ID SPTC1_HUMAN Reviewed; 473 AA. AC O15269; A8K681; Q5VWB4; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 25-JAN-2012, entry version 111. DE RecName: Full=Serine palmitoyltransferase 1; DE EC=2.3.1.50; DE AltName: Full=Long chain base biosynthesis protein 1; DE Short=LCB 1; DE AltName: Full=Serine-palmitoyl-CoA transferase 1; DE Short=SPT 1; DE Short=SPT1; GN Name=SPTLC1; Synonyms=LCB1; 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=Kidney; RX MEDLINE=98028405; PubMed=9363775; RX DOI=10.1111/j.1432-1033.1997.00239.x; RA Weiss B., Stoffel W.; RT "Human and murine serine-palmitoyl-CoA transferase. Cloning, RT expression and characterization of the key enzyme in sphingolipid RT synthesis."; RL Eur. J. Biochem. 249:239-247(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS HSAN1A TRP-133; RP TYR-133 AND ASP-144. RX MEDLINE=21135094; PubMed=11242114; DOI=10.1038/85879; RA Dawkins J.L., Hulme D.J., Brahmbhatt S.B., Auer-Grumbach M., RA Nicholson G.A.; RT "Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain RT base subunit-1, cause hereditary sensory neuropathy type I."; RL Nat. Genet. 27:309-312(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., RA Rogers J., Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP TISSUE SPECIFICITY. RX PubMed=17023427; DOI=10.1074/jbc.M608066200; RA Hornemann T., Richard S., Ruetti M.F., Wei Y., von Eckardstein A.; RT "Cloning and initial characterization of a new subunit for mammalian RT serine-palmitoyltransferase."; RL J. Biol. Chem. 281:37275-37281(2006). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE SPT COMPLEX, AND RP INTERACTION WITH C3ORF57 AND C14ORF147. RX PubMed=19416851; DOI=10.1073/pnas.0811269106; RA Han G., Gupta S.D., Gable K., Niranjanakumari S., Moitra P., RA Eichler F., Brown R.H. Jr., Harmon J.M., Dunn T.M.; RT "Identification of small subunits of mammalian serine RT palmitoyltransferase that confer distinct acyl-CoA substrate RT specificities."; RL Proc. Natl. Acad. Sci. U.S.A. 106:8186-8191(2009). RN [8] RP INTERACTION WITH ORMDL3. RX PubMed=20182505; DOI=10.1038/nature08787; RA Breslow D.K., Collins S.R., Bodenmiller B., Aebersold R., Simons K., RA Shevchenko A., Ejsing C.S., Weissman J.S.; RT "Orm family proteins mediate sphingolipid homeostasis."; RL Nature 463:1048-1053(2010). RN [9] 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., RA Buerckstuemmer T., 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 [10] RP VARIANT ALA-387. RX PubMed=15037712; RA Verhoeven K., Coen K., De Vriendt E., Jacobs A., Van Gerwen V., RA Smouts I., Pou-Serradell A., Martin J.-J., Timmerman V., De Jonghe P.; RT "SPTLC1 mutation in twin sisters with hereditary sensory neuropathy RT type I."; RL Neurology 62:1001-1002(2004). RN [11] RP VARIANT LEU-151. RX PubMed=17060578; DOI=10.1212/01.wnl.0000240068.21499.f5; RA Meggouh F., Bienfait H.M.E., Weterman M.A.J., de Visser M., Baas F.; RT "Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 RT gene."; RL Neurology 67:1476-1478(2006). RN [12] RP VARIANT [LARGE SCALE ANALYSIS] TRP-239. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). RN [13] RP VARIANTS HSAN1A PHE-331 AND VAL-352. RX PubMed=19651702; DOI=10.1093/brain/awp198; RA Rotthier A., Baets J., De Vriendt E., Jacobs A., Auer-Grumbach M., RA Levy N., Bonello-Palot N., Kilic S.S., Weis J., Nascimento A., RA Swinkels M., Kruyt M.C., Jordanova A., De Jonghe P., Timmerman V.; RT "Genes for hereditary sensory and autonomic neuropathies: a genotype- RT phenotype correlation."; RL Brain 132:2699-2711(2009). RN [14] RP CHARACTERIZATION OF VARIANTS HSAN1A TYR-133; TRP-133 AND ASP-144, RP CHARACTERIZATION OF VARIANT ALA-387, AND LACK OF ASSOCIATION OF RP VARIANT ALA-387 WITH HSAN1A. RX PubMed=19132419; DOI=10.1007/s10048-008-0168-7; RA Hornemann T., Penno A., Richard S., Nicholson G., van Dijk F.S., RA Rotthier A., Timmerman