfunction and cell death."; RL EMBO J. 35:1276-1297(2016). RN [10] RP DISCUSSION ON INVOLVEMENT IN WSMN. RX PubMed=27459931; DOI=10.1016/j.neurobiolaging.2016.03.021; RA Hodges K., Brewer S.S., Labbe C., Soto-Ortolaza A.I., Walton R.L., RA Strongosky A.J., Uitti R.J., van Gerpen J.A., Ertekin-Taner N., RA Kantarci K., Lowe V.J., Parisi J.E., Savica R., Graff-Radford J., RA Jones D.T., Knopman D.S., Petersen R.C., Murray M.E., RA Graff-Radford N.R., Ferman T.J., Dickson D.W., Wszolek Z.K., RA Boeve B.F., Ross O.A., Lorenzo-Betancor O.; RT "RAB39B gene mutations are not a common cause of Parkinson's disease RT or dementia with Lewy bodies."; RL Neurobiol. Aging 45:107-108(2016). RN [11] RP DISCUSSION ON INVOLVEMENT IN WSMN. RX PubMed=26739247; DOI=10.1016/j.parkreldis.2015.12.014; RA Loechte T., Brueggemann N., Vollstedt E.J., Krause P., Domingo A., RA Rosales R., Lee L.V., Hopfner F., Westenberger A., Kuehn A., Klein C., RA Lohmann K.; RT "RAB39B mutations are a rare finding in Parkinson disease patients."; RL Parkinsonism Relat. Disord. 23:116-117(2016). RN [12] RP VARIANT WSMN ARG-192, AND SUBCELLULAR LOCATION. RX PubMed=26399558; DOI=10.1186/s13024-015-0045-4; RA Mata I.F., Jang Y., Kim C.H., Hanna D.S., Dorschner M.O., Samii A., RA Agarwal P., Roberts J.W., Klepitskaya O., Shprecher D.R., Chung K.A., RA Factor S.A., Espay A.J., Revilla F.J., Higgins D.S., Litvan I., RA Leverenz J.B., Yearout D., Inca-Martinez M., Martinez E., RA Thompson T.R., Cholerton B.A., Hu S.C., Edwards K.L., Kim K.S., RA Zabetian C.P.; RT "The RAB39B p.G192R mutation causes X-linked dominant Parkinson's RT disease."; RL Mol. Neurodegener. 10:50-50(2015). RN [13] RP VARIANT WSMN 186-TRP--CYS-213 DEL. RX PubMed=27066548; DOI=10.1212/NXG.0000000000000009; RG French Parkinson's Disease Genetics Study Group (PDG) and the International Parkinson's Disease Genomics Consortium (IPDGC); RA Lesage S., Bras J., Cormier-Dequaire F., Condroyer C., Nicolas A., RA Darwent L., Guerreiro R., Majounie E., Federoff M., Heutink P., RA Wood N.W., Gasser T., Hardy J., Tison F., Singleton A., Brice A.; RT "Loss-of-function mutations in RAB39B are associated with typical RT early-onset Parkinson disease."; RL Neurol. Genet. 1:E9-E9(2015). CC -!- FUNCTION: Small GTPases Rab involved in autophagy CC (PubMed:27103069). The small GTPases Rab are key regulators of CC intracellular membrane trafficking, from the formation of CC transport vesicles to their fusion with membranes. Rabs cycle CC between an inactive GDP-bound form and an active GTP-bound form CC that is able to recruit to membranes different sets of downstream CC effectors directly responsible for vesicle formation, movement, CC tethering and fusion (PubMed:27103069). May regulate the CC homeostasis of SNCA/alpha-synuclein. Together with PICK1 proposed CC to ensure selectively GRIA2 exit from the endoplasmic reticulum to CC the Golgi and to regulate AMPAR compostion at the post-synapses CC and thus synaptic transmission (By similarity). CC {ECO:0000250|UniProtKB:Q8BHC1, ECO:0000269|PubMed:27103069}. CC -!- SUBUNIT: Interacts (in GTP-bound form) with PICK1 (via PDZ CC domain); a PICK1 homodimer may allow simultaneous association of CC RAB39B and GRIA2 to PICK1 which is involved in GRIA2 trafficking. CC {ECO:0000269|PubMed:25784538}. CC -!