ID   VPS4_DICDI              Reviewed;         444 AA.
AC   Q54PT2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Vacuolar protein sorting-associated protein 4;
DE            EC=3.6.4.6;
GN   Name=vps4; ORFNames=DDB_G0284347;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Involved in intracellular protein transport probably out of a
CC       prevacuolar endosomal compartment. May be involved in the release of
CC       components of the bilayered coat from the endosomal membrane. The
CC       association with ESCRT-III complex mediates the ATP-dependent
CC       disassembly of the ESCRT-III complex (By similarity). {ECO:0000250}.
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: Prevacuolar compartment membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}. Endosome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The MIT domain may serve as an adapter for the ESCRT-III
CC       complex. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AAFI02000064; EAL65222.1; -; Genomic_DNA.
DR   RefSeq; XP_638572.1; XM_633480.1.
DR   AlphaFoldDB; Q54PT2; -.
DR   SMR; Q54PT2; -.
DR   STRING; 44689.Q54PT2; -.
DR   PaxDb; 44689-DDB0234037; -.
DR   ABCD; Q54PT2; 5 sequenced antibodies.
DR   EnsemblProtists; EAL65222; EAL65222; DDB_G0284347.
DR   GeneID; 8624544; -.
DR   KEGG; ddi:DDB_G0284347; -.
DR   dictyBase; DDB_G0284347; vps4.
DR   eggNOG; KOG0739; Eukaryota.
DR   HOGENOM; CLU_000688_21_2_1; -.
DR   InParanoid; Q54PT2; -.
DR   OMA; IEWTNEF; -.
DR   PhylomeDB; Q54PT2; -.
DR   Reactome; R-DDI-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-DDI-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   PRO; PR:Q54PT2; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0036019; C:endolysosome; IDA:dictyBase.
DR   GO; GO:0005768; C:endosome; ISS:dictyBase.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140220; C:pathogen-containing vacuole; IDA:dictyBase.
DR   GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0016197; P:endosomal transport; ISS:dictyBase.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; HEP:dictyBase.
DR   GO; GO:0009611; P:response to wounding; IDA:dictyBase.
DR   GO; GO:0007033; P:vacuole organization; IBA:GO_Central.
DR   CDD; cd02678; MIT_VPS4; 1.
DR   CDD; cd19521; RecA-like_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..444
FT                   /note="Vacuolar protein sorting-associated protein 4"
FT                   /id="PRO_0000331380"
FT   DOMAIN          2..80
FT                   /note="MIT"
FT   REGION          79..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..98
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   444 AA;  49605 MW;  764EAB9A43A34284 CRC64;
     MGDVNFLQKA IQIVQQATEQ DNAKNYAEAH RLYIQSLEWF TTALKYEKSE RSKATIKAKT
     LEYLQRAEQL KEYLDKSKNK KPVAVGGNKS NSAGSANGAG KSAKEDDEDM DPEDKKRNDS
     LSSSIVTTKP NVKWDDVAGL YQAKEYLKEA VIFPIKFPQM FTGNRKPWKG ILLYGPPGTG
     KSYLAKAVAT EISSTFFSIS PSDIVTKWLG DSEKLVKQLF EMAREKNNSV IFIDEVDSLC
     SSRNDQESES ARRIKTEFLI QMNGVGNDSD GILVLAATNI PWGLDLAIRR RFEKRIYIGL
     PEPQARAKMF QIHIGSTPNT LVQADYKKLA DLTEGYSGSD IGSLVKDAIM QPVRAVQCAT
     HFKQIRAPSR EDPSVMTDYV TPCSPGDPLA QEMTWMDIDP TKLKEPEITI ADCLKSLRVI
     KPSVNKADLD RYVEFTNDFG QDGV
//