ID   NDUAC_HUMAN             Reviewed;         145 AA.
AC   Q9UI09; F8VQS7; Q53XX0; Q9BRV6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   28-JAN-2026, entry version 196.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12;
DE   AltName: Full=13 kDa differentiation-associated protein;
DE   AltName: Full=Complex I-B17.2;
DE            Short=CI-B17.2;
DE            Short=CIB17.2;
DE   AltName: Full=NADH-ubiquinone oxidoreductase subunit B17.2;
GN   Name=NDUFA12; Synonyms=DAP13;
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].
RX   PubMed=10830904; DOI=10.1007/s004390000278;
RA   Triepels R., Smeitink J., Loeffen J., Smeets R., Trijbels F.,
RA   van den Heuvel L.;
RT   "Characterization of the human complex I NDUFB7 and 17.2-kDa cDNAs and
RT   mutational analysis of 19 genes of the HP fraction in complex I-deficient-
RT   patients.";
RL   Hum. Genet. 106:385-391(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Adrenal gland;
RX   PubMed=10931946; DOI=10.1073/pnas.160270997;
RA   Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA   Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA   Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA   Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA   Chen M.-D., Chen J.-L.;
RT   "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT   and full-length cDNA cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-104.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-104.
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   IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA   Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA   Ghosh S.S., Capaldi R.A.;
RT   "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT   one-step immunopurification.";
RL   J. Biol. Chem. 278:13619-13622(2003).
RN   [7]
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., Buerckstuemmer T.,
RA   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   [8]
RP   INVOLVEMENT IN MC1DN23, AND VARIANT MC1DN23 60-ARG--LYS-145 DEL.
RX   PubMed=21617257; DOI=10.1136/jmg.2011.088856;
RA   Ostergaard E., Rodenburg R.J., van den Brand M., Thomsen L.L., Duno M.,
RA   Batbayli M., Wibrand F., Nijtmans L.;
RT   "Respiratory chain complex I deficiency due to NDUFA12 mutations as a new
RT   cause of Leigh syndrome.";
RL   J. Med. Genet. 48:737-740(2011).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [12]
RP   FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX   PubMed=27626371; DOI=10.1038/nature19754;
RA   Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA   Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA   Salim A., Ryan M.T.;
RT   "Accessory subunits are integral for assembly and function of human
RT   mitochondrial complex I.";
RL   Nature 538:123-126(2016).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I), that is believed not to be
CC       involved in catalysis. Complex I functions in the transfer of electrons
CC       from NADH to the respiratory chain. The immediate electron acceptor for
CC       the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC       {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC   -!- INTERACTION:
CC       Q9UI09; Q96JP2: MYO15B; NbExp=3; IntAct=EBI-1246332, EBI-7950783;
CC       Q9UI09; Q9H2B2: SYT4; NbExp=3; IntAct=EBI-1246332, EBI-751132;
CC       Q9UI09; Q6PL24: TMED8; NbExp=3; IntAct=EBI-1246332, EBI-11603430;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC       {ECO:0000255}; Matrix side {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9UI09-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9UI09-2; Sequence=VSP_046948;
CC   -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 23 (MC1DN23)
CC       [MIM:618244]: A form of mitochondrial complex I deficiency, the most
CC       common biochemical signature of mitochondrial disorders, a group of
CC       highly heterogeneous conditions characterized by defective oxidative
CC       phosphorylation, which collectively affects 1 in 5-10000 live births.
CC       Clinical disorders have variable severity, ranging from lethal neonatal
CC       disease to adult-onset neurodegenerative disorders. Phenotypes include
CC       macrocephaly with progressive leukodystrophy, non-specific
CC       encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC       syndrome, Leber hereditary optic neuropathy, and some forms of
CC       Parkinson disease. MC1DN23 transmission pattern is consistent with
CC       autosomal recessive inheritance. {ECO:0000269|PubMed:21617257}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- MISCELLANEOUS: In NDUFA12-knockout cells, complex I assembly is not
CC       affected, probably due to substitution by the NDUFAF2 paralog.
CC       {ECO:0000269|PubMed:27626371}.
CC   -!- SIMILARITY: Belongs to the complex I NDUFA12 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AF217092; AAF91224.1; -; mRNA.
DR   EMBL; AF112208; AAF17196.1; -; mRNA.
DR   EMBL; BT007220; AAP35884.1; -; mRNA.
DR   EMBL; AC011598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132009; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005936; AAH05936.1; -; mRNA.
DR   CCDS; CCDS58263.1; -. [Q9UI09-2]
DR   CCDS; CCDS9050.1; -. [Q9UI09-1]
DR   RefSeq; NP_001245267.1; NM_001258338.2. [Q9UI09-2]
DR   RefSeq; NP_061326.1; NM_018838.5. [Q9UI09-1]
DR   PDB; 5XTB; EM; 3.40 A; N=2-144.
DR   PDB; 5XTD; EM; 3.70 A; N=2-144.
DR   PDB; 5XTH; EM; 3.90 A; N=2-144.
DR   PDB; 5XTI; EM; 17.40 A; BN/N=2-144.
DR   PDB; 9CWT; EM; 3.44 A; N=1-145.
DR   PDBsum; 5XTB; -.
DR   PDBsum; 5XTD; -.
DR   PDBsum; 5XTH; -.
DR   PDBsum; 5XTI; -.
DR   PDBsum; 9CWT; -.
DR   AlphaFoldDB; Q9UI09; -.
DR   EMDB; EMD-45974; -.
DR   SMR; Q9UI09; -.
DR   BioGRID; 121013; 226.
DR   ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR   CORUM; Q9UI09; -.
DR   FunCoup; Q9UI09; 2240.
DR   IntAct; Q9UI09; 112.
