SNF8_MOUSE
ID SNF8_MOUSE Reviewed; 258 AA.
AC Q9CZ28; A2A6M2;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Vacuolar-sorting protein SNF8;
DE AltName: Full=ESCRT-II complex subunit VPS22;
GN Name=Snf8; Synonyms=D11Moh34;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Spleen;
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).
CC -!- FUNCTION: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II), which is required for multivesicular body
CC (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC MVB pathway mediates delivery of transmembrane proteins into the lumen
CC of the lysosome for degradation. The ESCRT-II complex is probably
CC involved in the recruitment of the ESCRT-III complex. The ESCRT-II
CC complex may also play a role in transcription regulation by
CC participating in derepression of transcription by RNA polymerase II,
CC possibly via its interaction with ELL. Required for degradation of both
CC endocytosed EGF and EGFR, but not for the EGFR ligand-mediated
CC internalization. Required for the exosomal release of SDCBP, CD63 and
CC syndecan (By similarity). {ECO:0000250|UniProtKB:Q96H20}.
CC -!- SUBUNIT: Component of the endosomal sorting complex required for
CC transport II (ESCRT-II), composed of SNF8, VPS25 and VPS36. SNF8 is
CC essential for the stability of the ESCRT-II complex. ESCRT-II interacts
CC with ELL. Interacts with TSG101 (via the C-terminal domain). Interacts
CC with RILPL1 (via the N-terminal domain); which recruits ESCRT-II to the
CC endosome membranes. Interacts with 14-3-3 proteins (By similarity).
CC {ECO:0000250|UniProtKB:Q96H20}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC {ECO:0000250}. Nucleus {ECO:0000305}. Late endosome membrane
CC {ECO:0000250}. Note=Recruited to the endosome membrane to participate
CC in vesicle formation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF8 family. {ECO:0000305}.
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DR EMBL; AK013058; BAB28626.1; -; mRNA.
DR EMBL; AL603682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003938; AAH03938.1; -; mRNA.
DR CCDS; CCDS25288.1; -.
DR RefSeq; NP_291046.1; NM_033568.2.
DR AlphaFoldDB; Q9CZ28; -.
DR SMR; Q9CZ28; -.
DR BioGRID; 205435; 10.
DR IntAct; Q9CZ28; 4.
DR STRING; 10090.ENSMUSP00000006217; -.
DR iPTMnet; Q9CZ28; -.
DR PhosphoSitePlus; Q9CZ28; -.
DR EPD; Q9CZ28; -.
DR MaxQB; Q9CZ28; -.
DR PaxDb; Q9CZ28; -.
DR PeptideAtlas; Q9CZ28; -.
DR PRIDE; Q9CZ28; -.
DR ProteomicsDB; 261289; -.
DR Antibodypedia; 30335; 197 antibodies from 23 providers.
DR DNASU; 27681; -.
DR Ensembl; ENSMUST00000006217; ENSMUSP00000006217; ENSMUSG00000006058.
DR GeneID; 27681; -.
DR KEGG; mmu:27681; -.
DR UCSC; uc007lbb.1; mouse.
DR CTD; 11267; -.
DR MGI; MGI:1343161; Snf8.
DR VEuPathDB; HostDB:ENSMUSG00000006058; -.
DR eggNOG; KOG3341; Eukaryota.
DR GeneTree; ENSGT00390000007843; -.
DR InParanoid; Q9CZ28; -.
DR OMA; SNTEQGC; -.
DR OrthoDB; 869548at2759; -.
DR PhylomeDB; Q9CZ28; -.
DR TreeFam; TF105950; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 27681; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Snf8; mouse.
DR PRO; PR:Q9CZ28; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CZ28; protein.
DR Bgee; ENSMUSG00000006058; Expressed in embryonic brain and 258 other tissues.
DR ExpressionAtlas; Q9CZ28; baseline and differential.
DR Genevisible; Q9CZ28; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0000814; C:ESCRT II complex; ISO:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0016247; F:channel regulator activity; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISO:MGI.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0042176; P:regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0061635; P:regulation of protein complex stability; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:1903772; P:regulation of viral budding via host ESCRT complex; ISO:MGI.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR016689; ESCRT-2_cplx_Snf8.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12806; PTHR12806; 1.
DR Pfam; PF04157; EAP30; 1.
DR PIRSF; PIRSF017215; ESCRT2_Vps22; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Methylation; Nucleus;
KW Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..258
FT /note="Vacuolar-sorting protein SNF8"
FT /id="PRO_0000215210"
FT COILED 27..53
FT /evidence="ECO:0000255"
FT MOD_RES 4
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96H20"
SQ SEQUENCE 258 AA; 28886 MW; FD64947ED7815D5E CRC64;
MHRRGVGAGA IAKKKLAEAK YKERGTVLAE DQLAQMSKQL DMFKTNLEEF ASKHKQEIRK
NPEFRVQFQD MCATIGVDPL ASGKGFWSEM LGVGDFYYEL GVQIIEVCLA LKHRNGGLIT
LEELHQQVLK GRGKFAQDVS QDDLIRAIKK LKALGTGFGI IPVGGTYLIQ SVPAELNMDH
TVVLQLAEKN GYVTVSEIKT SLKWETERAR QVLEHLLKEG LAWLDLQAPG EAHYWLPALF
TDLYSQEISA EEAKEAFP