- INTERACTION: CC Q08379:GOLGA2; NbExp=3; IntAct=EBI-9089467, EBI-618309; CC Q96T51:RUFY1; NbExp=3; IntAct=EBI-9089467, EBI-3941207; CC Q8IUH5:ZDHHC17; NbExp=3; IntAct=EBI-9089467, EBI-524753; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle CC membrane {ECO:0000269|PubMed:26399558}; Lipid-anchor CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus CC {ECO:0000269|PubMed:20159109, ECO:0000269|PubMed:24349490}. CC Note=Partial colocalization with markers that cycle from the cell CC surface to the trans-Golgi network. CC {ECO:0000250|UniProtKB:Q8BHC1}. CC -!- TISSUE SPECIFICITY: Highly expressed in the brain. CC {ECO:0000269|PubMed:20159109}. CC -!- DISEASE: Mental retardation, X-linked 72 (MRX72) [MIM:300271]: A CC disorder characterized by significantly below average general CC intellectual functioning associated with impairments in adaptive CC behavior and manifested during the developmental period. CC Intellectual deficiency is the only primary symptom of non- CC syndromic X-linked mental retardation, while syndromic mental CC retardation presents with associated physical, neurological and/or CC psychiatric manifestations. MRX72 patients can manifest autism CC spectrum disorder, seizures and macrocephaly as additional CC features. {ECO:0000269|PubMed:20159109}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- DISEASE: Waisman syndrome (WSMN) [MIM:311510]: A neurologic CC disorder characterized by delayed psychomotor development, CC intellectual disability, and early-onset Parkinson disease. CC {ECO:0000269|PubMed:25434005, ECO:0000269|PubMed:26399558, CC ECO:0000269|PubMed:27066548}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. Its CC association with Parkinson disease is however unclear CC (PubMed:26739247, PubMed:27459931). According to a number of CC studies, variations affecting this gene are not a frequent cause CC of Parkinson disease, suggesting that RAB39B does not play a major CC role in Parkinson disease etiology (PubMed:26739247, CC PubMed:27459931). {ECO:0000269|PubMed:26739247, CC ECO:0000269|PubMed:27459931}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY052478; AAL12244.1; -; mRNA. DR EMBL; AL834460; CAD39120.1; -; mRNA. DR EMBL; AL356738; CAI41468.1; -; Genomic_DNA. DR EMBL; BC009714; AAH09714.1; -; mRNA. DR CCDS; CCDS14766.1; -. DR RefSeq; NP_741995.1; NM_171998.3. DR UniGene; Hs.632832; -. DR ProteinModelPortal; Q96DA2; -. DR SMR; Q96DA2; -. DR BioGrid; 125507; 30. DR IntAct; Q96DA2; 5. DR STRING; 9606.ENSP00000358466; -. DR iPTMnet; Q96DA2; -. DR PhosphoSitePlus; Q96DA2; -. DR DMDM; 27734447; -. DR EPD; Q96DA2; -. DR MaxQB; Q96DA2; -. DR PaxDb; Q96DA2; -. DR PeptideAtlas; Q96DA2; -. DR PRIDE; Q96DA2; -. DR ProteomicsDB; 76264; -. DR DNASU; 116442; -. DR Ensembl; ENST00000369454; ENSP00000358466; ENSG00000155961. DR GeneID; 116442; -. DR KEGG; hsa:116442; -. DR UCSC; uc004fne.5; human. DR CTD; 116442; -. DR DisGeNET; 116442; -. DR EuPathDB; HostDB:ENSG00000155961.4; -. DR GeneCards; RAB39B; -. DR HGNC; HGNC:16499; RAB39B. DR HPA; HPA001114; -. DR HPA; HPA042505; -. DR MalaCards; RAB39B; -. DR MIM; 300271; phenotype. DR MIM; 300774; gene. DR MIM; 311510; phenotype. DR neXtProt; NX_Q96DA2; -. DR OpenTargets; ENSG00000155961; -. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA34131; -. DR eggNOG; KOG0091; Eukaryota. DR eggNOG; ENOG410ZQFG; LUCA. DR GeneTree; ENSGT00760000118841; -. DR HOGENOM; HOG000233968; -. DR HOVERGEN; HBG009351; -. DR InParanoid; Q96DA2; -. DR KO; K07925; -. DR OMA; FIETSSR; -. DR OrthoDB; EOG091G0RUB; -. DR PhylomeDB; Q96DA2; -. DR TreeFam; TF300032; -. DR Reactome; R-HSA-8873719; RAB geranylgeranylation. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR GeneWiki; RAB39B; -. DR GenomeRNAi; 116442; -. DR PRO; PR:Q96DA2; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000155961; Expressed in 120 organ(s), highest expression level in endothelial cell. DR CleanEx; HS_RAB39B; -. DR Genevisible; Q96DA2; HS. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005622; C:intracellular; IDA:LIFEdb. DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0031982; C:vesicle; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IEA:InterPro. DR GO; GO:0031489; F:myosin V binding; IPI:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB. DR GO; GO:0050808; P:synapse organization; ISS:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; ISS:UniProtKB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR Pfam; PF00071; Ras; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW Autism spectrum disorder; Autophagy; Cell membrane; Complete proteome; KW Cytoplasmic vesicle; Disease mutation; Golgi apparatus; GTP-binding; KW Lipoprotein; Membrane; Mental retardation; Methylation; KW Nucleotide-binding; Parkinson disease; Phosphoprotein; Prenylation; KW Protein transport; Reference proteome; Transport. FT CHAIN 1 213 Ras-related protein Rab-39B. FT /FTId=PRO_0000121255. FT NP_BIND 15 22 GTP. {ECO:0000250}. FT NP_BIND 64 68 GTP. {ECO:0000250}. FT NP_BIND 123 126 GTP. {ECO:0000250}. FT MOTIF 37 45 Effector region. {ECO:0000250}. FT MOD_RES 201 201 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8BHC1}. FT MOD_RES 213 213 Cysteine methyl ester. {ECO:0000250}. FT LIPID 211 211 S-geranylgeranyl cysteine. {ECO:0000250}. FT LIPID 213 213 S-geranylgeranyl cysteine. {ECO:0000250}. FT VARIANT 168 168 T -> K (in WSMN; loss of function FT mutation; expression of the mutation in FT neuroblastoma cells results in low levels FT of the mutant protein; FT dbSNP:rs587777874). FT {ECO:0000269|PubMed:25434005}. FT /FTId=VAR_073264. FT VARIANT 186 213 Missing (in WSMN). FT {ECO:0000269|PubMed:27066548}. FT /FTId=VAR_078514. FT VARIANT 192 192 G -> R (in WSMN; impaired localization to FT cytoplasmic vesicles; dbSNP:rs864309527). FT {ECO:0000269|PubMed:26399558}. FT /FTId=VAR_078515. FT MUTAGEN 22 22 S->N: Dominant negative mutant. FT {ECO:0000269|PubMed:27103069}. FT MUTAGEN 68 68 Q->L: Constitutively active mutant locked FT in the active GTP-bound form. FT {ECO:0000269|PubMed:27103069}. FT CONFLICT 57 57 R -> T (in Ref. 1; AAL12244). FT {ECO:0000305}. SQ SEQUENCE 213 AA; 24622 MW; 2B2C5B35C61FA88E CRC64; MEAIWLYQFR LIVIGDSTVG KSCLIRRFTE GRFAQVSDPT VGVDFFSRLV EIEPGKRIKL QIWDTAGQER FRSITRAYYR NSVGGLLLFD ITNRRSFQNV HEWLEETKVH VQPYQIVFVL VGHKCDLDTQ RQVTRHEAEK LAAAYGMKYI ETSARDAINV EKAFTDLTRD IYELVKRGEI TIQEGWEGVK SGFVPNVVHS SEEVVKSERR CLC //