OSTP_MOUSE
ID OSTP_MOUSE Reviewed; 294 AA.
AC P10923; P19008; Q91VH4;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Osteopontin;
DE AltName: Full=2AR;
DE AltName: Full=Bone sialoprotein 1;
DE AltName: Full=Calcium oxalate crystal growth inhibitor protein;
DE AltName: Full=Early T-lymphocyte activation 1 protein;
DE AltName: Full=Minopontin;
DE AltName: Full=Secreted phosphoprotein 1;
DE Short=SPP-1;
DE Flags: Precursor;
GN Name=Spp1; Synonyms=Eta-1, Op, Spp-1;
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].
RX PubMed=2722855; DOI=10.1016/s0021-9258(18)60584-8;
RA Craig A.M., Smith J.H., Denhardt D.T.;
RT "Osteopontin, a transformation-associated cell adhesion phosphoprotein, is
RT induced by 12-O-tetradecanoylphorbol 13-acetate in mouse epidermis.";
RL J. Biol. Chem. 264:9682-9689(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2787378; DOI=10.1084/jem.170.1.145;
RA Patarca R., Freeman G.J., Singh R.P., Wei F.-Y., Durfee T., Blattner F.,
RA Regnier D.C., Kozak C.A., Mock B.A., Morse H.C. III, Jerrells T.R.,
RA Cantor H.;
RT "Structural and functional studies of the early T lymphocyte activation 1
RT (Eta-1) gene. Definition of a novel T cell-dependent response associated
RT with genetic resistance to bacterial infection.";
RL J. Exp. Med. 170:145-161(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Macrophage;
RX PubMed=2726465; DOI=10.1093/nar/17.8.3298;
RA Miyazaki Y., Setoguchi M., Yoshida S., Higuchi Y., Akizuki S., Yamamoto S.;
RT "Nucleotide sequence of cDNA for mouse osteopontin-like protein.";
RL Nucleic Acids Res. 17:3298-3298(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=2387863; DOI=10.1016/s0021-9258(18)77320-1;
RA Miyazaki Y., Setoguchi M., Yoshida S.Y., Akizuki S., Yamamoto S.;
RT "The mouse osteopontin gene. Expression in monocytic lineages and complete
RT nucleotide sequence.";
RL J. Biol. Chem. 265:14432-14438(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 17-37.
RC TISSUE=Kidney;
RX PubMed=1414495; DOI=10.1002/jbmr.5650070905;
RA Worcester E.M., Blumenthal S.S., Beshensky A.M., Lewand D.L.;
RT "The calcium oxalate crystal growth inhibitor protein produced by mouse
RT kidney cortical cells in culture is osteopontin.";
RL J. Bone Miner. Res. 7:1029-1036(1992).
RN [7]
RP PROTEIN SEQUENCE OF 158-176, AND FUNCTION.
RX PubMed=2351930; DOI=10.1084/jem.171.6.1931;
RA Singh R.P., Patarca R., Schwartz J., Singh P., Cantor H.;
RT "Definition of a specific interaction between the early T lymphocyte
RT activation 1 (Eta-1) protein and murine macrophages in vitro and its effect
RT upon macrophages in vivo.";
RL J. Exp. Med. 171:1931-1942(1990).
RN [8]
RP FUNCTION.
RX PubMed=10657301; DOI=10.1126/science.287.5454.860;
RA Ashkar S., Weber G.F., Panoutsakopoulou V., Sanchirico M.E., Jansson M.,
RA Zawaideh S., Rittling S.R., Denhardt D.T., Glimcher M.J., Cantor H.;
RT "Eta-1 (osteopontin): an early component of type-1 (cell-mediated)
RT immunity.";
RL Science 287:860-864(2000).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-288 AND SER-290, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283 AND SER-290, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-228; SER-231;
RP SER-234; SER-283; SER-288 AND SER-290, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Pancreas;
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).
RN [12]
RP DEPHOSPHORYLATION.
RX PubMed=23427088; DOI=10.1002/jbmr.1901;
RA Narisawa S., Yadav M.C., Millan J.L.;
RT "In vivo overexpression of tissue-nonspecific alkaline phosphatase
RT increases skeletal mineralization and affects the phosphorylation status of
RT osteopontin.";
RL J. Bone Miner. Res. 28:1587-1598(2013).
CC -!- FUNCTION: Major non-collagenous bone protein that binds tightly to
CC hydroxyapatite. Appears to form an integral part of the mineralized
CC matrix. Probably important to cell-matrix interaction.
CC {ECO:0000250|UniProtKB:P31096}.
CC -!- FUNCTION: Acts as a cytokine involved in enhancing production of
CC interferon-gamma and interleukin-12 and reducing production of
CC interleukin-10 and is essential in the pathway that leads to type I
CC immunity. {ECO:0000269|PubMed:10657301, ECO:0000269|PubMed:2351930}.
CC -!- SUBUNIT: Ligand for integrin alpha-V/beta-3.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Extensively phosphorylated by FAM20C in the extracellular medium
CC at multiple sites within the S-x-E/pS motif (By similarity). The
CC phosphorylated form inhibits hydroxyapatite crystallization
CC (PubMed:23427088). Dephosphorylation via a mechanism involving
CC ALPL/TNAP promotes hydroxyapatite crystallization (PubMed:23427088).
CC {ECO:0000250|UniProtKB:P10451, ECO:0000269|PubMed:23427088}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P10451}.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2,
CC between a glutamine and the epsilon-amino group of a lysine residue,
CC forming homopolymers and heteropolymers, increasing its collagen
CC binding properties. {ECO:0000250|UniProtKB:P31096}.
