VPS4B_BOVIN
ID VPS4B_BOVIN Reviewed; 444 AA.
AC Q0VD48;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Vacuolar protein sorting-associated protein 4B;
DE EC=3.6.4.6;
GN Name=VPS4B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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. Involved in
CC cytokinesis. VPS4A/B are required for the exosomal release of SDCBP,
CC CD63 and syndecan (By similarity). {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. Interacts
CC with CHMP1A, CHMP1B, CHMP2A, CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and
CC CHMP6. Interacts with VPS4B; the interaction suggests a heteromeric
CC assembly with VPS4B. Interacts with SPAST. Interacts with IST1 (By
CC similarity). 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) (By similarity). {ECO:0000250|UniProtKB:O75351}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC119836; AAI19837.1; -; mRNA.
DR RefSeq; NP_001069624.1; NM_001076156.1.
DR AlphaFoldDB; Q0VD48; -.
DR SMR; Q0VD48; -.
DR STRING; 9913.ENSBTAP00000013862; -.
DR PaxDb; Q0VD48; -.
DR PRIDE; Q0VD48; -.
DR Ensembl; ENSBTAT00000013862; ENSBTAP00000013862; ENSBTAG00000010492.
DR Ensembl; ENSBTAT00000081581; ENSBTAP00000065188; ENSBTAG00000010492.
DR GeneID; 539357; -.
DR KEGG; bta:539357; -.
DR CTD; 9525; -.
DR VEuPathDB; HostDB:ENSBTAG00000010492; -.
DR VGNC; VGNC:36825; VPS4B.
DR eggNOG; KOG0739; Eukaryota.
DR GeneTree; ENSGT00940000154973; -.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; Q0VD48; -.
DR OMA; AVQYFIH; -.
DR OrthoDB; 787710at2759; -.
DR TreeFam; TF105012; -.
DR Proteomes; UP000009136; Chromosome 24.
DR Bgee; ENSBTAG00000010492; Expressed in neutrophil and 105 other tissues.
DR ExpressionAtlas; Q0VD48; baseline and differential.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0090543; C:Flemming body; IEA:Ensembl.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0000922; C:spindle pole; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:1904903; P:ESCRT III complex disassembly; IEA:Ensembl.
DR GO; GO:0061738; P:late endosomal microautophagy; IEA:Ensembl.
DR GO; GO:0061952; P:midbody abscission; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR GO; GO:0036258; P:multivesicular body assembly; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; IEA:Ensembl.
DR GO; GO:0006997; P:nucleus organization; IEA:Ensembl.
DR GO; GO:1903724; P:positive regulation of centriole elongation; IEA:Ensembl.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
DR GO; GO:0051261; P:protein depolymerization; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0033993; P:response to lipid; IEA:Ensembl.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:Ensembl.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:Ensembl.
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_0000331378"
FT DOMAIN 4..82
FT /note="MIT"
FT REGION 77..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..82
FT /evidence="ECO:0000255"
FT COMPBIAS 77..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 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75351"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75351"
SQ SEQUENCE 444 AA; 49264 MW; 7C9D31E0BE4C1861 CRC64;
MASTPTNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA
KCTEYLDRAE KLKEYLKKRE KKPQKPVKEG QPAPADEKGN DSDGEGESDD PEKKKLQNQL
QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK
SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC
GSRSENESEA ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL
PEAHARAAMF KLHLGTTQNS LTEADFRDLG KKTEGYSGAD ISIIVRDALM QPVRKVQSAT
HFKKVRGPSR ADPNNIVDDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVC MSDMLRSLSS
TKPTVNEHDL LKLKKFTEDF GQEG
