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 22-JUL-2015, entry version 120. 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). CC -!- FUNCTION: May play a role in vesicle-mediated protein trafficking CC to lysosomal compartments and in membrane docking/fusion reactions CC of late endosomes/lysosomes. {ECO:0000250}. CC -!- SUBUNIT: Part of a large heterooligomeric complex together with CC VPS16, VPS18 and VPS33A. Interacts with STX7 (By similarity). CC Interacts with ECM29 (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9H9C1:VIPAS39 (xeno); NbExp=3; IntAct=EBI-2527812, EBI-749080; CC -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side CC {ECO:0000250}. Lysosome membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. CC Cytoplasmic vesicle {ECO:0000250}. 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; 229-273, 821-864. DR BioGrid; 214887; 8. DR IntAct; Q91W86; 1. DR STRING; 10090.ENSMUSP00000034644; -. DR PhosphoSite; 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; NOG294563; -. 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: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:0034058; P:endosomal vesicle fusion; ISO:MGI. DR GO; GO:0007032; P:endosome organization; IBA:GO_Central. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central. 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:0035542; P:regulation of SNARE complex assembly; IBA:GO_Central. DR GO; GO:1901998; P:toxin transport; IMP:MGI. DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central. 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; Coiled coil; Complete proteome; Cytoplasmic vesicle; KW Endosome; Lysosome; Membrane; Metal-binding; Nucleotide-binding; KW Protein transport; Reference proteome; Repeat; Transport; Zinc; KW 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 //