DR   MINT; Q9UI09; -.
DR   STRING; 9606.ENSP00000330737; -.
DR   BindingDB; Q9UI09; -.
DR   ChEMBL; CHEMBL2363065; -.
DR   DrugBank; DB00157; NADH.
DR   DrugCentral; Q9UI09; -.
DR   GlyGen; Q9UI09; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UI09; -.
DR   PhosphoSitePlus; Q9UI09; -.
DR   BioMuta; NDUFA12; -.
DR   DMDM; 12229870; -.
DR   jPOST; Q9UI09; -.
DR   MassIVE; Q9UI09; -.
DR   PaxDb; 9606-ENSP00000330737; -.
DR   PeptideAtlas; Q9UI09; -.
DR   ProteomicsDB; 28348; -.
DR   ProteomicsDB; 84447; -. [Q9UI09-1]
DR   Pumba; Q9UI09; -.
DR   TopDownProteomics; Q9UI09-1; -. [Q9UI09-1]
DR   Antibodypedia; 30095; 166 antibodies from 28 providers.
DR   DNASU; 55967; -.
DR   Ensembl; ENST00000327772.7; ENSP00000330737.2; ENSG00000184752.15. [Q9UI09-1]
DR   Ensembl; ENST00000547986.5; ENSP00000450130.1; ENSG00000184752.15. [Q9UI09-2]
DR   GeneID; 55967; -.
DR   KEGG; hsa:55967; -.
DR   MANE-Select; ENST00000327772.7; ENSP00000330737.2; NM_018838.5; NP_061326.1.
DR   UCSC; uc001tdl.5; human. [Q9UI09-1]
DR   AGR; HGNC:23987; -.
DR   ClinPGx; PA142671269; -.
DR   CTD; 55967; -.
DR   DisGeNET; 55967; -.
DR   GeneCards; NDUFA12; -.
DR   HGNC; HGNC:23987; NDUFA12.
DR   HPA; ENSG00000184752; Tissue enhanced (skeletal muscle, tongue).
DR   MalaCards; NDUFA12; -.
DR   MIM; 614530; gene.
DR   MIM; 618244; phenotype.
DR   OpenTargets; ENSG00000184752; -.
DR   VEuPathDB; HostDB:ENSG00000184752; -.
DR   eggNOG; KOG3382; Eukaryota.
DR   GeneTree; ENSGT00390000005848; -.
DR   HOGENOM; CLU_110455_1_0_1; -.
DR   InParanoid; Q9UI09; -.
DR   OMA; VIYTAEM; -.
DR   OrthoDB; 274641at2759; -.
DR   PAN-GO; Q9UI09; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UI09; -.
DR   BioCyc; MetaCyc:HS03370-MONOMER; -.
DR   PathwayCommons; Q9UI09; -.
DR   Reactome; R-HSA-611105; Respiratory electron transport.
DR   Reactome; R-HSA-6799198; Complex I biogenesis.
DR   SignaLink; Q9UI09; -.
DR   SIGNOR; Q9UI09; -.
DR   Agora; ENSG00000184752; -.
DR   BioGRID-ORCS; 55967; 14 hits in 1157 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; NDUFA12; human.
DR   GenomeRNAi; 55967; -.
DR   Pharos; Q9UI09; Tclin.
DR   PRO; PR:Q9UI09; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q9UI09; protein.
DR   Bgee; ENSG00000184752; Expressed in left ventricle myocardium and 190 other cell types or tissues.
DR   ExpressionAtlas; Q9UI09; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0045271; C:respiratory chain complex I; IDA:UniProtKB.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; NAS:UniProtKB.
DR   GO; GO:0009060; P:aerobic respiration; NAS:ComplexPortal.
DR   GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:CAFA.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; NAS:ComplexPortal.
DR   InterPro; IPR007763; NDUFA12.
DR   PANTHER; PTHR12910:SF2; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 12; 1.
DR   PANTHER; PTHR12910; NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT B17.2; 1.
DR   Pfam; PF05071; NDUFA12; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Disease variant;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Primary mitochondrial disease; Proteomics identification;
KW   Reference proteome; Respiratory chain; Transport.
FT   CHAIN           1..145
FT                   /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT                   subunit 12"
FT                   /id="PRO_0000118845"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378,
FT                   ECO:0007744|PubMed:25944712"
FT   VAR_SEQ         58..145
FT                   /note="RHRWVVYTTEMNGKNTFWDVDGSMVPPEWHRWLHSMTDDPPTTKPLTARKFI
FT                   WTNHKFNVTGTPEQYVPYSTTRKKIQEWIPPSTPYK -> IVGFTV (in isoform
FT                   2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_046948"
FT   VARIANT         60..145
FT                   /note="Missing (in MC1DN23)"
FT                   /evidence="ECO:0000269|PubMed:21617257"
FT                   /id="VAR_081459"
FT   VARIANT         104
FT                   /note="T -> A (in dbSNP:rs17850017)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT                   /id="VAR_060682"
FT   HELIX           3..15
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           68..70
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   HELIX           84..90
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   TURN            98..100
FT                   /evidence="ECO:0007829|PDB:5XTB"
FT   STRAND          118..121
FT                   /evidence="ECO:0007829|PDB:5XTB"
SQ   SEQUENCE   145 AA;  17114 MW;  C76C7F2F5974AFF9 CRC64;
     MELVQVLKRG LQQITGHGGL RGYLRVFFRT NDAKVGTLVG EDKYGNKYYE DNKQFFGRHR
     WVVYTTEMNG KNTFWDVDGS MVPPEWHRWL HSMTDDPPTT KPLTARKFIW TNHKFNVTGT
     PEQYVPYSTT RKKIQEWIPP STPYK
//