ID   VPP2_MOUSE              Reviewed;         856 AA.
AC   P15920; A4FU82; Q3U2X3; Q8VHU0; Q9JHJ2;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   27-MAR-2024, entry version 199.
DE   RecName: Full=V-type proton ATPase 116 kDa subunit a 2;
DE            Short=V-ATPase 116 kDa subunit a 2;
DE   AltName: Full=Immune suppressor factor J6B7;
DE            Short=ISF;
DE   AltName: Full=Lysosomal H(+)-transporting ATPase V0 subunit a 2;
DE   AltName: Full=ShIF;
DE   AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2;
GN   Name=Atp6v0a2; Synonyms=Atp6n1b, Tj6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=2247090; DOI=10.1016/0161-5890(90)90102-6;
RA   Lee C.-K., Ghoshal K., Beaman K.D.;
RT   "Cloning of a cDNA for a T cell produced molecule with a putative immune
RT   regulatory role.";
RL   Mol. Immunol. 27:1137-1144(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=10722719; DOI=10.1074/jbc.275.12.8760;
RA   Toyomura T., Oka T., Yamaguchi C., Wada Y., Futai M.;
RT   "Three subunit a isoforms of mouse vacuolar H+-ATPase. Preferential
RT   expression of the a3 isoform during osteoclast differentiation.";
RL   J. Biol. Chem. 275:8760-8765(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Heart;
RX   PubMed=10702241; DOI=10.1074/jbc.275.10.6824;
RA   Nishi T., Forgac M.;
RT   "Molecular cloning and expression of three isoforms of the 100-kDa a
RT   subunit of the mouse vacuolar proton-translocating ATPase.";
RL   J. Biol. Chem. 275:6824-6830(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NOD; TISSUE=Dendritic cell, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
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 [MRNA] OF 569-856, AND TISSUE SPECIFICITY.
RX   PubMed=11375395; DOI=10.1074/jbc.m101781200;
RA   Tulin E.E., Onoda N., Maeda M., Hasegawa M., Nosaka T., Nomura H.,
RA   Asano S., Kitamura T.;
RT   "A novel secreted form of immune suppressor factor with high homology to
RT   vacuolar ATPases identified by a forward genetic approach of functional
RT   screening based on cell proliferation.";
RL   J. Biol. Chem. 276:27519-27526(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSCD2.
RX   PubMed=16415858; DOI=10.1038/ncb1348;
RA   Hurtado-Lorenzo A., Skinner M., El Annan J., Futai M., Sun-Wada G.-H.,
RA   Bourgoin S., Casanova J., Wildeman A., Bechoua S., Ausiello D.A., Brown D.,
RA   Marshansky V.;
RT   "V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the
RT   protein degradative pathway.";
RL   Nat. Cell Biol. 8:124-136(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-700, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-700, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (By similarity). Essential
CC       component of the endosomal pH-sensing machinery (PubMed:16415858). May
CC       play a role in maintaining the Golgi functions, such as glycosylation
CC       maturation, by controlling the Golgi pH (By similarity). In aerobic
CC       conditions, involved in intracellular iron homeostasis, thus triggering
CC       the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to
CC       HIF1A hydroxylation and subsequent proteasomal degradation (By
CC       similarity). {ECO:0000250|UniProtKB:Q29466,
CC       ECO:0000250|UniProtKB:Q93050, ECO:0000250|UniProtKB:Q9Y487,
CC       ECO:0000269|PubMed:16415858}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). Directly interacts with PSCD2 through its N-terminal
CC       cytosolic tail in an intra-endosomal acidification-dependent manner
CC       (PubMed:16415858). Disruption of this interaction results in the
CC       inhibition of endocytosis (PubMed:16415858). Interacts with SPAAR (By
CC       similarity). {ECO:0000250|UniProtKB:Q93050,
CC       ECO:0000250|UniProtKB:Q9Y487, ECO:0000269|PubMed:16415858}.
CC   -!- INTERACTION:
CC       P15920; P63034: Cyth2; NbExp=5; IntAct=EBI-988456, EBI-988425;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16415858};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16415858}. Endosome
CC       membrane {ECO:0000269|PubMed:16415858}. Note=In kidney proximal
CC       tubules, detected in subapical early endosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P15920-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15920-2; Sequence=VSP_032088;
CC   -!- TISSUE SPECIFICITY: Relatively high expression in kidney and liver.
CC       Lower levels in the spleen, testis, and skeletal muscle. Also expressed
CC       in the thymus. {ECO:0000269|PubMed:11375395}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL57303.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M31226; AAA39336.1; -; mRNA.
DR   EMBL; X55184; CAA38968.1; -; mRNA.
DR   EMBL; AB022323; BAA93007.1; -; mRNA.
DR   EMBL; AF218252; AAF59921.1; -; mRNA.
DR   EMBL; AK032909; BAC28081.1; -; mRNA.
DR   EMBL; AK155055; BAE33017.1; -; mRNA.
DR   EMBL; BC108991; AAI08992.1; -; mRNA.
DR   EMBL; BC108992; AAI08993.1; -; mRNA.
DR   EMBL; BC112905; AAI12906.1; -; mRNA.
DR   EMBL; AF388674; AAL57303.1; ALT_INIT; mRNA.
DR   CCDS; CCDS84963.1; -. [P15920-1]
DR   PIR; JH0287; JH0287.
DR   RefSeq; NP_035726.2; NM_011596.5. [P15920-1]
DR   PDB; 2LX4; NMR; -; A=1-17.
