VPS35_MOUSE
ID VPS35_MOUSE Reviewed; 796 AA.
AC Q9EQH3; Q61123;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Vacuolar protein sorting-associated protein 35;
DE AltName: Full=Maternal-embryonic 3;
DE AltName: Full=Vesicle protein sorting 35;
GN Name=Vps35; Synonyms=Mem3;
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].
RC TISSUE=Embryo, and Embryonic carcinoma;
RX PubMed=8678978; DOI=10.1007/s003359900174;
RA Hwang S.-Y., Benjamin L.E., Oh B., Rothstein J.L., Ackerman S.L.,
RA Beddington R.S.P., Solter D., Knowles B.B.;
RT "Genetic mapping and embryonic expression of a novel, maternally
RT transcribed gene Mem3.";
RL Mamm. Genome 7:586-590(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11112353; DOI=10.1006/geno.2000.6380;
RA Zhang P., Yu L., Gao J., Fu Q., Dai F., Zhao Y., Zheng L., Zhao S.;
RT "Cloning and characterization of human VPS35 and mouse Vps35 and mapping of
RT VPS35 to human chromosome 16q13-q21.";
RL Genomics 70:253-257(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PROTEIN SEQUENCE OF 91-107; 218-226; 297-305; 313-323; 372-382; 404-417 AND
RP 574-582, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH VPS26B.
RX PubMed=16190980; DOI=10.1111/j.1600-0854.2005.00328.x;
RA Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C., Gleeson P.A.,
RA Wicking C., Teasdale R.D.;
RT "A novel mammalian retromer component, Vps26B.";
RL Traffic 6:991-1001(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP SUBUNIT.
RX PubMed=21040701; DOI=10.1016/j.bbrc.2010.10.121;
RA Kim E., Lee Y., Lee H.J., Kim J.S., Song B.S., Huh J.W., Lee S.R.,
RA Kim S.U., Kim S.H., Hong Y., Shim I., Chang K.T.;
RT "Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin
RT trafficking.";
RL Biochem. Biophys. Res. Commun. 403:167-171(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [10]
RP SUBUNIT.
RX PubMed=20875039; DOI=10.1111/j.1600-0854.2010.01124.x;
RA Norwood S.J., Shaw D.J., Cowieson N.P., Owen D.J., Teasdale R.D.,
RA Collins B.M.;
RT "Assembly and solution structure of the core retromer protein complex.";
RL Traffic 12:56-71(2011).
RN [11]
RP SUBUNIT.
RX PubMed=21920005; DOI=10.1111/j.1600-0854.2011.01284.x;
RA Bugarcic A., Zhe Y., Kerr M.C., Griffin J., Collins B.M., Teasdale R.D.;
RT "Vps26A and Vps26B subunits define distinct retromer complexes.";
RL Traffic 12:1759-1773(2011).
RN [12]
RP INTERACTION WITH LRRK2.
RX PubMed=23395371; DOI=10.1016/j.neuron.2012.11.033;
RA MacLeod D.A., Rhinn H., Kuwahara T., Zolin A., Di Paolo G., McCabe B.D.,
RA MacCabe B.D., Marder K.S., Honig L.S., Clark L.N., Small S.A.,
RA Abeliovich A.;
RT "RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting and
RT Parkinson's disease risk.";
RL Neuron 77:425-439(2013).
RN [13]
RP INTERACTION WITH SORCS2, AND TISSUE SPECIFICITY.
RX PubMed=28469074; DOI=10.1172/jci.insight.88995;
RA Ma Q., Yang J., Milner T.A., Vonsattel J.G., Palko M.E., Tessarollo L.,
RA Hempstead B.L.;
RT "SorCS2-mediated NR2A trafficking regulates motor deficits in Huntington's
RT disease.";
RL JCI Insight 2:0-0(2017).
CC -!- FUNCTION: Acts as component of the retromer cargo-selective complex
CC (CSC). The CSC is believed to be the core functional component of
CC retromer or respective retromer complex variants acting to prevent
CC missorting of selected transmembrane cargo proteins into the lysosomal
CC degradation pathway. The recruitment of the CSC to the endosomal
CC membrane involves RAB7A and SNX3. The CSC seems to associate with the
CC cytoplasmic domain of cargo proteins predominantly via VPS35; however,
CC these interactions seem to be of low affinity and retromer SNX proteins
CC may also contribute to cargo selectivity thus questioning the classical
CC function of the CSC. The SNX-BAR retromer mediates retrograde transport
CC of cargo proteins from endosomes to the trans-Golgi network (TGN) and
CC is involved in endosome-to-plasma membrane transport for cargo protein
CC recycling. The SNX3-retromer mediates the retrograde transport of WLS
CC distinct from the SNX-BAR retromer pathway. The SNX27-retromer is
CC believed to be involved in endosome-to-plasma membrane trafficking and
CC recycling of a broad spectrum of cargo proteins. The CSC seems to act
CC as recruitment hub for other proteins, such as the WASH complex and
CC TBC1D5 (Probable). Required for retrograde transport of lysosomal
CC enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of
CC the polymeric immunoglobulin receptor (pIgR-pIgA). Required for
CC endosomal localization of WASHC2 and mediates the association of the
CC CSC with the WASH complex (By similarity).
