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PDZ11_HUMAN Reviewed; 140 AA.
Q5EBL8; D3DVU3; Q6UWE1; Q9P0Q1;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
16-AUG-2005, sequence version 2.
07-APR-2021, entry version 148.
RecName: Full=PDZ domain-containing protein 11;
AltName: Full=ATPase-interacting PDZ protein;
AltName: Full=Plasma membrane calcium ATPase-interacting single-PDZ protein;
Short=PMCA-interacting single-PDZ protein;
Name=PDZD11; Synonyms=AIPP1, PDZK11, PISP;
ORFNames=HSPC227, UNQ6486/PRO21335;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for 300
previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
cells.";
Genome Res. 10:1546-1560(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to
identify novel human secreted and transmembrane proteins: a bioinformatics
assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Artery smooth muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Chondrosarcoma, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH ATP2B1; ATP2B2; ATP2B3 AND ATP2B4, SUBCELLULAR LOCATION,
AND TISSUE SPECIFICITY.
PubMed=12763866; DOI=10.1111/j.1749-6632.2003.tb07230.x;
Goellner G.M., DeMarco S.J., Strehler E.E.;
"Characterization of PISP, a novel single-PDZ protein that binds to all
plasma membrane Ca2+-ATPase b-splice variants.";
Ann. N. Y. Acad. Sci. 986:461-471(2003).
[10]
INTERACTION WITH ATP7A, AND IDENTIFICATION OF ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2).
PubMed=16051599; DOI=10.1074/jbc.m505889200;
Stephenson S.E., Dubach D., Lim C.M., Mercer J.F., La Fontaine S.;
"A single PDZ domain protein interacts with the Menkes copper ATPase,
ATP7A. A new protein implicated in copper homeostasis.";
J. Biol. Chem. 280:33270-33279(2005).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
FUNCTION, INTERACTION WITH PLEKHA7, AND SUBCELLULAR LOCATION.
PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
"A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
Promote alpha-Toxin Cytotoxicity.";
Cell Rep. 25:2132-2147(2018).
[13]
VARIANT TYR-81.
PubMed=23033978; DOI=10.1056/nejmoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: Mediates docking of ADAM10 to zonula adherens by interacting
with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10-
binding protein TSPAN33. {ECO:0000269|PubMed:30463011}.
-!- SUBUNIT: Interacts with ATP2B1, ATP2B2, ATP2B3, ATP2B4 and ATP7A
(PubMed:12763866, PubMed:16051599). Interacts with PLEKHA7 (via WW
domains) at zonula adherens; this interaction is essential for the
interaction between PLEKHA7 and the ADAM10-binding protein TSPAN33
(PubMed:30463011). {ECO:0000269|PubMed:12763866,
ECO:0000269|PubMed:16051599, ECO:0000269|PubMed:30463011}.
-!- INTERACTION:
Q5EBL8; Q04656: ATP7A; NbExp=4; IntAct=EBI-1644207, EBI-7706409;
Q5EBL8; Q86UL8-2: MAGI2; NbExp=3; IntAct=EBI-1644207, EBI-12081182;
Q5EBL8; Q9HAU0: PLEKHA5; NbExp=11; IntAct=EBI-1644207, EBI-945934;
-!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
{ECO:0000269|PubMed:12763866}. Cell junction, adherens junction
{ECO:0000269|PubMed:30463011}. Cell membrane
{ECO:0000269|PubMed:30463011}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=AIPP1a;
IsoId=Q5EBL8-1; Sequence=Displayed;
Name=2; Synonyms=AIPP1b;
IsoId=Q5EBL8-2; Sequence=VSP_015077;
-!- TISSUE SPECIFICITY: Widely expressed (at protein level).
{ECO:0000269|PubMed:12763866}.
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EMBL; AF151061; AAF36147.1; -; mRNA.
EMBL; AY358829; AAQ89188.1; -; mRNA.
EMBL; AK024746; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CR457149; CAG33430.1; -; mRNA.
EMBL; BX537725; CAD97820.1; -; mRNA.
EMBL; AL357752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471132; EAX05345.1; -; Genomic_DNA.
EMBL; CH471132; EAX05346.1; -; Genomic_DNA.
EMBL; BC012996; AAH12996.1; -; mRNA.
EMBL; BC089433; AAH89433.1; -; mRNA.
CCDS; CCDS14400.1; -. [Q5EBL8-1]
RefSeq; NP_057568.1; NM_016484.4. [Q5EBL8-1]
RefSeq; XP_011529275.1; XM_011530973.2.
RefSeq; XP_016885057.1; XM_017029568.1.
SMR; Q5EBL8; -.
