VPS36_MOUSE
ID VPS36_MOUSE Reviewed; 386 AA.
AC Q91XD6; Q9CVA3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Vacuolar protein-sorting-associated protein 36;
DE AltName: Full=ESCRT-II complex subunit VPS36;
GN Name=Vps36;
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=FVB/N; TISSUE=Liver;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-161.
RC STRAIN=C57BL/6J; TISSUE=Stomach;
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, LIPID-BINDING, AND INTERACTION WITH
RP UBIQUITIN.
RX PubMed=15755741; DOI=10.1074/jbc.m501510200;
RA Slagsvold T., Aasland R., Hirano S., Bache K.G., Raiborg C., Trambaiolo D.,
RA Wakatsuki S., Stenmark H.;
RT "Eap45 in mammalian ESCRT-II binds ubiquitin via a phosphoinositide-
RT interacting GLUE domain.";
RL J. Biol. Chem. 280:19600-19606(2005).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 1-139 IN COMPLEX WITH RPS27A.
RX PubMed=17057714; DOI=10.1038/nsmb1163;
RA Hirano S., Suzuki N., Slagsvold T., Kawasaki M., Trambaiolo D., Kato R.,
RA Stenmark H., Wakatsuki S.;
RT "Structural basis of ubiquitin recognition by mammalian Eap45 GLUE
RT domain.";
RL Nat. Struct. Mol. Biol. 13:1031-1032(2006).
CC -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC required for transport 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. Its ability to
CC bind ubiquitin probably plays a role in endosomal sorting of
CC ubiquitinated cargo proteins by ESCRT complexes. The ESCRT-II complex
CC may also play a role in transcription regulation, possibly via its
CC interaction with ELL. Binds phosphoinosides such as PtdIns(3,4,5)P3.
CC {ECO:0000250|UniProtKB:Q86VN1, ECO:0000269|PubMed:15755741}.
CC -!- SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30,
CC VPS25/EAP20 and VPS36/EAP45 (By similarity). Component of the endosomal
CC sorting complex required for transport II (ESCRT-II), composed of SNF8,
CC VPS36 and two copies of VPS25 (By similarity). Interacts with VPS25,
CC SNF8, TSG101 and CHMP6 (By similarity). Interacts (via GLUE domain)
CC with ubiquitin (PubMed:15755741). Interacts with RILPL1 (via the C-
CC terminal domain); which recruits ESCRT-II to the endosome membranes (By
CC similarity). Interacts with ECPAS (By similarity).
CC {ECO:0000250|UniProtKB:P0C0A2, ECO:0000250|UniProtKB:Q86VN1,
CC ECO:0000269|PubMed:15755741}.
CC -!- INTERACTION:
CC Q91XD6; P62990: UBC; Xeno; NbExp=2; IntAct=EBI-8318017, EBI-413053;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}.
CC Late endosome {ECO:0000269|PubMed:15755741}. Membrane {ECO:0000250}.
CC Nucleus {ECO:0000250}. Note=Colocalizes with ubiquitinated proteins on
CC late endosomes. Recruited to the endosome membrane to participate in
CC vesicle formation. {ECO:0000269|PubMed:15755741}.
CC -!- DOMAIN: The GLUE domain (GRAM-like ubiquitin-binding in EAP45) mediates
CC binding to ubiquitin and phosphoinosides.
CC {ECO:0000269|PubMed:15755741}.
CC -!- SIMILARITY: Belongs to the VPS36 family. {ECO:0000305}.
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DR EMBL; BC010811; AAH10811.1; -; mRNA.
DR EMBL; AK008946; BAB25984.1; -; mRNA.
DR CCDS; CCDS22171.1; -.
DR RefSeq; NP_081614.1; NM_027338.1.
DR PDB; 2DX5; X-ray; 3.35 A; A=1-139.
DR PDBsum; 2DX5; -.
DR AlphaFoldDB; Q91XD6; -.