CC {ECO:0000250|UniProtKB:Q96QK1}.
CC -!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
CC complex (CSC), also described as vacuolar protein sorting subcomplex
CC (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35. The CSC has
CC a highly elongated structure with VPS26 and VPS29 binding independently
CC at opposite distal ends of VPS35 as central platform (PubMed:21040701,
CC PubMed:20875039, PubMed:21920005). The CSC is believed to associate
CC with variable sorting nexins to form functionally distinct retromer
CC complex variants. The originally described retromer complex (also
CC called SNX-BAR retromer) is a pentamer containing the CSC and a
CC heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2
CC and SNX5 or SNX6 (also called SNX-BAR subcomplex); the affinity between
CC the respective CSC and SNX-BAR subcomplexes is low. The CSC associates
CC with SNX3 to form a SNX3-retromer complex. The CSC associates with
CC SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-
CC retromer complex (Probable). Interacts with VPS26A, VPS29, VPS26B and
CC LRRK2 (PubMed:16190980, PubMed:21040701, PubMed:20875039,
CC PubMed:21920005, PubMed:23395371). Interacts with SNX1, SNX2, IGF2R,
CC SNX3, GOLPH3, SLC11A2, WASHC2, FKBP15, WASHC1, EHD1. Interacts with
CC MAGEL2; leading to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase
CC complex retromer-containing endosomes (By similarity). Interacts with
CC SORCS2 (PubMed:28469074). {ECO:0000250|UniProtKB:Q96QK1,
CC ECO:0000269|PubMed:16190980, ECO:0000269|PubMed:20875039,
CC ECO:0000269|PubMed:21040701, ECO:0000269|PubMed:21920005,
CC ECO:0000269|PubMed:23395371, ECO:0000269|PubMed:28469074}.
CC -!- INTERACTION:
CC Q9EQH3; O88307: Sorl1; NbExp=2; IntAct=EBI-775825, EBI-7540114;
CC Q9EQH3; Q6PHU5: Sort1; NbExp=3; IntAct=EBI-775825, EBI-6985663;
CC Q9EQH3; P40336-1: Vps26a; NbExp=2; IntAct=EBI-775825, EBI-15553779;
CC Q9EQH3; Q9QZ88: Vps29; NbExp=5; IntAct=EBI-775825, EBI-8334188;
CC Q9EQH3; Q9QZ88-1: Vps29; NbExp=3; IntAct=EBI-775825, EBI-15553808;
CC Q9EQH3; Q5T1M5: FKBP15; Xeno; NbExp=3; IntAct=EBI-775825, EBI-5235934;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Endosome
CC {ECO:0000250|UniProtKB:Q96QK1}. Early endosome {ECO:0000305}. Late
CC endosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in striatum (at protein level)
CC (PubMed:28469074). Ubiquitous. Highly expressed in fat tissue, testis,
CC brain, kidney, thymus, liver and pancreas, and at lower levels in
CC heart, intestine and skeletal muscle. Detected in oocytes, pre-
CC implantation embryos and at 6.5-12.5 dpc.
CC {ECO:0000269|PubMed:28469074}.
CC -!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18153.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U47024; AAB18153.1; ALT_FRAME; mRNA.
DR EMBL; AF226323; AAG40621.1; -; mRNA.
DR EMBL; BC005469; AAH05469.1; -; mRNA.
DR EMBL; BC006637; AAH06637.1; -; mRNA.
DR CCDS; CCDS40421.1; -.
DR RefSeq; NP_075373.1; NM_022997.4.
DR PDB; 6VAB; EM; 4.90 A; B/D=1-796.
DR PDB; 6VAC; EM; 5.70 A; A=1-796.
DR PDBsum; 6VAB; -.
DR PDBsum; 6VAC; -.
DR AlphaFoldDB; Q9EQH3; -.
DR SMR; Q9EQH3; -.
DR BioGRID; 211137; 32.
DR CORUM; Q9EQH3; -.
DR DIP; DIP-32210N; -.
DR IntAct; Q9EQH3; 33.
DR MINT; Q9EQH3; -.
DR STRING; 10090.ENSMUSP00000034131; -.
DR iPTMnet; Q9EQH3; -.
DR PhosphoSitePlus; Q9EQH3; -.
DR SwissPalm; Q9EQH3; -.