CC -!- SIMILARITY: Belongs to the osteopontin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14284.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; J04806; AAA57265.1; -; mRNA.
DR EMBL; X16151; CAA34276.1; -; mRNA.
DR EMBL; X13986; CAA32165.1; -; mRNA.
DR EMBL; X51834; CAA36132.1; -; Genomic_DNA.
DR EMBL; BC014284; AAH14284.1; ALT_INIT; mRNA.
DR EMBL; BC057858; AAH57858.1; -; mRNA.
DR CCDS; CCDS19486.1; -.
DR PIR; A37818; A37818.
DR RefSeq; NP_001191162.1; NM_001204233.1.
DR RefSeq; NP_033289.2; NM_009263.3.
DR AlphaFoldDB; P10923; -.
DR BioGRID; 203467; 15.
DR IntAct; P10923; 1.
DR STRING; 10090.ENSMUSP00000108367; -.
DR GlyGen; P10923; 3 sites.
DR iPTMnet; P10923; -.
DR PhosphoSitePlus; P10923; -.
DR CPTAC; non-CPTAC-3592; -.
DR EPD; P10923; -.
DR jPOST; P10923; -.
DR PaxDb; P10923; -.
DR PeptideAtlas; P10923; -.
DR PRIDE; P10923; -.
DR ProteomicsDB; 294082; -.
DR ABCD; P10923; 7 sequenced antibodies.
DR Antibodypedia; 3695; 1494 antibodies from 49 providers.
DR DNASU; 20750; -.
DR Ensembl; ENSMUST00000031243; ENSMUSP00000031243; ENSMUSG00000029304.
DR Ensembl; ENSMUST00000112747; ENSMUSP00000108367; ENSMUSG00000029304.
DR Ensembl; ENSMUST00000112748; ENSMUSP00000108368; ENSMUSG00000029304.
DR GeneID; 20750; -.
DR KEGG; mmu:20750; -.
DR UCSC; uc008yki.2; mouse.
DR CTD; 6696; -.
DR MGI; MGI:98389; Spp1.
DR VEuPathDB; HostDB:ENSMUSG00000029304; -.
DR eggNOG; ENOG502S5R4; Eukaryota.
DR GeneTree; ENSGT00390000002509; -.
DR HOGENOM; CLU_953033_0_0_1; -.
DR InParanoid; P10923; -.
DR OrthoDB; 1280650at2759; -.
DR PhylomeDB; P10923; -.
DR TreeFam; TF350201; -.
DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 20750; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Spp1; mouse.
DR PRO; PR:P10923; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P10923; protein.
DR Bgee; ENSMUSG00000029304; Expressed in vault of skull and 257 other tissues.
DR ExpressionAtlas; P10923; baseline and differential.
DR Genevisible; P10923; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; NAS:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0006710; P:androgen catabolic process; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IDA:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:MGI.
DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:MGI.
DR GO; GO:0071498; P:cellular response to fluid shear stress; IDA:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; ISO:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:MGI.
DR GO; GO:0072044; P:collecting duct development; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
DR GO; GO:0045780; P:positive regulation of bone resorption; ISO:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR GO; GO:2000866; P:positive regulation of estradiol secretion; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0010033; P:response to organic substance; ISO:MGI.
DR GO; GO:0048545; P:response to steroid hormone; ISO:MGI.
DR GO; GO:0033280; P:response to vitamin D; ISO:MGI.
DR GO; GO:0034418; P:urate biosynthetic process; IMP:MGI.
DR DisProt; DP01448; -.
DR InterPro; IPR002038; Osteopontin.
DR InterPro; IPR019841; Osteopontin_CS.
DR PANTHER; PTHR10607; PTHR10607; 1.
DR Pfam; PF00865; Osteopontin; 1.
DR PRINTS; PR00216; OSTEOPONTIN.
DR SMART; SM00017; OSTEO; 1.
DR PROSITE; PS00884; OSTEOPONTIN; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell adhesion; Cytokine; Direct protein sequencing;
KW Glycoprotein; Phosphoprotein; Reference proteome; Secreted; Sialic acid;
KW Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..294
FT /note="Osteopontin"
FT /id="PRO_0000020322"
FT REGION 42..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 144..146
FT /note="Cell attachment site"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31096"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10451"
FT CARBOHYD 123
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 132
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 137
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="L -> P (in Ref. 2; CAA34276)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="E -> G (in Ref. 1; AAA57265)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="S -> N (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="V -> F (in Ref. 3; CAA32165 and 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="N -> D (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="D -> Y (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="D -> N (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="K -> R (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="R -> S (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="Q -> H (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="Y -> H (in Ref. 5; AAH14284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 294 AA; 32459 MW; 9D5F32D67ABC53EA CRC64;
MRLAVICFCL FGIASSLPVK VTDSGSSEEK LYSLHPDPIA TWLVPDPSQK QNLLAPQNAV
SSEEKDDFKQ ETLPSNSNES HDHMDDDDDD DDDDGDHAES EDSVDSDESD ESHHSDESDE
TVTASTQADT FTPIVPTVDV PNGRGDSLAY GLRSKSRSFQ VSDEQYPDAT DEDLTSHMKS
GESKESLDVI PVAQLLSMPS DQDNNGKGSH ESSQLDEPSL ETHRLEHSKE SQESADQSDV
IDSQASSKAS LEHQSHKFHS HKDKLVLDPK SKEDDRYLKF RISHELESSS SEVN