V., von Eckardstein A.; RT "A systematic comparison of all mutations in hereditary sensory RT neuropathy type I (HSAN I) reveals that the G387A mutation is not RT disease associated."; RL Neurogenetics 10:135-143(2009). RN [15] RP VARIANT HSAN1A PHE-331, AND CHARACTERIZATION OF VARIANTS HSAN1A RP PHE-331 AND VAL-352. RX PubMed=21618344; DOI=10.1002/humu.21481; RA Rotthier A., Penno A., Rautenstrauss B., Auer-Grumbach M., RA Stettner G.M., Asselbergh B., Van Hoof K., Sticht H., Levy N., RA Timmerman V., Hornemann T., Janssens K.; RT "Characterization of two mutations in the SPTLC1 subunit of serine RT palmitoyltransferase associated with hereditary sensory and autonomic RT neuropathy type I."; RL Hum. Mutat. 32:E2211-E2225(2011). CC -!- FUNCTION: Serine palmitoyltransferase (SPT). The heterodimer CC formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The CC composition of the serine palmitoyltransferase (SPT) complex CC determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA CC complex shows a strong preference for C16-CoA substrate, while the CC SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as CC substrates, with a slight preference for C14-CoA. The SPTLC1- CC SPTLC2-SPTSSB complex shows a strong preference for C18-CoA CC substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an CC ability to use a broader range of acyl-CoAs, without apparent CC preference. CC -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D- CC sphinganine + CO(2). CC -!- COFACTOR: Pyridoxal phosphate (By similarity). CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism. CC -!- SUBUNIT: Heterodimer with SPTLC2 or SPTLC3. Component of the CC serine palmitoyltransferase (SPT) complex, composed of SPTLC1, CC either SPTLC2 or SPTLC3, and either SSSPTA or SSSPTB. Interacts CC with SPTSSA and SPTSSB; the interaction is direct. Interacts with CC ORMDL3. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass CC membrane protein (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. Not detected in small CC intestine. CC -!- DISEASE: Defects in SPTLC1 are the cause of hereditary sensory and CC autonomic neuropathy type 1A (HSAN1A) [MIM:162400]. The hereditary CC sensory and autonomic neuropathies are a genetically and CC clinically heterogeneous group of disorders characterized by CC degeneration of dorsal root and autonomic ganglion cells, and by CC sensory and/or autonomic abnormalities. HSAN1A is an autosomal CC dominant axonal neuropathy with onset in the second or third CC decades. Initial symptoms are loss of pain, touch, heat, and cold CC sensation over the feet, followed by distal muscle wasting and CC weakness. Loss of pain sensation leads to chronic skin ulcers and CC distal amputations. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. CC -!- CAUTION: Variant Ala-387 has been originally thought to cause CC HSAN1A (PubMed:15037712). Subsequently, it has been shown to be a CC rare, benign polymorphism found in homozygous state in a healthy CC individual (PubMed:19132419). CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/SPTLC1"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y08685; CAA69941.1; -; mRNA. DR EMBL; AF286717; AAK29328.1; -; Genomic_DNA. DR EMBL; AF286703; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286704; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286705; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286706; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286707; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286708; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286709; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286710; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286711; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286712; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286713; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286714; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286715; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AF286716; AAK29328.1; JOINED; Genomic_DNA. DR