TPPC9_HUMAN
ID TPPC9_HUMAN Reviewed; 1148 AA.
AC Q96Q05; Q4VTT3; Q658K7; Q6P149; Q6ZQT3; Q7L5C4; Q86Y21; Q96SL2; Q9BQA2;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Trafficking protein particle complex subunit 9;
DE AltName: Full=NIK- and IKBKB-binding protein;
DE AltName: Full=Tularik gene 1 protein;
GN Name=TRAPPC9; Synonyms=KIAA1882, NIBP; ORFNames=T1;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11572484; DOI=10.1093/dnares/8.4.179;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXI. The
RT complete sequences of 60 new cDNA clones from brain which code for large
RT proteins.";
RL DNA Res. 8:179-187(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum, and Teratocarcinoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-1148 (ISOFORM 3).
RC TISSUE=Lung, and Skin;
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 [LARGE SCALE MRNA] OF 198-1148 (ISOFORM 1).
RC TISSUE=Uterus;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 205-1148 (ISOFORM 1).
RX PubMed=12676587; DOI=10.1016/s1535-6108(03)00054-0;
RA Mu D., Chen L., Zhang X., See L.-H., Koch C.M., Yen C., Tong J.J.,
RA Spiegel L., Nguyen K.C.Q., Servoss A., Peng Y., Pei L., Marks J.R.,
RA Lowe S., Hoey T., Jan L.Y., McCombie W.R., Wigler M.H., Powers S.;
RT "Genomic amplification and oncogenic properties of the KCNK9 potassium
RT channel gene.";
RL Cancer Cell 3:297-302(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 938-1148 (ISOFORM 1), FUNCTION, INTERACTION
RP WITH IKBKB AND MAP3K14, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=15951441; DOI=10.1074/jbc.m501670200;
RA Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V.,
RA Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.;
RT "NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-(kappa)B
RT activation.";
RL J. Biol. Chem. 280:29233-29241(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP INVOLVEMENT IN MRT13.
RX PubMed=20004763; DOI=10.1016/j.ajhg.2009.10.027;
RA Mochida G.H., Mahajnah M., Hill A.D., Basel-Vanagaite L., Gleason D.,
RA Hill R.S., Bodell A., Crosier M., Straussberg R., Walsh C.A.;
RT "A truncating mutation of TRAPPC9 is associated with autosomal-recessive
RT intellectual disability and postnatal microcephaly.";
RL Am. J. Hum. Genet. 85:897-902(2009).
RN [9]
RP INVOLVEMENT IN MRT13.
RX PubMed=20004765; DOI=10.1016/j.ajhg.2009.11.009;
RA Mir A., Kaufman L., Noor A., Motazacker M.M., Jamil T., Azam M.,
RA Kahrizi K., Rafiq M.A., Weksberg R., Nasr T., Naeem F., Tzschach A.,
RA Kuss A.W., Ishak G.E., Doherty D., Ropers H.H., Barkovich A.J.,
RA Najmabadi H., Ayub M., Vincent J.B.;
RT "Identification of mutations in TRAPPC9, which encodes the NIK- and IKK-
RT beta-binding protein, in nonsyndromic autosomal-recessive mental
RT retardation.";
RL Am. J. Hum. Genet. 85:909-915(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION IN TRAPP COMPLEX.
RX PubMed=21525244; DOI=10.1091/mbc.e10-11-0873;
RA Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early
RT stage in ER-to-Golgi trafficking.";
RL Mol. Biol. Cell 22:2083-2093(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND SER-953, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Functions as an activator of NF-kappa-B through increased
CC phosphorylation of the IKK complex. May function in neuronal cells
CC differentiation. May play a role in vesicular transport from
CC endoplasmic reticulum to Golgi. {ECO:0000269|PubMed:15951441}.
CC -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC TRAPPC12. Directly interacts with IKBKB and MAP3K14.
CC {ECO:0000269|PubMed:15951441, ECO:0000269|PubMed:21525244}.
CC -!- INTERACTION:
CC Q96Q05; Q9CQP2: Trappc2; Xeno; NbExp=2; IntAct=EBI-6160596, EBI-1172267;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Processes and cell bodies of neurons. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96Q05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96Q05-2; Sequence=VSP_034349;
CC Name=3;
CC IsoId=Q96Q05-3; Sequence=VSP_034350;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in muscle and kidney and
CC to a lower extent in brain, heart and placenta.
