VPS4B_PONAB
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 03-AUG-2022, entry version 89.
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; 787710at2759; -.
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:0006996; P:organelle organization; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR031255; VPS4.
DR InterPro; IPR015415; Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR PANTHER; PTHR23074:SF72; PTHR23074:SF72; 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; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 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
