(data stored in ACNUC5340 zone)

SWISSPROT: MIK1_ARATH

ID   MIK1_ARATH              Reviewed;        1013 AA.
AC   Q9M0G7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAY-2019, entry version 149.
DE   RecName: Full=MDIS1-interacting receptor like kinase 1 {ECO:0000303|PubMed:26863186};
DE            Short=AtMIK1 {ECO:0000303|PubMed:26863186};
DE   AltName: Full=Leucine-rich repeat receptor-like protein kinase PXL2 {ECO:0000303|PubMed:17570668};
DE            EC=2.7.11.1 {ECO:0000305};
DE   AltName: Full=Protein PHLOEM INTERCALATED WITH XYLEM-LIKE 2 {ECO:0000303|PubMed:17570668};
DE   Flags: Precursor;
GN   Name=MIK1 {ECO:0000303|PubMed:26863186};
GN   Synonyms=PXL2 {ECO:0000303|PubMed:17570668};
GN   OrderedLocusNames=At4g28650 {ECO:0000312|Araport:AT4G28650};
GN   ORFNames=T5F17.100 {ECO:0000312|EMBL:CAB81453.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA   Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT   "Genome-wide cloning and sequence analysis of leucine-rich repeat
RT   receptor-like protein kinase genes in Arabidopsis thaliana.";
RL   BMC Genomics 11:19-19(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana
RT   reference genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17570668; DOI=10.1016/j.cub.2007.05.049;
RA   Fisher K., Turner S.;
RT   "PXY, a receptor-like kinase essential for maintaining polarity during
RT   plant vascular-tissue development.";
RL   Curr. Biol. 17:1061-1066(2007).
RN   [5]
RP   REVIEW.
RX   PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA   Wang G., Fiers M.;
RT   "CLE peptide signaling during plant development.";
RL   Protoplasma 240:33-43(2010).
RN   [6]
RP   FUNCTION, INTERACTION WITH MDIS1 AND LURE1.2, TISSUE SPECIFICITY,
RP   PHOSPHORYLATION AT THR-710; THR-741; THR-742; THR-862; SER-864;
RP   TYR-879; THR-880 AND THR-992, AND SUBUNIT.
RX   PubMed=26863186; DOI=10.1038/nature16975;
RA   Wang T., Liang L., Xue Y., Jia P.F., Chen W., Zhang M.X., Wang Y.C.,
RA   Li H.J., Yang W.C.;
RT   "A receptor heteromer mediates the male perception of female
RT   attractants in plants.";
RL   Nature 531:241-244(2016).
CC   -!- FUNCTION: Involved in the regulation of procambium maintenance and
CC       polarity during vascular-tissue development (PubMed:17570668).
CC       Involved in the pollen tube perception of the female signal
CC       (PubMed:26863186). Phosphorylates MDSI1 (PubMed:26863186).
CC       {ECO:0000269|PubMed:17570668, ECO:0000269|PubMed:26863186}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Homodimer. Interacts with MDIS1 and LURE1.2.
CC       {ECO:0000269|PubMed:26863186}.
CC   -!- INTERACTION:
CC       Q9LT96:At5g49770; NbExp=2; IntAct=EBI-16196224, EBI-17123993;
CC       Q9FL28:FLS2; NbExp=3; IntAct=EBI-16196224, EBI-1799448;
CC       Q4VP08:LURE1.2; NbExp=4; IntAct=EBI-16196224, EBI-16196186;
CC       C0LGU7:MDIS1; NbExp=7; IntAct=EBI-16196224, EBI-16196163;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in pollen tubes.
CC       {ECO:0000269|PubMed:26863186}.
CC   -!- PTM: Autophosphorylation induced by the interaction with LURE1.2.
CC       {ECO:0000269|PubMed:26863186}.
CC   -!- DISRUPTION PHENOTYPE: Reduced procambial cells number, and
CC       adjacent or interspersed xylem and phloem formation.
