ID RIN3_HUMAN Reviewed; 985 AA. AC Q8TB24; Q76LB3; Q8NF30; Q8TEE8; Q8WYP4; Q9H6A5; Q9HAG1; DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 4. DT 24-JAN-2024, entry version 175. DE RecName: Full=Ras and Rab interactor 3; DE AltName: Full=Ras interaction/interference protein 3; GN Name=RIN3; 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] (ISOFORM 1), FUNCTION, INTERACTION WITH BIN1 AND RP RAB5B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12972505; DOI=10.1242/jcs.00718; RA Kajiho H., Saito K., Tsujita K., Kontani K., Araki Y., Kurosu H., RA Katada T.; RT "RIN3: a novel Rab5 GEF interacting with amphiphysin II involved in the RT early endocytic pathway."; RL J. Cell Sci. 116:4159-4168(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167 AND 405-985 (ISOFORM 1), RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-985 (ISOFORM 4), AND VARIANT RP MET-425. RC TISSUE=Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-985 (ISOFORM 1). RC TISSUE=Eye; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 435-959 (ISOFORM 1). RC TISSUE=Leukocyte, and Spleen; RX PubMed=11733506; DOI=10.1074/jbc.m106276200; RA Saito K., Murai J., Kajiho H., Kontani K., Kurosu H., Katada T.; RT "A novel binding protein composed of homophilic tetramer exhibits unique RT properties for the small GTPase Rab5."; RL J. Biol. Chem. 277:3412-3418(2002). RN [6] RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=18486601; DOI=10.1016/j.bbrc.2008.05.027; RA Yoshikawa M., Kajiho H., Sakurai K., Minoda T., Nakagawa S., Kontani K., RA Katada T.; RT "Tyr-phosphorylation signals translocate RIN3, the small GTPase Rab5-GEF, RT to early endocytic vesicles."; RL Biochem. Biophys. Res. Commun. 372:168-172(2008). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-825 AND THR-828, AND RP INTERACTION WITH RAB31. RX PubMed=21586568; DOI=10.1074/jbc.m110.172445; RA Kajiho H., Sakurai K., Minoda T., Yoshikawa M., Nakagawa S., Fukushima S., RA Kontani K., Katada T.; RT "Characterization of RIN3 as a guanine nucleotide exchange factor for the RT Rab5 subfamily GTPase Rab31."; RL J. Biol. Chem. 286:24364-24373(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (1.11 ANGSTROMS) OF 452-467 IN COMPLEX WITH CD2AP, RP AND INTERACTION WITH CD2AP. RG Structural genomics consortium (SGC); RT "Atomic resolution crystal structure of the 2nd SH3 domain from human CD2AP RT (CMS) in complex with a proline-rich peptide from human RIN3."; RL Submitted (DEC-2011) to the PDB data bank. CC -!- FUNCTION: Ras effector protein that functions as a guanine nucleotide CC exchange (GEF) for RAB5B and RAB31, by exchanging bound GDP for free CC GTP. Required for normal RAB31 function. {ECO:0000269|PubMed:12972505, CC ECO:0000269|PubMed:21586568}. CC -!- SUBUNIT: Interacts with CD2AP, RAB5B, RAB31 and BIN1. CC {ECO:0000269|PubMed:12972505, ECO:0000269|PubMed:21586568, CC ECO:0000269|Ref.8}. CC -!- INTERACTION: CC Q8TB24; O00499: BIN1; NbExp=2; IntAct=EBI-1570523, EBI-719094; CC Q8TB24; Q9Y5K6: CD2AP; NbExp=3; IntAct=EBI-1570523, EBI-298152; CC Q8TB24; P46108: CRK; NbExp=2; IntAct=EBI-1570523, EBI-886; CC Q8TB24; P16333: NCK1; NbExp=2; IntAct=EBI-1570523, EBI-389883; CC Q8TB24; P19174: PLCG1; NbExp=3; IntAct=EBI-1570523, EBI-79387; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18486601, CC ECO:0000269|PubMed:21586568}. Cytoplasmic vesicle CC {ECO:0000269|PubMed:12972505, ECO:0000269|PubMed:18486601, CC ECO:0000269|PubMed:21586568}. Early endosome CC {ECO:0000269|PubMed:18486601}. Note=Activation of tyrosine CC phosphorylation signaling induces translocation to cytoplasmic CC vesicles. {ECO:0000269|PubMed:18486601}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8TB24-1; Sequence=Displayed; CC Name=4; CC IsoId=Q8TB24-4; Sequence=VSP_007587, VSP_007588; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12972505}. CC -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13888.