ID VPS11_MOUSE Reviewed; 941 AA. AC Q91W86; Q9DBX8; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 19-SEP-2002, sequence version 2. DT 31-OCT-2006, entry version 40. DE Vacuolar protein sorting-associated protein 11. 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. 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=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 (By similarity). CC -!- SUBUNIT: Large hetero-oligomeric complex together with VPS16, CC VPS18 and VPS33A. Interacts with STX7 (By similarity). CC -!- SUBCELLULAR LOCATION: Endosome; late endosome; late endosomal CC membrane; peripheral membrane protein (By similarity). Lysosome; CC lysosomal membrane; peripheral membrane protein (By similarity). CC Cytoplasmic, peripheral membrane protein associated with late CC endosomes/lysosomes (By similarity). CC -!- SIMILARITY: Contains 1 clathrin repeat. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. 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; BC016258; AAH16258.1; ALT_INIT; mRNA. DR Ensembl; ENSMUSG00000032127; Mus musculus. DR KEGG; mmu:71732; -. DR MGI; MGI:1918982; Vps11. DR ArrayExpress; Q91W86; -. DR GO; GO:0005884; C:actin filament; IDA:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:MGI. DR InterPro; IPR011990; TPR-like_helical. DR InterPro; IPR011046; WD40_like. DR InterPro; IPR001841; Znf_RING. DR Pfam; PF00097; zf-C3HC4; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG. DR PROSITE; PS50089; ZF_RING_2; 1. KW ATP-binding; Coiled coil; Membrane; Metal-binding; Nucleotide-binding; KW Protein transport; Transport; Zinc; Zinc-finger. FT CHAIN 1 941 Vacuolar protein sorting-associated FT protein 11. FT /FTId=PRO_0000055903. FT REPEAT 413 537 Clathrin. FT NP_BIND 193 200 ATP (Potential). FT ZN_FING 822 861 RING-type. FT COILED 772 813 Potential. FT CONFLICT 1 1 M -> S (in Ref. 2). FT CONFLICT 28 28 A -> T (in Ref. 2). FT CONFLICT 34 34 V -> T (in Ref. 2). FT CONFLICT 37 38 SA -> PT (in Ref. 2). FT CONFLICT 132 132 F -> L (in Ref. 2). FT CONFLICT 186 186 N -> S (in Ref. 2). FT CONFLICT 276 276 V -> A (in Ref. 2). FT CONFLICT 326 326 V -> G (in Ref. 1). FT CONFLICT 330 330 V -> I (in Ref. 1). FT CONFLICT 551 551 I -> T (in Ref. 1). FT CONFLICT 583 583 A -> F (in Ref. 2). FT CONFLICT 584 584 P -> L (in Ref. 1). FT CONFLICT 589 589 N -> S (in Ref. 1). SQ SEQUENCE 941 AA; 107770 MW; C41780A111C9881C 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 IAYSAVFEDV VDVLAEWGSL YVLTRDGRVH ALQEKDTQTK LEMLFKKNLF EMAINLAKSQ HLDSDGLAQI FMQYGDHLYS KGNHDGAVQQ YIRTIGKLEP SYVIRKFLDA QRIHNLTAYL QTLHRQSLAN ADHTTLLLNC YTKLKDSSKL EEFIKTKSES EVHFDVETAI KVLRQAGYYS HALYLAENHA HHEWYLKIQL EDIKNYQEAL RYIGKLPFEQ AESNMKRYGK ILMHHIPEQT TQLLKGLCTD YRPSLEGRGD REAPSCRANS 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 //