EMBL; AK291546; BAF84235.1; -; mRNA. DR EMBL; AL391219; CAH70209.1; -; Genomic_DNA. DR EMBL; AL354751; CAH70209.1; JOINED; Genomic_DNA. DR EMBL; AL354751; CAH69924.1; -; Genomic_DNA. DR EMBL; AL391219; CAH69924.1; JOINED; Genomic_DNA. DR EMBL; CH471089; EAW62804.1; -; Genomic_DNA. DR IPI; IPI00005745; -. DR RefSeq; NP_006406.1; NM_006415.2. DR UniGene; Hs.90458; -. DR ProteinModelPortal; O15269; -. DR SMR; O15269; 54-471. DR DIP; DIP-45626N; -. DR IntAct; O15269; 5. DR STRING; O15269; -. DR PhosphoSite; O15269; -. DR PeptideAtlas; O15269; -. DR PRIDE; O15269; -. DR Ensembl; ENST00000262554; ENSP00000262554; ENSG00000090054. DR GeneID; 10558; -. DR KEGG; hsa:10558; -. DR UCSC; uc004arl.1; human. DR CTD; 10558; -. DR GeneCards; GC09M094793; -. DR H-InvDB; HIX0008162; -. DR HGNC; HGNC:11277; SPTLC1. DR HPA; CAB018747; -. DR HPA; HPA010860; -. DR MIM; 162400; phenotype. DR MIM; 605712; gene. DR neXtProt; NX_O15269; -. DR Orphanet; 36386; Hereditary sensory and autonomic neuropathy type 1. DR PharmGKB; PA36106; -. DR HOVERGEN; HBG003992; -. DR InParanoid; O15269; -. DR OrthoDB; EOG4XPQFX; -. DR PhylomeDB; O15269; -. DR BRENDA; 2.3.1.50; 2681. DR Reactome; REACT_22258; Metabolism of lipids and lipoproteins. DR DrugBank; DB00133; L-Serine. DR DrugBank; DB00114; Pyridoxal Phosphate. DR NextBio; 40067; -. DR ArrayExpress; O15269; -. DR Bgee; O15269; -. DR CleanEx; HS_SPTLC1; -. DR Genevestigator; O15269; -. DR GermOnline; ENSG00000090054; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0035339; C:SPOTS complex; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0004758; F:serine C-palmitoyltransferase activity; IDA:UniProtKB. DR GO; GO:0016769; F:transferase activity, transferring nitrogenous groups; IEA:InterPro. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1. DR Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1. DR KO; K00654; -. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; FALSE_NEG. PE 1: Evidence at protein level; KW Acyltransferase; Complete proteome; Disease mutation; KW Endoplasmic reticulum; Membrane; Neuropathy; Polymorphism; KW Pyridoxal phosphate; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 473 Serine palmitoyltransferase 1. FT /FTId=PRO_0000163853. FT TOPO_DOM 1 15 Lumenal (Potential). FT TRANSMEM 16 36 Helical; (Potential). FT TOPO_DOM 37 473 Cytoplasmic (Potential). FT VARIANT 133 133 C -> W (in HSAN1A; reduced activity; does FT not interfere with SPT complex FT formation). FT /FTId=VAR_011392. FT VARIANT 133 133 C -> Y (in HSAN1A; reduced activity; does FT not interfere with SPT complex FT formation). FT /FTId=VAR_011393. FT VARIANT 144 144 V -> D (in HSAN1A; reduced activity; does FT not interfere with SPT complex FT formation). FT /FTId=VAR_011394. FT VARIANT 151 151 R -> L (in dbSNP:rs45461899). FT /FTId=VAR_037889. FT VARIANT 239 239 R -> W (in a breast cancer sample; FT somatic mutation). FT /FTId=VAR_036610. FT VARIANT 331 331 S -> F (in HSAN1A; reduced activity). FT /FTId=VAR_066245. FT VARIANT 352 352 A -> V (in HSAN1A; reduced activity). FT /FTId=VAR_066246. FT VARIANT 387 387 G -> A (rare polymorphism; does not FT affect activity; does not interfere with FT SPT complex formation). FT /FTId=VAR_037890. SQ SEQUENCE 473 AA; 52744 MW; BA9E056A869D2EA2 CRC64; MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS DLTVKEKEEL IEEWQPEPLV PPVPKDHPAL NYNIVSGPPS HKTVVNGKEC INFASFNFLG LLDNPRVKAA ALASLKKYGV GTCGPRGFYG TFDVHLDLED RLAKFMKTEE AIIYSYGFAT IASAIPAYSK RGDIVFVDRA ACFAIQKGLQ ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP GIFAVLKEKC GQIHKALQGI SGLKVVGESL SPAFHLQLEE STGSREQDVR LLQEIVDQCM NRSIALTQAR YLEKEEKCLP PPSIRVVVTV EQTEEELERA ASTIKEVAQA VLL //