VPS4_DICDI
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 03-AUG-2022, entry version 126.
DE RecName: Full=Vacuolar protein sorting-associated protein 4;
DE EC=3.6.4.6;
GN Name=vps4; ORFNames=DDB_G0284347;
OS Dictyostelium discoideum (Slime mold).
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.DDB0234037; -.
DR PaxDb; Q54PT2; -.
DR PRIDE; Q54PT2; -.
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; MFELNVG; -.
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: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: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 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..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