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305}; CC Sequence=BAB15357.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC03432.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB081753; BAC16513.1; -; mRNA. DR EMBL; AL136332; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL159141; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK021762; BAB13888.1; ALT_SEQ; mRNA. DR EMBL; AK026092; BAB15357.1; ALT_INIT; mRNA. DR EMBL; AK074176; BAB85002.1; -; mRNA. DR EMBL; AK090451; BAC03432.1; ALT_SEQ; mRNA. DR EMBL; BC025248; AAH25248.2; -; mRNA. DR EMBL; AB060338; BAB84316.1; -; mRNA. DR CCDS; CCDS32144.1; -. [Q8TB24-1] DR PIR; T50623; T50623. DR RefSeq; NP_001306916.1; NM_001319987.1. DR RefSeq; NP_079108.3; NM_024832.4. [Q8TB24-1] DR PDB; 3U23; X-ray; 1.11 A; B=452-467. DR PDB; 4WCI; X-ray; 1.65 A; B/D/F=378-393. DR PDBsum; 3U23; -. DR PDBsum; 4WCI; -. DR AlphaFoldDB; Q8TB24; -. DR SMR; Q8TB24; -. DR BioGRID; 122974; 459. DR IntAct; Q8TB24; 419. DR MINT; Q8TB24; -. DR STRING; 9606.ENSP00000216487; -. DR MoonDB; Q8TB24; Predicted. DR iPTMnet; Q8TB24; -. DR PhosphoSitePlus; Q8TB24; -. DR BioMuta; RIN3; -. DR DMDM; 209572780; -. DR EPD; Q8TB24; -. DR jPOST; Q8TB24; -. DR MassIVE; Q8TB24; -. DR PaxDb; 9606-ENSP00000216487; -. DR PeptideAtlas; Q8TB24; -. DR ProteomicsDB; 73951; -. [Q8TB24-1] DR ProteomicsDB; 73952; -. [Q8TB24-4] DR Pumba; Q8TB24; -. DR Antibodypedia; 26773; 99 antibodies from 23 providers. DR DNASU; 79890; -. DR Ensembl; ENST00000216487.12; ENSP00000216487.7; ENSG00000100599.16. [Q8TB24-1] DR GeneID; 79890; -. DR KEGG; hsa:79890; -. DR MANE-Select; ENST00000216487.12; ENSP00000216487.7; NM_024832.5; NP_079108.3. DR UCSC; uc001yap.4; human. [Q8TB24-1] DR AGR; HGNC:18751; -. DR CTD; 79890; -. DR DisGeNET; 79890; -. DR GeneCards; RIN3; -. DR HGNC; HGNC:18751; RIN3. DR HPA; ENSG00000100599; Tissue enhanced (bone). DR MIM; 610223; gene. DR neXtProt; NX_Q8TB24; -. DR NIAGADS; ENSG00000100599; -. DR OpenTargets; ENSG00000100599; -. DR PharmGKB; PA38673; -. DR VEuPathDB; HostDB:ENSG00000100599; -. DR eggNOG; KOG2320; Eukaryota. DR GeneTree; ENSGT00940000158622; -. DR InParanoid; Q8TB24; -. DR OMA; DKESYFG; -. DR OrthoDB; 5483004at2759; -. DR PhylomeDB; Q8TB24; -. DR TreeFam; TF331067; -. DR PathwayCommons; Q8TB24; -. DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs. DR SignaLink; Q8TB24; -. DR BioGRID-ORCS; 79890; 14 hits in 1148 CRISPR screens. DR ChiTaRS; RIN3; human. DR GenomeRNAi; 79890; -. DR Pharos; Q8TB24; Tbio. DR PRO; PR:Q8TB24; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q8TB24; Protein. DR Bgee; ENSG00000100599; Expressed in granulocyte and 135 other cell types or tissues. DR ExpressionAtlas; Q8TB24; baseline and differential. DR Genevisible; Q8TB24; HS. DR GO; GO:0030424; C:axon; ISS:ARUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL. DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0030139; C:endocytic vesicle; IDA:ARUK-UCL. DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL. DR GO; GO:0031982; C:vesicle; IDA:ARUK-UCL. DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0006897; P:endocytosis; NAS:UniProtKB. DR GO; GO:0060755; P:negative regulation of mast cell chemotaxis; IMP:ARUK-UCL. DR GO; GO:0002091; P:negative regulation of receptor internalization; IMP:ARUK-UCL. DR GO; GO:0097494; P:regulation of vesicle size; IDA:ARUK-UCL. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd16130; RA_Rin3; 1. DR CDD; cd10395; SH2_RIN3; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 1.20.1050.80; VPS9 domain; 1. DR InterPro; IPR000159; RA_dom. DR InterPro; IPR035869; RIN3_SH2. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR003123; VPS9. DR InterPro; IPR045046; Vps9-like. DR InterPro; IPR037191; VPS9_dom_sf. DR PANTHER; PTHR23101; RAB GDP/GTP EXCHANGE FACTOR; 1. DR PANTHER; PTHR23101:SF58; RAS AND RAB INTERACTOR 3; 1. DR Pfam; PF02204; VPS9; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00167; VPS9; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF109993; VPS9 domain; 1. DR PROSITE; PS50200; RA; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS51205; VPS9; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle; KW Endosome; GTPase activation; Reference proteome; SH2 domain. FT CHAIN 1..985 FT /note="Ras and Rab interactor 3" FT /id="PRO_0000191322" FT DOMAIN 63..158 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 703..846 FT /note="VPS9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00550" FT DOMAIN 877..963 FT /note="Ras-associating" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 183..202 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 251..293 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..531 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 587..732 FT /note="Interaction with RAB5B" FT /evidence="ECO:0000269|PubMed:12972505" FT COMPBIAS 275..293 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..336 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..382 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..444 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 501..531 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 878..903 FT /note="DFICVSYLEPEQQARTLASRADTQAQ -> VRPESGRGPVGPCPRHHPCCLL FT AKEP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_007587" FT VAR_SEQ 904..985 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_007588" FT VARIANT 111 FT /note="E -> K (in dbSNP:rs2274542)" FT /id="VAR_046645" FT VARIANT 215 FT /note="H -> L (in dbSNP:rs3829947)" FT /id="VAR_059960" FT VARIANT 215 FT /note="H -> P (in dbSNP:rs3829947)" FT /id="VAR_046646" FT VARIANT 215 FT /note="H -> R (in dbSNP:rs3829947)" FT /id="VAR_059961" FT VARIANT 425 FT /note="T -> I (in dbSNP:rs3742717)" FT /id="VAR_052946" FT VARIANT 425 FT /note="T -> M (in dbSNP:rs3742717)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_046647" FT VARIANT 613 FT /note="G -> A (in dbSNP:rs12434929)" FT /id="VAR_046648" FT MUTAGEN 825 FT /note="Y->A: Strongly reduced guanine nucleotide exchange FT factor activity toward RAB31; when associated with A-828." FT /evidence="ECO:0000269|PubMed:21586568" FT MUTAGEN 828 FT /note="T->A: Strongly reduced guanine nucleotide exchange FT factor activity toward RAB31; when associated with A-825." FT /evidence="ECO:0000269|PubMed:21586568" FT CONFLICT 742 FT /note="I -> F (in Ref. 4; AAH25248)" FT /evidence="ECO:0000305" FT CONFLICT 965 FT /note="Missing (in Ref. 3; BAB15357 and 4; AAH25248)" FT /evidence="ECO:0000305" SQ SEQUENCE 985 AA; 107854 MW; A8949EA0D61570BB CRC64; MIRHAGAPAR GDPTGPVPVV GKGEEEEEED GMRLCLPANP KNCLPHRRGI SILEKLIKTC PVWLQLSLGQ AEVARILHRV VAGMFLVRRD SSSKQLVLCV HFPSLNESSA EVLEYTIKEE KSILYLEGSA LVFEDIFRLI AFYCVSRDLL PFTLRLPQAI LEASSFTDLE TIANLGLGFW DSSLNPPQER GKPAEPPRDR APGFPLVSSL RPTAHDANCA CEIELSVGND RLWFVNPIFI EDCSSALPTD QPPLGNCPAR PLPPTSDATS PTSRWAPRRP PPPPPVLPLQ PCSPAQPPVL PALAPAPACP LPTSPPVPAP HVTPHAPGPP DHPNQPPMMT CERLPCPTAG LGPLREEAMK PGAASSPLQQ VPAPPLPAKK NLPTAPPRRR VSERVSLEDQ SPGMAAEGDQ LSLPPQGTSD GPEDTPREST EQGQDTEVKA SDPHSMPELP RTAKQPPVPP PRKKRISRQL ASTLPAPLEN AELCTQAMAL ETPTPGPPRE GQSPASQAGT QHPPAQATAH SQSSPEFKGS LASLSDSLGV SVMATDQDSY STSSTEEELE QFSSPSVKKK PSMILGKARH RLSFASFSSM FHAFLSNNRK LYKKVVELAQ DKGSYFGSLV QDYKVYSLEM MARQTSSTEM LQEIRTMMTQ LKSYLLQSTE LKALVDPALH SEEELEAIVE SALYKCVLKP LKEAINSCLH QIHSKDGSLQ QLKENQLVIL ATTTTDLGVT TSVPEVPMME KILQKFTSMH KAYSPEKKIS ILLKTCKLIY DSMALGNPGK PYGADDFLPV LMYVLARSNL TEMLLNVEYM MELMDPALQL GEGSYYLTTT YGALEHIKSY DKITVTRQLS VEVQDSIHRW ERRRTLNKAR ASRSSVQDFI CVSYLEPEQQ ARTLASRADT QAQALCAQCA EKFAVERPQA HRLFVLVDGR CFQLADDALP HCIKGYLLRS EPKRDFHFVY RPLDGGGGGG GGSPPCLVVR EPNFL //