DR SMR; Q91XD6; -.
DR BioGRID; 213894; 7.
DR DIP; DIP-29247N; -.
DR IntAct; Q91XD6; 1.
DR STRING; 10090.ENSMUSP00000033866; -.
DR iPTMnet; Q91XD6; -.
DR PhosphoSitePlus; Q91XD6; -.
DR EPD; Q91XD6; -.
DR MaxQB; Q91XD6; -.
DR PaxDb; Q91XD6; -.
DR PRIDE; Q91XD6; -.
DR ProteomicsDB; 275182; -.
DR Antibodypedia; 24193; 73 antibodies from 20 providers.
DR DNASU; 70160; -.
DR Ensembl; ENSMUST00000033866; ENSMUSP00000033866; ENSMUSG00000031479.
DR GeneID; 70160; -.
DR KEGG; mmu:70160; -.
DR UCSC; uc009lct.1; mouse.
DR CTD; 51028; -.
DR MGI; MGI:1917410; Vps36.
DR VEuPathDB; HostDB:ENSMUSG00000031479; -.
DR eggNOG; KOG2760; Eukaryota.
DR GeneTree; ENSGT00390000017209; -.
DR HOGENOM; CLU_015433_0_0_1; -.
DR InParanoid; Q91XD6; -.
DR OMA; TLNARVW; -.
DR OrthoDB; 981902at2759; -.
DR PhylomeDB; Q91XD6; -.
DR TreeFam; TF314770; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 70160; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Vps36; mouse.
DR EvolutionaryTrace; Q91XD6; -.
DR PRO; PR:Q91XD6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91XD6; protein.
DR Bgee; ENSMUSG00000031479; Expressed in trigeminal ganglion and 241 other tissues.
DR ExpressionAtlas; Q91XD6; baseline and differential.
DR Genevisible; Q91XD6; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0000814; C:ESCRT II complex; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0031902; C:late endosome membrane; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:InterPro.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
DR GO; GO:0016197; P:endosomal transport; IC: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 Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR021648; GLUE_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR040608; Snf8/Vps36.
DR InterPro; IPR037855; Vps36.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR13128; PTHR13128; 1.
DR Pfam; PF04157; EAP30; 1.
DR Pfam; PF11605; Vps36_ESCRT-II; 1.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS51495; GLUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Endosome; Lipid-binding; Membrane;
KW Nucleus; Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..386
FT /note="Vacuolar protein-sorting-associated protein 36"
FT /id="PRO_0000215223"
FT DOMAIN 1..88
FT /note="GLUE N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT DOMAIN 105..138
FT /note="GLUE C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00828"
FT COILED 160..185
FT /evidence="ECO:0000255"
FT STRAND 17..30
FT /evidence="ECO:0007829|PDB:2DX5"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:2DX5"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2DX5"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2DX5"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2DX5"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2DX5"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2DX5"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2DX5"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2DX5"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:2DX5"
SQ SEQUENCE 386 AA; 43736 MW; 0036479499DD89C8 CRC64;
MDRFVWTSGL LEINETLVIQ QRGVRVYDGE EKIKFDAGTL LLSTHRLIWR DQKNNECCMA
IPLSQIVFIE EQAAGIGKSA KIVVHLHPAP SNKEPGPFQS SKNSYIRLSF KEHGQIEFYR
RLSEEMTQRR WETVPVSQSL QTNKGPQPGR VRAVGIVGIE RKLEEKRKET DKNISEAFED
LSKLMIKAKE MVELSKSIAN KIKEKQGDVT EDETIRFKSY LLSMGIANPV TRETYGSGTQ
YHMQLAKQLA GILQAPLEER GGIMSLTEVY CLVNRARGME LLSPEDLVNA CKMLEALKLP
IRLRVFDSGV MVIELQTHKE EEMVASALET VSERGSLTSE EFAKLVGMSV LLAKERLLLA
EKMGHLCRDD SVEGLRFYPN LFMTQN
