ID   VPS4B_PONAB             Reviewed;         444 AA.
AC   Q5R658;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   28-JUN-2023, entry version 93.
DE   RecName: Full=Vacuolar protein sorting-associated protein 4B;
DE            EC=3.6.4.6;
GN   Name=VPS4B;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in late steps of the endosomal multivesicular bodies
CC       (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and
CC       catalyzes their disassembly, possibly in combination with membrane
CC       fission. Redistributes the ESCRT-III components to the cytoplasm for
CC       further rounds of MVB sorting. MVBs contain intraluminal vesicles
CC       (ILVs) that are generated by invagination and scission from the
CC       limiting membrane of the endosome and mostly are delivered to lysosomes
CC       enabling degradation of membrane proteins, such as stimulated growth
CC       factor receptors, lysosomal enzymes and lipids. VPS4A/B are required
CC       for the exosomal release of SDCBP, CD63 and syndecan (By similarity).
CC       {ECO:0000250|UniProtKB:O75351}.
CC   -!- FUNCTION: (Microbial infection) In conjunction with the ESCRT machinery
CC       also appears to function in topologically equivalent membrane fission
CC       events, such as the terminal stages of cytokinesis and enveloped virus
CC       budding (lentiviruses). {ECO:0000250|UniProtKB:O75351}.
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   -!- SUBUNIT: Proposed to be monomeric or homodimeric in nucleotide-free
CC       form and to oligomerize upon binding to ATP to form two stacked
CC       hexameric or heptameric rings with a central pore through which ESCRT-
CC       III substrates are translocated in an ATP-dependent manner. In vitro,
CC       associates on the inside of a helical tubular structure formed by a
CC       CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B and
CC       CHMP6. Interacts with VPS4A; the interaction suggests a heteromeric
CC       assembly with VPS4A. Interacts with VTA1 (By similarity).
CC       {ECO:0000250|UniProtKB:O75351}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane
CC       {ECO:0000250|UniProtKB:P46467}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P46467}. Note=Membrane-associated in the
CC       prevacuolar endosomal compartment. {ECO:0000250|UniProtKB:P46467}.
CC   -!- DOMAIN: The MIT domain serves as an adapter for ESCRT-III proteins. It
CC       forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT
CC       interacting motif) helices along the groove between MIT helices 2 and 3
CC       present in a subset of ESCRT-III proteins thus establishing the
CC       canonical MIM-MIT interaction. In an extended conformation along the
CC       groove between helices 1 and 3, also binds to a type-2 MIT interacting
CC       motif (MIM2). {ECO:0000250|UniProtKB:O75351}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; CR860638; CAH92758.1; -; mRNA.
DR   RefSeq; NP_001126608.1; NM_001133136.1.
DR   AlphaFoldDB; Q5R658; -.
DR   SMR; Q5R658; -.
DR   STRING; 9601.ENSPPYP00000010341; -.
DR   GeneID; 100173605; -.
DR   KEGG; pon:100173605; -.
DR   CTD; 9525; -.
DR   eggNOG; KOG0739; Eukaryota.
DR   InParanoid; Q5R658; -.
DR   OrthoDB; 276256at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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:SF72; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 4B; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Coiled coil; Endosome; Hydrolase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..444
FT                   /note="Vacuolar protein sorting-associated protein 4B"
FT                   /id="PRO_0000331379"
FT   DOMAIN          4..82
FT                   /note="MIT"
FT   REGION          78..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          19..82
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        78..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         174..181
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75351"
FT   MOD_RES         102
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75351"
FT   MOD_RES         108
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75351"
FT   MOD_RES         410
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O75351"
SQ   SEQUENCE   444 AA;  49330 MW;  B6549F4E19C210F4 CRC64;
     MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA
     QCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN DSDGEGESDD PEKKKLQNQL
     QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK
     SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC
     GSRSENESEA ARRIKTEFLV QMRGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL
     PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM QPVRKVQSAT
     HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVS MSDMLRSLSN
     TKPTVNEHDL LKLKKFTEDF GQEG
//