CC {ECO:0000269|PubMed:15951441}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 13
CC (MRT13) [MIM:613192]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. Brain
CC magnetic resonance imaging of MRT13 patients indicates the presence of
CC mild cerebral white matter hypoplasia. Microcephaly is present in some
CC but not all affected individuals. {ECO:0000269|PubMed:20004763,
CC ECO:0000269|PubMed:20004765}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the NIBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06206.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55299.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB67775.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB067469; BAB67775.1; ALT_INIT; mRNA.
DR EMBL; AK027689; BAB55299.1; ALT_INIT; mRNA.
DR EMBL; AK128755; BAC87600.1; -; mRNA.
DR EMBL; BC003650; AAH03650.3; -; mRNA.
DR EMBL; BC006206; AAH06206.3; ALT_INIT; mRNA.
DR EMBL; BC065288; AAH65288.1; -; mRNA.
DR EMBL; AL833973; CAH56384.1; -; mRNA.
DR EMBL; AY190606; AAO38740.1; -; mRNA.
DR EMBL; AY630619; AAV31908.1; -; mRNA.
DR CCDS; CCDS34946.1; -. [Q96Q05-1]
DR CCDS; CCDS55278.1; -. [Q96Q05-1]
DR RefSeq; NP_001153844.1; NM_001160372.3. [Q96Q05-1]
DR RefSeq; NP_001308575.1; NM_001321646.1. [Q96Q05-3]
DR RefSeq; NP_113654.4; NM_031466.7. [Q96Q05-1]
DR AlphaFoldDB; Q96Q05; -.
DR BioGRID; 123730; 97.
DR ComplexPortal; CPX-4749; TRAPP II complex, TRAPPC2 variant.
DR ComplexPortal; CPX-6902; TRAPP II complex, TRAPPC2B variant.
DR CORUM; Q96Q05; -.
DR IntAct; Q96Q05; 38.
DR MINT; Q96Q05; -.
DR STRING; 9606.ENSP00000373979; -.
DR iPTMnet; Q96Q05; -.
DR MetOSite; Q96Q05; -.
DR PhosphoSitePlus; Q96Q05; -.
DR BioMuta; TRAPPC9; -.
DR DMDM; 190359999; -.
DR EPD; Q96Q05; -.
DR jPOST; Q96Q05; -.
DR MassIVE; Q96Q05; -.
DR MaxQB; Q96Q05; -.
DR PaxDb; Q96Q05; -.
DR PeptideAtlas; Q96Q05; -.
DR PRIDE; Q96Q05; -.
DR ProteomicsDB; 77800; -. [Q96Q05-1]
DR ProteomicsDB; 77801; -. [Q96Q05-2]
DR ProteomicsDB; 77802; -. [Q96Q05-3]
DR Antibodypedia; 14382; 130 antibodies from 20 providers.
DR DNASU; 83696; -.
DR Ensembl; ENST00000438773.4; ENSP00000405060.3; ENSG00000167632.18. [Q96Q05-1]
DR Ensembl; ENST00000648948.2; ENSP00000498020.1; ENSG00000167632.18. [Q96Q05-1]
DR GeneID; 83696; -.
DR KEGG; hsa:83696; -.
DR MANE-Select; ENST00000438773.4; ENSP00000405060.3; NM_001160372.4; NP_001153844.1.
DR UCSC; uc003yvh.2; human. [Q96Q05-1]
DR CTD; 83696; -.
DR DisGeNET; 83696; -.
DR GeneCards; TRAPPC9; -.
DR HGNC; HGNC:30832; TRAPPC9.
DR HPA; ENSG00000167632; Low tissue specificity.
DR MalaCards; TRAPPC9; -.
DR MIM; 611966; gene.
DR MIM; 613192; phenotype.
DR neXtProt; NX_Q96Q05; -.
DR OpenTargets; ENSG00000167632; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR Orphanet; 352530; Intellectual disability-obesity-brain malformations-facial dysmorphism syndrome.
DR PharmGKB; PA162406921; -.
DR VEuPathDB; HostDB:ENSG00000167632; -.
DR eggNOG; KOG1953; Eukaryota.
DR GeneTree; ENSGT00390000006486; -.
DR InParanoid; Q96Q05; -.
DR OMA; HDHPVEH; -.
DR OrthoDB; 71855at2759; -.
DR PhylomeDB; Q96Q05; -.
DR TreeFam; TF314341; -.
DR PathwayCommons; Q96Q05; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; Q96Q05; -.
DR BioGRID-ORCS; 83696; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; TRAPPC9; human.
DR GenomeRNAi; 83696; -.
DR Pharos; Q96Q05; Tbio.
