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   27-MAR-2024, entry version 158.
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; 7.
DR   STRING; 284812.Q09803; -.
DR   iPTMnet; Q09803; -.
DR   SwissPalm; Q09803; -.
DR   MaxQB; Q09803; -.
DR   PaxDb; 4896-SPAC2G11-06-1; -.
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; IEWTNEF; -.
DR   PhylomeDB; Q09803; -.
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:0007084; P:mitotic nuclear membrane reassembly; 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; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 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; Spast_Vps4_C.
DR   InterPro; IPR045253; VPS4_MIT.
DR   PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR23074:SF83; VESICLE-FUSING ATPASE; 1.
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; MIT domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//