DR EPD; Q9EQH3; -.
DR jPOST; Q9EQH3; -.
DR MaxQB; Q9EQH3; -.
DR PaxDb; Q9EQH3; -.
DR PRIDE; Q9EQH3; -.
DR ProteomicsDB; 297815; -.
DR Antibodypedia; 28023; 257 antibodies from 41 providers.
DR DNASU; 65114; -.
DR Ensembl; ENSMUST00000034131; ENSMUSP00000034131; ENSMUSG00000031696.
DR GeneID; 65114; -.
DR KEGG; mmu:65114; -.
DR UCSC; uc009mpo.1; mouse.
DR CTD; 55737; -.
DR MGI; MGI:1890467; Vps35.
DR VEuPathDB; HostDB:ENSMUSG00000031696; -.
DR eggNOG; KOG1107; Eukaryota.
DR GeneTree; ENSGT00390000007315; -.
DR HOGENOM; CLU_005836_1_0_1; -.
DR InParanoid; Q9EQH3; -.
DR OMA; WWVVENP; -.
DR OrthoDB; 316875at2759; -.
DR PhylomeDB; Q9EQH3; -.
DR TreeFam; TF105659; -.
DR Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
DR BioGRID-ORCS; 65114; 31 hits in 75 CRISPR screens.
DR ChiTaRS; Vps35; mouse.
DR PRO; PR:Q9EQH3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9EQH3; protein.
DR Bgee; ENSMUSG00000031696; Expressed in medial ganglionic eminence and 255 other tissues.
DR ExpressionAtlas; Q9EQH3; baseline and differential.
DR Genevisible; Q9EQH3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISA:MGI.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0099073; C:mitochondrion-derived vesicle; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ParkinsonsUK-UCL.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
DR GO; GO:0030906; C:retromer, cargo-selective complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097422; C:tubular endosome; ISS:UniProtKB.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0007040; P:lysosome organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
DR GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:1902823; P:negative regulation of late endosome to lysosome transport; ISO:MGI.
DR GO; GO:1905166; P:negative regulation of lysosomal protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032463; P:negative regulation of protein homooligomerization; IMP:ParkinsonsUK-UCL.
DR GO; GO:1903828; P:negative regulation of protein localization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
DR GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031648; P:protein destabilization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR GO; GO:0033365; P:protein localization to organelle; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; ISO:MGI.
DR GO; GO:1902950; P:regulation of dendritic spine maintenance; ISO:MGI.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:2000331; P:regulation of terminal button organization; ISO:MGI.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IDA:SynGO.
DR GO; GO:0045056; P:transcytosis; ISS:UniProtKB.
DR GO; GO:0006624; P:vacuolar protein processing; ISA:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:ParkinsonsUK-UCL.
DR Gene3D; 1.25.40.660; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR005378; Vps35.
DR InterPro; IPR042491; Vps35_C.
DR PANTHER; PTHR11099; PTHR11099; 1.
DR Pfam; PF03635; Vps35; 1.
DR PIRSF; PIRSF009375; Retromer_Vps35; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Endosome; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..796
FT /note="Vacuolar protein sorting-associated protein 35"
FT /id="PRO_0000065897"
FT REGION 25..44
FT /note="Interaction with SNX3"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 205..215
FT /note="Interaction with SNX3"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 438..796
FT /note="Interaction with SLC11A2"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 500..693
FT /note="Interaction with IGF2R cytoplasmic domain"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT REGION 776..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96QK1"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 791
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:19131326"
SQ SEQUENCE 796 AA; 91713 MW; 2ABD338111D641CC CRC64;
MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP
KSYYELYMAI SDELHYLEVY LTDEFAKGRK VADLYELVQY AGNIIPRLYL LITVGVVYVK
SFPQSRKDIL KDLVEMCRGV QHPLRGLFLR NYLLQCTRNI LPDEGEPTDE ETTGDISDSM
DFVLLNFAEM NKLWVRMQHQ GHSRDREKRE RERQELRILV GTNLVRLSQL EGVNVERYKQ
IVLTGILEQV VNCRDALAQE YLMECIIQVF PDEFHLQTLN PFLRACAELH QNVNVKNIII
ALIDRLALFA HREDGPGIPA EIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL QVSLINLAMK
CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR LLKIPVDTYN NILTVLKLKH
FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE IVSQDQVDSI MNLVSTLIQD QPDQPVEDPD
PEDFADEQSL VGRFIHLLRS DDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA
FRYKENSQMD DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE
TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR TQCALAASKL
LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL KKALKIANQC MDPSLQVQLF
IEILNRYIYF YEKENDAVTI QVLNQLIQKI REDLPNLESS EETEQINKHF HNTLEHLRSR
RESPESEGPI YEGLIL