CC       {ECO:0000269|PubMed:17570668}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- WEB RESOURCE: Name=PlantP kinase Classification PPC;
CC       URL="http://plantsp.genomics.purdue.edu/family/class.html";
DR   EMBL; FJ708756; ACN59350.1; -; mRNA.
DR   EMBL; AL161573; CAB81453.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85518.1; -; Genomic_DNA.
DR   PIR; T10659; T10659.
DR   RefSeq; NP_194594.1; NM_119007.3.
DR   SMR; Q9M0G7; -.
DR   BioGrid; 14270; 32.
DR   DIP; DIP-61969N; -.
DR   IntAct; Q9M0G7; 31.
DR   STRING; 3702.AT4G28650.1; -.
DR   iPTMnet; Q9M0G7; -.
DR   PaxDb; Q9M0G7; -.
DR   PRIDE; Q9M0G7; -.
DR   EnsemblPlants; AT4G28650.1; AT4G28650.1; AT4G28650.
DR   GeneID; 828983; -.
DR   Gramene; AT4G28650.1; AT4G28650.1; AT4G28650.
DR   KEGG; ath:AT4G28650; -.
DR   Araport; AT4G28650; -.
DR   TAIR; locus:2139885; AT4G28650.
DR   eggNOG; ENOG410IJBE; Eukaryota.
DR   eggNOG; COG0515; LUCA.
DR   eggNOG; COG4886; LUCA.
DR   HOGENOM; HOG000116551; -.
DR   InParanoid; Q9M0G7; -.
DR   OMA; KHIITGW; -.
DR   OrthoDB; 89025at2759; -.
DR   PhylomeDB; Q9M0G7; -.
DR   PRO; PR:Q9M0G7; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9M0G7; baseline and differential.
DR   Genevisible; Q9M0G7; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR   GO; GO:0010183; P:pollen tube guidance; IGI:TAIR.
DR   GO; GO:0010067; P:procambium histogenesis; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR   Gene3D; 3.80.10.10; -; 4.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013210; LRR_N_plant-typ.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00560; LRR_1; 1.
DR   Pfam; PF13516; LRR_6; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9M0G7.
DR   SWISS-2DPAGE; Q9M0G7.
KW   ATP-binding; Cell membrane; Complete proteome; Developmental protein;
KW   Differentiation; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24   1013       MDIS1-interacting receptor like kinase 1.
FT                                /FTId=PRO_0000401293.
FT   TOPO_DOM     24    633       Extracellular. {ECO:0000255}.
FT   TRANSMEM    634    654       Helical. {ECO:0000255}.
FT   TOPO_DOM    655   1013       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       70     94       LRR 1. {ECO:0000255}.
FT   REPEAT       95    117       LRR 2. {ECO:0000255}.
FT   REPEAT      119    137       LRR 3. {ECO:0000255}.
FT   REPEAT      139    163       LRR 4. {ECO:0000255}.
FT   REPEAT      164    186       LRR 5. {ECO:0000255}.
FT   REPEAT      187    213       LRR 6. {ECO:0000255}.
FT   REPEAT      215    234       LRR 7. {ECO:0000255}.
FT   REPEAT      235    259       LRR 8. {ECO:0000255}.
FT   REPEAT      260    283       LRR 9. {ECO:0000255}.
FT   REPEAT      284    307       LRR 10. {ECO:0000255}.
FT   REPEAT      308    331       LRR 11. {ECO:0000255}.
FT   REPEAT      333    355       LRR 12. {ECO:0000255}.
FT   REPEAT      357    379       LRR 13. {ECO:0000255}.
FT   REPEAT      381    403       LRR 14. {ECO:0000255}.
FT   REPEAT      405    426       LRR 15. {ECO:0000255}.
FT   REPEAT      427    451       LRR 16. {ECO:0000255}.
