VPS4_SCHPO
ID VPS4_SCHPO Reviewed; 432 AA.
AC Q09803;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Suppressor protein of bem1/bed5 double mutants;
DE EC=3.6.4.6;
GN Name=vps4; ORFNames=SPAC2G11.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Valencik M.L., Pringle J.R.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28242692; DOI=10.1073/pnas.1613916114;
RA Gu M., LaJoie D., Chen O.S., von Appen A., Ladinsky M.S., Redd M.J.,
RA Nikolova L., Bjorkman P.J., Sundquist W.I., Ullman K.S., Frost A.;
RT "LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission
RT yeast and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2166-E2175(2017).
CC -!- FUNCTION: Involved in the transport of biosynthetic membrane proteins
CC from the prevacuolar/endosomal compartment to the vacuole. Involved in
CC multivesicular body (MVB) protein sorting. Catalyzes the ATP-dependent
CC dissociation of class E VPS proteins from endosomal membranes, such as
CC the disassembly of the ESCRT-III complex (By similarity). Plays a role
CC in regulating nuclear envelope (NE) morphology and nuclear integrity,
CC particularly during spindle pole body (SPB) extrusion or insertion
CC through the NE, and perhaps during karyokinesis (PubMed:28242692).
CC {ECO:0000250|UniProtKB:P52917, ECO:0000269|PubMed:28242692}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Slow growth rates of spores and severe nuclear
CC envelope (NE) morphology defects (PubMed:28242692). Asymmetric and even
CC failed karyokinesis (PubMed:28242692). Overgrowth of nuclear membranes,
CC so-called karmellae, in cells with daughter spindle pole bodies (SPBs)
CC that often fail to separate normally or display extensive delays in
CC separation (PubMed:28242692). Large fenestrations through both the
CC inner and outer nuclear membranes and abnormal nuclear integrity, i.e.
CC leaking nuclei (PubMed:28242692). Extensive whorls of disorganized
CC tubulo-vesicular membranes that are topologically continuous with the
CC adjacent karmellae (PubMed:28242692). Decreased number of nuclear pore
CC complexes (NPCs) (PubMed:28242692). Simultaneous knockout of cmp7 or
CC lem2 suppresses the slow growth rates of spores and severe nuclear
CC envelope (NE) morphology defects (PubMed:28242692).
CC {ECO:0000269|PubMed:28242692}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; L33456; AAA35347.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91171.1; -; Genomic_DNA.
DR PIR; T38572; S62461.
DR RefSeq; NP_593086.1; NM_001018484.2.
DR AlphaFoldDB; Q09803; -.
DR SMR; Q09803; -.
DR BioGRID; 278533; 6.
DR STRING; 4896.SPAC2G11.06.1; -.
DR iPTMnet; Q09803; -.
DR SwissPalm; Q09803; -.
DR MaxQB; Q09803; -.
DR PaxDb; Q09803; -.
DR PRIDE; Q09803; -.
DR EnsemblFungi; SPAC2G11.06.1; SPAC2G11.06.1:pep; SPAC2G11.06.
DR GeneID; 2542054; -.
DR KEGG; spo:SPAC2G11.06; -.
DR PomBase; SPAC2G11.06; vps4.
DR VEuPathDB; FungiDB:SPAC2G11.06; -.
DR eggNOG; KOG0739; Eukaryota.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; Q09803; -.
DR OMA; MFELNVG; -.
DR PhylomeDB; Q09803; -.
DR Reactome; R-SPO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-SPO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:Q09803; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:PomBase.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:PomBase.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:PomBase.
DR GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR CDD; cd02678; MIT_VPS4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endosome; Hydrolase; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..432
FT /note="Suppressor protein of bem1/bed5 double mutants"
FT /id="PRO_0000084769"
FT DOMAIN 3..80
FT /note="MIT"
FT REGION 83..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 432 AA; 48402 MW; 65E6948AB9360D1E CRC64;
MSNPDCLSKA ISLVKTAIDN DNAEQYPDAY KYYQSALDYF MMALKYEKNE KSKEIIRSKV
IEYLDRAEKL KVYLQEKNNQ ISSKSRVSNG NVEGSNSPTA NEALDSDAKK LRSALTSAIL
VEKPNVRWDD IAGLENAKEA LKETVLLPIK LPQLFSHGRK PWSGILLYGP PGTGKSYLAK
AVATEAGSTF FSISSSDLVS KWMGESERLV RQLFEMAREQ KPSIIFIDEI DSLCGSRSEG
ESESSRRIKT EFLVQMNGVG KDESGVLVLG ATNIPWTLDS AIRRRFEKRI YIPLPNAHAR
ARMFELNVGK IPSELTSQDF KELAKMTDGY SGSDISIVVR DAIMEPVRRI HTATHFKEVY
DNKSNRTLVT PCSPGDPDAF ESSWLEVNPE DIMEPKLTVR DFYSAVRKVK PTLNAGDIEK
HTQFTKDFGA EG
