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 16-MAR-2016, entry version 126. DE RecName: Full=Vacuolar protein sorting-associated protein 11 homolog; GN Name=Vps11; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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 RT project: 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 RT 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 RT of class C Vps/HOPS tether subunits in polarized and nonpolarized RT cells."; RL Mol. Biol. Cell 22:1699-1715(2011). RN [5] 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 RT early 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 CC and autophagic pathways. Believed to act as a core component of CC the putative HOPS and CORVET endosomal tethering complexes which CC are proposed to be involved in the Rab5-to-Rab7 endosome CC conversion probably implicating MON1A/B, and via binding SNAREs CC and SNARE complexes to mediate tethering and docking events during CC SNARE-mediated membrane fusion. The HOPS complex is proposed to be CC recruited to Rab7 on the late endosomal membrane and to regulate CC late endocytic, phagocytic and autophagic traffic towards CC lysosomes. The CORVET complex is proposed to function as a Rab5 CC effector to mediate early endosome fusion probably in specific CC endosome subpopulations. Required for fusion of endosomes and CC autophagosomes with lysosomes. Involved in cargo transport from CC early to late endosomes and required for the transition from early CC to late endosomes (By similarity). {ECO:0000250|UniProtKB:Q9H270}. CC -!- SUBUNIT: Core component of at least two putative endosomal CC tethering complexes, the homotypic fusion and vacuole protein CC sorting (HOPS) complex and the class C core vacuaole/endosome CC tethering (CORVET) complex. Their common core is composed of the CC class C Vps proteins VPS11, VPS16, VPS18 and VPS33A, which in HOPS CC further associates with VPS39 and VPS41 and in CORVET with VPS8 CC and TGFBRAP1 (PubMed:25266290). Interacts with RAB5C CC (PubMed:25266290). Interacts with TGFBRAP1, MON1B, STX7, STX17, CC ECM29, EZR, RDX, MSN (By similarity). Associates with adaptor CC 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 CC membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side CC {ECO:0000305}. Cytoplasmic vesicle {ECO:0000305}. Early endosome CC {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. CC Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}. CC -!- SIMILARITY: Belongs to the VPS11 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CHCR (clathrin heavy-chain) repeats. CC {ECO:0000255|PROSITE-ProRule:PRU01006}. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00175}. 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 UniGene; Mm.295013; -. DR ProteinModelPortal; Q91W86; -. DR SMR; Q91W86; 140-218, 820-864. DR BioGrid; 214887; 8. DR IntAct; Q91W86; 3. DR STRING; 10090.ENSMUSP00000034644; -. DR iPTMnet; Q91W86; -. DR PhosphoSite; Q91W86; -. DR EPD; Q91W86; -. DR MaxQB; Q91W86; -. DR PaxDb; 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; ENSGT00390000015058; -. DR HOGENOM; HOG000216424; -. DR HOVERGEN; HBG055822; -. DR InParanoid; Q91W86; -. DR OMA; QHSILVS; -. DR OrthoDB; EOG7J9VNV; -. DR TreeFam; TF300479; -. DR NextBio; 334355; -. DR PRO; PR:Q91W86; -. DR Proteomes; UP000000589; Chromosome 9. DR Bgee; Q91W86; -. DR CleanEx; MM_VPS11; -. 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; ISO:MGI. DR GO; GO:0005764; C:lysosome; ISO:MGI. 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:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0034058; P:endosomal vesicle fusion; ISO:MGI. 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:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI. DR GO; GO:1902115; P:regulation of organelle assembly; ISO:MGI. DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI. DR GO; GO:1901998; P:toxin transport; IMP:MGI. 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; IPR016528; VPS11. DR InterPro; IPR024763; VPS11_C. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom. DR InterPro; IPR017986; WD40_repeat_dom. 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 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; Complete proteome; KW Cytoplasmic vesicle; Endosome; Lysosome; Membrane; Metal-binding; KW Nucleotide-binding; Protein transport; Reference proteome; Repeat; KW Transport; Zinc; Zinc-finger. FT INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q9H270}. FT CHAIN 2 941 Vacuolar protein sorting-associated FT protein 11 homolog. FT /FTId=PRO_0000055903. FT REPEAT 411 561 CHCR 1. FT REPEAT 572 736 CHCR 2. FT ZN_FING 822 861 RING-type. {ECO:0000255|PROSITE- FT ProRule:PRU00175}. FT COILED 772 813 {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000250|UniProtKB:Q9H270}. FT CONFLICT 1 1 M -> HAS (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 28 28 A -> T (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 34 34 V -> T (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 37 38 SA -> PT (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 132 132 F -> L (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 186 186 N -> S (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 276 276 V -> A (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 326 326 G -> V (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 330 330 I -> V (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 551 551 T -> I (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 583 584 AL -> FP (in Ref. 2; AAH16258). FT {ECO:0000305}. FT CONFLICT 589 589 S -> N (in Ref. 2; AAH16258). FT {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 //