FT   REPEAT      453    475       LRR 17. {ECO:0000255}.
FT   REPEAT      477    498       LRR 18. {ECO:0000255}.
FT   REPEAT      499    523       LRR 19. {ECO:0000255}.
FT   REPEAT      525    547       LRR 20. {ECO:0000255}.
FT   REPEAT      548    571       LRR 21. {ECO:0000255}.
FT   REPEAT      573    595       LRR 22. {ECO:0000255}.
FT   DOMAIN      699    983       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     705    713       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    831    831       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     728    728       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     691    691       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O22476}.
FT   MOD_RES     710    710       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     741    741       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     742    742       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     777    777       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:O22476}.
FT   MOD_RES     818    818       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:C0LGT6}.
FT   MOD_RES     862    862       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     864    864       Phosphoserine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     872    872       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:C0LGT6}.
FT   MOD_RES     879    879       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     880    880       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   MOD_RES     992    992       Phosphothreonine; by autocatalysis.
FT                                {ECO:0000269|PubMed:26863186}.
FT   CARBOHYD     61     61       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     82     82       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    101    101       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    137    137       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    146    146       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    151    151       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    155    155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    199    199       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    271    271       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    341    341       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    381    381       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    389    389       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    535    535       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    578    578       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   1013 AA;  110478 MW;  AE52A716DCC26695 CRC64;
     MKMKIIVLFL YYCYIGSTSS VLASIDNVNE LSVLLSVKST LVDPLNFLKD WKLSDTSDHC
     NWTGVRCNSN GNVEKLDLAG MNLTGKISDS ISQLSSLVSF NISCNGFESL LPKSIPPLKS
     IDISQNSFSG SLFLFSNESL GLVHLNASGN NLSGNLTEDL GNLVSLEVLD LRGNFFQGSL
     PSSFKNLQKL RFLGLSGNNL TGELPSVLGQ LPSLETAILG YNEFKGPIPP EFGNINSLKY
     LDLAIGKLSG EIPSELGKLK SLETLLLYEN NFTGTIPREI GSITTLKVLD FSDNALTGEI
     PMEITKLKNL QLLNLMRNKL SGSIPPAISS LAQLQVLELW NNTLSGELPS DLGKNSPLQW
     LDVSSNSFSG EIPSTLCNKG NLTKLILFNN TFTGQIPATL STCQSLVRVR MQNNLLNGSI
     PIGFGKLEKL QRLELAGNRL SGGIPGDISD SVSLSFIDFS RNQIRSSLPS TILSIHNLQA
     FLVADNFISG EVPDQFQDCP SLSNLDLSSN TLTGTIPSSI ASCEKLVSLN LRNNNLTGEI
     PRQITTMSAL AVLDLSNNSL TGVLPESIGT SPALELLNVS YNKLTGPVPI NGFLKTINPD
     DLRGNSGLCG GVLPPCSKFQ RATSSHSSLH GKRIVAGWLI GIASVLALGI LTIVTRTLYK
     KWYSNGFCGD ETASKGEWPW RLMAFHRLGF TASDILACIK ESNMIGMGAT GIVYKAEMSR
     SSTVLAVKKL WRSAADIEDG TTGDFVGEVN LLGKLRHRNI VRLLGFLYND KNMMIVYEFM
     LNGNLGDAIH GKNAAGRLLV DWVSRYNIAL GVAHGLAYLH HDCHPPVIHR DIKSNNILLD
     ANLDARIADF GLARMMARKK ETVSMVAGSY GYIAPEYGYT LKVDEKIDIY SYGVVLLELL
     TGRRPLEPEF GESVDIVEWV RRKIRDNISL EEALDPNVGN CRYVQEEMLL VLQIALLCTT
     KLPKDRPSMR DVISMLGEAK PRRKSNSNEE NTSRSLAEKH SSVFSTSPVN GLL
//

If you have problems or comments...

PBIL Back to PBIL home page