DR   PDBsum; 2LX4; -.
DR   AlphaFoldDB; P15920; -.
DR   BMRB; P15920; -.
DR   SMR; P15920; -.
DR   BioGRID; 204208; 1.
DR   IntAct; P15920; 1.
DR   STRING; 10090.ENSMUSP00000039737; -.
DR   TCDB; 3.A.2.2.6; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P15920; -.
DR   PhosphoSitePlus; P15920; -.
DR   SwissPalm; P15920; -.
DR   EPD; P15920; -.
DR   jPOST; P15920; -.
DR   MaxQB; P15920; -.
DR   PaxDb; 10090-ENSMUSP00000039737; -.
DR   PeptideAtlas; P15920; -.
DR   ProteomicsDB; 300181; -. [P15920-1]
DR   ProteomicsDB; 300182; -. [P15920-2]
DR   Pumba; P15920; -.
DR   Antibodypedia; 31833; 132 antibodies from 25 providers.
DR   DNASU; 21871; -.
DR   Ensembl; ENSMUST00000037865.13; ENSMUSP00000039737.9; ENSMUSG00000038023.13. [P15920-1]
DR   GeneID; 21871; -.
DR   KEGG; mmu:21871; -.
DR   UCSC; uc008zqn.2; mouse. [P15920-2]
DR   UCSC; uc029voj.2; mouse. [P15920-1]
DR   AGR; MGI:104855; -.
DR   CTD; 23545; -.
DR   MGI; MGI:104855; Atp6v0a2.
DR   VEuPathDB; HostDB:ENSMUSG00000038023; -.
DR   eggNOG; KOG2189; Eukaryota.
DR   GeneTree; ENSGT00950000182881; -.
DR   HOGENOM; CLU_005230_0_0_1; -.
DR   InParanoid; P15920; -.
DR   OMA; TYVQLYI; -.
DR   OrthoDB; 1967517at2759; -.
DR   PhylomeDB; P15920; -.
DR   TreeFam; TF300346; -.
DR   Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-MMU-77387; Insulin receptor recycling.
DR   Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-MMU-983712; Ion channel transport.
DR   BioGRID-ORCS; 21871; 2 hits in 54 CRISPR screens.
DR   ChiTaRS; Atp6v0a2; mouse.
DR   PRO; PR:P15920; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; P15920; Protein.
DR   Bgee; ENSMUSG00000038023; Expressed in choroid plexus of fourth ventricle and 287 other cell types or tissues.
DR   ExpressionAtlas; P15920; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0043229; C:intracellular organelle; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IDA:MGI.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IDA:MGI.
DR   GO; GO:1902495; C:transmembrane transporter complex; IDA:MGI.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629:SF22; V-TYPE PROTON ATPASE 116 KDA SUBUNIT A 2; 1.
DR   PANTHER; PTHR11629; VACUOLAR PROTON ATPASES; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
DR   Genevisible; P15920; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Endosome;
KW   Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..856
FT                   /note="V-type proton ATPase 116 kDa subunit a 2"
FT                   /id="PRO_0000119217"
FT   TOPO_DOM        1..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        413..414
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        432..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        476..549
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        550..569
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        570..587
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        588..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        609..651
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        652..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        672..739
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        740..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        765..785
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        786..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        825..856
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         695
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         700
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..593
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_032088"
FT   CONFLICT        486
FT                   /note="S -> C (in Ref. 1; AAA39336/CAA38968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        791
FT                   /note="Missing (in Ref. 1; AAA39336/CAA38968)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..16
FT                   /evidence="ECO:0007829|PDB:2LX4"
SQ   SEQUENCE   856 AA;  98145 MW;  6A0D593F6F401E22 CRC64;
     MGSLFRSESM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK FVGEVKRCEE
     LERILVYLVQ EITRADIPLP EGEASPPAPP LKHVLEMQEQ LQKLEVELRE VTKNKEKLRK
     NLLELVEYTH MLRVTKTFLK RNVEFEPTYE EFPALENDSL LDYSCMQRLG AKLGFVSGLI
     QQGRVEAFER MLWRACKGYT IVTYAELDEC LEDPETGEVI KWYVFLISFW GEQIGHKVKK
     ICDCYHCHIY PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVCSRVV
     QVRKMKAIYH MLNMCSFDVT NKCLIAEVWC PEVDLPGLRR ALEEGSRESG ATIPSFMNTI
     PTKETPPTLI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT IITFPFLFAV MFGDFGHGFV
     MFLFALLLVL NENHPRLSQS QEILRMFFDG RYILLLMGLF SVYTGLIYND CFSKSVNLFG
     SGWNVSAMYS SSHSPEEQRK MVLWNDSTIR HSRTLQLDPN IPGVFRGPYP FGIDPIWNLA
     TNRLTFLNSF KMKMSVILGI FHMTFGVVLG IFNHLHFRKK FNVYLVSVPE ILFMLCIFGY
     LIFMIIYKWL AYSAETSREA PSILIEFINM FLFPTSKTHG LYPGQAHVQR VLVALTVLAV
     PVLFLGKPLF LLWLHNGRNC FGMSRSGYTL VRKDSEEEVS LLGNQDIEEG NSRMEEGCRE
     VTCEEFNFGE ILMTQAIHSI EYCLGCISNT ASYLRLWALS LAHAQLSDVL WAMLMRVGLR
     VDTTYGVLLL LPVMAFFAVL TIFILLVMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF
     SFSLLSSKFS NDDSIA
//