BioGRID; 119405; 28.
CORUM; Q5EBL8; -.
IntAct; Q5EBL8; 22.
MINT; Q5EBL8; -.
STRING; 9606.ENSP00000239666; -.
iPTMnet; Q5EBL8; -.
PhosphoSitePlus; Q5EBL8; -.
BioMuta; PDZD11; -.
DMDM; 73621365; -.
EPD; Q5EBL8; -.
jPOST; Q5EBL8; -.
MassIVE; Q5EBL8; -.
MaxQB; Q5EBL8; -.
PaxDb; Q5EBL8; -.
PeptideAtlas; Q5EBL8; -.
PRIDE; Q5EBL8; -.
ProteomicsDB; 62764; -. [Q5EBL8-1]
ProteomicsDB; 62765; -. [Q5EBL8-2]
Antibodypedia; 581; 72 antibodies.
DNASU; 51248; -.
Ensembl; ENST00000239666; ENSP00000239666; ENSG00000120509. [Q5EBL8-1]
Ensembl; ENST00000374454; ENSP00000363578; ENSG00000120509. [Q5EBL8-1]
GeneID; 51248; -.
KEGG; hsa:51248; -.
UCSC; uc004dyd.2; human. [Q5EBL8-1]
CTD; 51248; -.
GeneCards; PDZD11; -.
HGNC; HGNC:28034; PDZD11.
HPA; ENSG00000120509; Low tissue specificity.
MIM; 300632; gene.
neXtProt; NX_Q5EBL8; -.
OpenTargets; ENSG00000120509; -.
PharmGKB; PA134968632; -.
VEuPathDB; HostDB:ENSG00000120509.10; -.
eggNOG; KOG3528; Eukaryota.
GeneTree; ENSGT00940000153222; -.
HOGENOM; CLU_133335_0_0_1; -.
InParanoid; Q5EBL8; -.
OMA; AWIPPQD; -.
OrthoDB; 1530562at2759; -.
PhylomeDB; Q5EBL8; -.
TreeFam; TF318964; -.
PathwayCommons; Q5EBL8; -.
Reactome; R-HSA-196780; Biotin transport and metabolism.
Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
Reactome; R-HSA-425397; Transport of vitamins, nucleosides, and related molecules.
Reactome; R-HSA-6803544; Ion influx/efflux at host-pathogen interface.
Reactome; R-HSA-936837; Ion transport by P-type ATPases.
SIGNOR; Q5EBL8; -.
BioGRID-ORCS; 51248; 12 hits in 632 CRISPR screens.
ChiTaRS; PDZD11; human.
GeneWiki; PDZD11; -.
GenomeRNAi; 51248; -.
Pharos; Q5EBL8; Tbio.
PRO; PR:Q5EBL8; -.
Proteomes; UP000005640; Chromosome X.
RNAct; Q5EBL8; protein.
Bgee; ENSG00000120509; Expressed in substantia nigra and 213 other tissues.
Genevisible; Q5EBL8; HS.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0046930; C:pore complex; IMP:UniProtKB.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0045202; C:synapse; IBA:GO_Central.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019730; P:antimicrobial humoral response; TAS:Reactome.
GO; GO:0006768; P:biotin metabolic process; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
GO; GO:0007269; P:neurotransmitter secretion; IBA:GO_Central.
GO; GO:0015939; P:pantothenate metabolic process; TAS:Reactome.
GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
GO; GO:1903361; P:protein localization to basolateral plasma membrane; IBA:GO_Central.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
Gene3D; 2.30.42.10; -; 1.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF00595; PDZ; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF50156; SSF50156; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
Reference proteome; Secreted.
CHAIN 1..140
/note="PDZ domain-containing protein 11"
/id="PRO_0000058273"
DOMAIN 47..129
/note="PDZ"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
VAR_SEQ 1
/note="M -> MGWSCCLKLAGLLSLLNHFLSVLIHSSRALPE (in isoform
2)"
/evidence="ECO:0000303|PubMed:12975309"
/id="VSP_015077"
VARIANT 81
/note="S -> Y (in dbSNP:rs1245281228)"
/evidence="ECO:0000269|PubMed:23033978"
/id="VAR_069422"
SEQUENCE 140 AA; 16131 MW; 601216B821A36DCE CRC64;
MDSRIPYDDY PVVFLPAYEN PPAWIPPHER VHHPDYNNEL TQFLPRTITL KKPPGAQLGF
NIRGGKASQL GIFISKVIPD SDAHRAGLQE GDQVLAVNDV DFQDIEHSKA VEILKTAREI
SMRVRFFPYN YHRQKERTVH