ID VPS11_MOUSE Reviewed; 941 AA. AC Q91W86; Q5FWZ1; Q9DBX8; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 11-DEC-2019, entry version 155. DE RecName: Full=Vacuolar protein sorting-associated protein 11 homolog; GN Name=Vps11; 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; TISSUE=Lung; 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 MRNA]. RC TISSUE=Eye, and Salivary 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Kidney, Liver, Lung, 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 [4] RP SUBUNIT. RX PubMed=21411634; DOI=10.1091/mbc.e10-10-0799; RA Zlatic S.A., Tornieri K., L'Hernault S.W., Faundez V.; RT "Clathrin-dependent mechanisms modulate the subcellular distribution of RT class C Vps/HOPS tether subunits in polarized and nonpolarized cells."; RL Mol. Biol. Cell 22:1699-1715(2011). RN [5] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-904, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [6] RP SUBUNIT, AND INTERACTION WITH RAB5C. RX PubMed=25266290; DOI=10.1111/tra.12232; RA Perini E.D., Schaefer R., Stoeter M., Kalaidzidis Y., Zerial M.; RT "Mammalian CORVET is required for fusion and conversion of distinct early RT endosome subpopulations."; RL Traffic 15:1366-1389(2014). CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to CC lysosomal compartments including the endocytic membrane transport and CC autophagic pathways. Believed to act as a core component of the CC putative HOPS and CORVET endosomal tethering complexes which are CC proposed to be involved in the Rab5-to-Rab7 endosome conversion CC probably implicating MON1A/B, and via binding SNAREs and SNARE CC complexes to mediate tethering and docking events during SNARE-mediated CC membrane fusion. The HOPS complex is proposed to be recruited to Rab7 CC on the late endosomal membrane and to regulate late endocytic, CC phagocytic and autophagic traffic towards lysosomes. The CORVET complex CC is proposed to function as a Rab5 effector to mediate early endosome CC fusion probably in specific endosome subpopulations. Required for CC fusion of endosomes and autophagosomes with lysosomes. Involved in CC cargo transport from early to late endosomes and required for the CC transition from early to late endosomes (By similarity). CC {ECO:0000250|UniProtKB:Q9H270}. CC -!- SUBUNIT: Core component of at least two putative endosomal tethering CC complexes, the homotypic fusion and vacuole protein sorting (HOPS) CC complex and the class C core vacuole/endosome tethering (CORVET) CC complex. Their common core is composed of the class C Vps proteins CC VPS11, VPS16, VPS18 and VPS33A, which in HOPS further associates with CC VPS39 and VPS41 and in CORVET with VPS8 and TGFBRAP1 (PubMed:25266290). CC Interacts with RAB5C (PubMed:25266290). Interacts with TGFBRAP1, MON1B, CC STX7, STX17, ECPAS, EZR, RDX, MSN (By similarity). Associates with CC adaptor protein complex 3 (AP-3) and clathrin:AP-3 complexes CC (PubMed:21411634). {ECO:0000250|UniProtKB:Q9H270, CC ECO:0000269|PubMed:21411634, ECO:0000269|PubMed:25266290, CC ECO:0000305|PubMed:25266290}. CC -!- INTERACTION: CC Q9H9C1:VIPAS39 (xeno); NbExp=3; IntAct=EBI-2527812, EBI-749080; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein CC {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000305}. CC Lysosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane CC protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000305}. CC Cytoplasmic vesicle {ECO:0000305}. Early endosome {ECO:0000305}. CC Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle, CC clathrin-coated vesicle {ECO:0000305}. CC -!- SIMILARITY: Belongs to the VPS11 family. {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; AK004695; BAB23481.1; -; mRNA. DR EMBL; BC029004; AAH29004.1; -; mRNA. DR EMBL; BC016258; AAH16258.1; -; mRNA. DR CCDS; CCDS40599.1; -. DR RefSeq; NP_082165.1; NM_027889.1. DR BioGrid; 214887; 10. DR IntAct; Q91W86; 3. DR STRING; 10090.ENSMUSP00000034644; -. DR iPTMnet; Q91W86; -. DR PhosphoSitePlus; Q91W86; -. DR SwissPalm; Q91W86; -. DR EPD; Q91W86; -. DR MaxQB; Q91W86; -. DR PaxDb; Q91W86; -. DR PeptideAtlas; Q91W86; -. DR PRIDE; Q91W86; -. DR Ensembl; ENSMUST00000034644; ENSMUSP00000034644; ENSMUSG00000032127. DR GeneID; 71732; -. DR KEGG; mmu:71732; -. DR UCSC; uc009pdc.2; mouse. DR CTD; 55823; -. DR MGI; MGI:1918982; Vps11. DR eggNOG; KOG2114; Eukaryota. DR eggNOG; ENOG410XRNZ; LUCA. DR GeneTree; ENSGT00940000153635; -. DR HOGENOM; HOG000216424; -. DR InParanoid; Q91W86; -. DR KO; K20179; -. DR OMA; HDLGTKQ; -. DR OrthoDB; 429638at2759; -. DR TreeFam; TF300479; -. DR ChiTaRS; Vps11; mouse. DR PRO; PR:Q91W86; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; Q91W86; protein. DR Bgee; ENSMUSG00000032127; Expressed in 264 organ(s), highest expression level in dorsal pancreas. DR ExpressionAtlas; Q91W86; baseline and differential. DR Genevisible; Q91W86; MM. DR GO; GO:0005884; C:actin filament; IDA:MGI. DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell. DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0033263; C:CORVET complex; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB. DR GO; GO:0005768; C:endosome; ISO:MGI. DR GO; GO:0030897; C:HOPS complex; ISO:MGI. DR GO; GO:0005770; C:late endosome; ISO:MGI. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; ISO:MGI. DR GO; GO:0048786; C:presynaptic active zone; IDA:SynGO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0030674; F:protein binding, bridging; IBA:GO_Central. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0019905; F:syntaxin binding; ISO:MGI. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0034058; P:endosomal vesicle fusion; ISO:MGI. DR GO; GO:0007032; P:endosome organization; IBA:GO_Central. DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:1903364; P:positive regulation of cellular protein catabolic process; ISO:MGI. DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI. DR GO; GO:1902115; P:regulation of organelle assembly; ISO:MGI. DR GO; GO:0035542; P:regulation of SNARE complex assembly; IBA:GO_Central. DR GO; GO:1901998; P:toxin transport; IMP:MGI. DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central. DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central. DR Gene3D; 1.25.40.10; -; 1. DR Gene3D; 2.130.10.10; -; 1. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR016528; VPS11. DR InterPro; IPR024763; VPS11_C. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR23323:SF24; PTHR23323:SF24; 1. DR Pfam; PF00637; Clathrin; 1. DR Pfam; PF12451; VPS11_C; 1. DR PIRSF; PIRSF007860; VPS11; 1. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF48371; SSF48371; 1. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS50236; CHCR; 2. DR PROSITE; PS50089; ZF_RING_2; 1. PE 1: Evidence at protein level; KW Acetylation; Autophagy; Coiled coil; Cytoplasmic vesicle; Endosome; KW Lysosome; Membrane; Metal-binding; Methylation; Nucleotide-binding; KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport; KW Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q9H270" FT CHAIN 2..941 FT /note="Vacuolar protein sorting-associated protein 11 FT homolog" FT /id="PRO_0000055903" FT REPEAT 411..561 FT /note="CHCR 1" FT REPEAT 572..736 FT /note="CHCR 2" FT ZN_FING 822..861 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT COILED 772..813 FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:Q9H270" FT MOD_RES 813 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H270" FT MOD_RES 904 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000244|PubMed:24129315" FT MOD_RES 924 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H270" FT CONFLICT 1 FT /note="M -> HAS (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 28 FT /note="A -> T (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 34 FT /note="V -> T (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 37..38 FT /note="SA -> PT (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="F -> L (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 186 FT /note="N -> S (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="V -> A (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="G -> V (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="I -> V (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="T -> I (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 583..584 FT /note="AL -> FP (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" FT CONFLICT 589 FT /note="S -> N (in Ref. 2; AAH16258)" FT /evidence="ECO:0000305" SQ SEQUENCE 941 AA; 107719 MW; DB96F07E92C9E534 CRC64; MAAYLQWRRF VFFEKELVKE PLGNDGAAPG AAPVSGSAAS KFLCLPPGIT VCDSGRGSLV FGDMEGQIWF LPRSLQLTGF QAYKLRVTHL YQLKQHNILA SVGEDEEGIN PLVKIWNLEK RDGGNPLCTR IFPAIPGTEP TVVSCLTVHE NLNFMAIGFT DGSVTLNKGD ITRDRHSKTQ ILHKGNYPVT GLAFRQAGKT THLFVVTTEN VQSYIVSGKD YPRVELDTHG CGLRCSALSD PSQDLQFIVA GDECVYLYQP DERGPCFAFE GHKLIVHWFR GYLVIVSRDR KVSPKSEFTS RDSQNSDKQI LNIYDLCNKF IAYSAGFEDI VDVLAEWGSL YVLTRDGRVH ALQEKDTQTK LEMLFKKNLF EMAINLAKSQ HLDSDGLAQI FMQYGDHLYS KGNHDGAVQQ YIRTIGKLEP SYVIRKFLDA QRIHNLTAYL QTLHRQSLAN ADHTTLLLNC YTKLKDSSKL EEFIKTKSES EVHFDVETAI KVLRQAGYYS HALYLAENHA HHEWYLKIQL EDIKNYQEAL RYIGKLPFEQ AESNMKRYGK TLMHHIPEQT TQLLKGLCTD YRPSLEGRGD REALSCRASS EEFIPIFANN PRELKAFLEH MSEVQPDSPQ GIYDTLLELR LQNWAHEKDP QAKEKLHAEA ISLLKSGRFC DVFDKALVLC QMHDFQDGVL YLYEQGKLFQ QIMHYHMQHE QYRQVIAVCE RHGEQEPSLW EQALSYFARK EEDCKEYVAA VLRHIENKSL MPPLLVVQTL AHNSTATLSI IRDYLVQKLQ KQSQQIAQDE LRVRRYREET TRIRQEIQEL KASPKIFQKT KCSICNSALE LPSVHFLCGH SFHQHCFESY SESDADCPTC LPENRKVMDM IRAQEQKRDL HDQFQHQLKC SNDSFSVIAD YFGRGVFNKL TLLTDPPTAR LTPSLEAGLQ RDLLMHSRRG T //