VPS11_MOUSE
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 03-AUG-2022, entry version 168.
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). Interacts with PLEKHM1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H270, ECO:0000269|PubMed:21411634,
CC ECO:0000269|PubMed:25266290, ECO:0000305|PubMed:25266290}.
CC -!- INTERACTION:
CC Q91W86; 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}.
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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 AlphaFoldDB; Q91W86; -.
DR SMR; Q91W86; -.
DR BioGRID; 214887; 15.
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 ProteomicsDB; 297581; -.
DR Antibodypedia; 32587; 227 antibodies from 33 providers.
DR DNASU; 71732; -.
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 VEuPathDB; HostDB:ENSMUSG00000032127; -.
DR eggNOG; KOG2114; Eukaryota.
DR GeneTree; ENSGT00940000153635; -.
DR HOGENOM; CLU_001287_0_1_1; -.
DR InParanoid; Q91W86; -.
DR OMA; MRPQSTM; -.
DR OrthoDB; 429638at2759; -.
DR PhylomeDB; Q91W86; -.
DR TreeFam; TF300479; -.
DR BioGRID-ORCS; 71732; 30 hits in 77 CRISPR screens.
DR ChiTaRS; Vps11; mouse.
DR PRO; PR:Q91W86; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q91W86; protein.
DR Bgee; ENSMUSG00000032127; Expressed in interventricular septum and 243 other tissues.
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:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; 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:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISO:MGI.
DR GO; GO:0048284; P:organelle fusion; IBA:GO_Central.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:1902115; P:regulation of organelle assembly; ISO:MGI.
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:0007744|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