DR PRO; PR:Q96Q05; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96Q05; protein.
DR Bgee; ENSG00000167632; Expressed in hindlimb stylopod muscle and 178 other tissues.
DR ExpressionAtlas; Q96Q05; baseline and differential.
DR Genevisible; Q96Q05; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0030008; C:TRAPP complex; IDA:UniProtKB.
DR GO; GO:1990071; C:TRAPPII protein complex; IC:ComplexPortal.
DR GO; GO:0021987; P:cerebral cortex development; IMP:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IC:ComplexPortal.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:0006901; P:vesicle coating; IC:ComplexPortal.
DR GO; GO:0099022; P:vesicle tethering; IC:ComplexPortal.
DR InterPro; IPR013935; TRAPP_II_complex_Trs120.
DR PANTHER; PTHR21512; PTHR21512; 1.
DR Pfam; PF08626; TRAPPC9-Trs120; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Differentiation; Endoplasmic reticulum;
KW Golgi apparatus; Intellectual disability; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1148
FT /note="Trafficking protein particle complex subunit 9"
FT /id="PRO_0000341586"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1
FT /note="M -> MVPAGDQDRAPHRGKPAQAGARTSRASRALRSWRRSQAARATVTHPR
FT GGHDRGSHGGYREGHRGCRRDPQWASAGPPPLSFTEEVKFELRALKDWDFKM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034349"
FT VAR_SEQ 286..294
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_034350"
FT CONFLICT 505
FT /note="Missing (in Ref. 4; CAH56384)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="I -> V (in Ref. 2; BAC87600)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="V -> E (in Ref. 2; BAB55299)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1148 AA; 128530 MW; 532932462A6853CC CRC64;
MSVPDYMQCA EDHQTLLVVV QPVGIVSEEN FFRIYKRICS VSQISVRDSQ RVLYIRYRHH
YPPENNEWGD FQTHRKVVGL ITITDCFSAK DWPQTFEKFH VQKEIYGSTL YDSRLFVFGL
QGEIVEQPRT DVAFYPNYED CQTVEKRIED FIESLFIVLE SKRLDRATDK SGDKIPLLCV
PFEKKDFVGL DTDSRHYKKR CQGRMRKHVG DLCLQAGMLQ DSLVHYHMSV ELLRSVNDFL
WLGAALEGLC SASVIYHYPG GTGGKSGARR FQGSTLPAEA ANRHRPGAQE VLIDPGALTT
NGINPDTSTE IGRAKNCLSP EDIIDKYKEA ISYYSKYKNA GVIELEACIK AVRVLAIQKR
SMEASEFLQN AVYINLRQLS EEEKIQRYSI LSELYELIGF HRKSAFFKRV AAMQCVAPSI
AEPGWRACYK LLLETLPGYS LSLDPKDFSR GTHRGWAAVQ MRLLHELVYA SRRMGNPALS
VRHLSFLLQT MLDFLSDQEK KDVAQSLENY TSKCPGTMEP IALPGGLTLP PVPFTKLPIV
RHVKLLNLPA SLRPHKMKSL LGQNVSTKSP FIYSPIIAHN RGEERNKKID FQWVQGDVCE
VQLMVYNPMP FELRVENMGL LTSGVEFESL PAALSLPAES GLYPVTLVGV PQTTGTITVN
GYHTTVFGVF SDCLLDNLPG IKTSGSTVEV IPALPRLQIS TSLPRSAHSL QPSSGDEIST
NVSVQLYNGE SQQLIIKLEN IGMEPLEKLE VTSKVLTTKE KLYGDFLSWK LEETLAQFPL
QPGKVATFTI NIKVKLDFSC QENLLQDLSD DGISVSGFPL SSPFRQVVRP RVEGKPVNPP
ESNKAGDYSH VKTLEAVLNF KYSGGPGHTE GYYRNLSLGL HVEVEPSVFF TRVSTLPATS
TRQCHLLLDV FNSTEHELTV STRSSEALIL HAGECQRMAI QVDKFNFESF PESPGEKGQF
ANPKQLEEER REARGLEIHS KLGICWRIPS LKRSGEASVE GLLNQLVLEH LQLAPLQWDV
LVDGQPCDRE AVAACQVGDP VRLEVRLTNR SPRSVGPFAL TVVPFQDHQN GVHNYDLHDT
VSFVGSSTFY LDAVQPSGQS ACLGALLFLY TGDFFLHIRF HEDSTSKELP PSWFCLPSVH
VCALEAQA
