VPS4_BOMMO
ID VPS4_BOMMO Reviewed; 438 AA.
AC D0FH76;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Vacuolar protein sorting-associated protein 4 {ECO:0000305};
DE EC=3.6.4.6 {ECO:0000269|PubMed:23053938};
DE AltName: Full=BmVps4 {ECO:0000303|PubMed:23053938, ECO:0000303|PubMed:28973578};
DE AltName: Full=Vacuolar protein sorting 4 {ECO:0000303|PubMed:23053938, ECO:0000303|PubMed:28973578};
GN Name=VPS4 {ECO:0000303|PubMed:23053938, ECO:0000312|EMBL:ACX69978.1};
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091 {ECO:0000312|EMBL:ACX69978.1};
RN [1] {ECO:0000312|EMBL:ACX69978.1}
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, MUTAGENESIS OF LYS-174 AND GLU-229, AND 3D-STRUCTURE MODELING.
RC STRAIN=306 {ECO:0000303|PubMed:23053938};
RC TISSUE=Midgut {ECO:0000303|PubMed:23053938};
RX PubMed=23053938; DOI=10.1007/s11033-012-1911-6;
RA Xia H., Zhang C., Feng F., Yuan Y., Zhou Y., Liu X., Zhu K., Yao Q.,
RA Chen K.;
RT "Molecular cloning, expression and characterization of a novel vacuolar
RT protein sorting 4 gene in silkworm, Bombyx mori.";
RL Mol. Biol. Rep. 39:10339-10346(2012).
RN [2] {ECO:0000312|EnsemblMetazoa:BGIBMGA006243-TA}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T {ECO:0000312|EnsemblMetazoa:BGIBMGA006243-TA};
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [3]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=28973578; DOI=10.1093/jisesa/iex055;
RA Xia H., Shao D., Liu X., Wang Q., Zhou Y., Chen K.;
RT "Identification and Characterization of BmVta1, a Bombyx mori (Lepidoptera:
RT Bombycidae) Homologue for Vta1 That is Up-Regulated in Development.";
RL J. Insect Sci. 17:79-86(2017).
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 {ECO:0000250|UniProtKB:Q9UN37}.
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 Evidence={ECO:0000269|PubMed:23053938};
CC -!- ACTIVITY REGULATION: Activated by Mg(2+), but not by Ca(2+).
CC {ECO:0000269|PubMed:23053938}.
CC -!- SUBUNIT: Oligomerizes. {ECO:0000269|PubMed:23053938}.
CC -!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane
CC {ECO:0000250|UniProtKB:Q8VEJ9}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8VEJ9}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9UN37}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9UN37}. Midbody {ECO:0000250|UniProtKB:Q9UN37}.
CC Cytoplasm {ECO:0000269|PubMed:28973578}. Note=Membrane-associated in
CC the prevacuolar endosomal compartment. Localizes to the midbody of
CC dividing cells. {ECO:0000250|UniProtKB:Q9UN37}.
CC -!- TISSUE SPECIFICITY: Expressed highly in head, silk gland and testis
CC with lower levels in fat body and ganglion. Also expressed in ovary and
CC hemolymph, and weakly in Malpighian tube and midgut.
CC {ECO:0000269|PubMed:28973578}.
CC -!- DEVELOPMENTAL STAGE: Expression is up-regulated during metamorphosis
CC and embryogenesis. Barely expressed in third instar. Expression
CC increases in fourth and fifth instar and is sharply increased in pupa,
CC moth and oosperm. {ECO:0000269|PubMed:28973578}.
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.
CC {ECO:0000255|RuleBase:RU003651}.
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DR EMBL; GQ995504; ACX69978.1; -; mRNA.
DR EMBL; BABH01034002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001161188.1; NM_001167716.1.
DR RefSeq; XP_012545394.1; XM_012689940.1.
DR RefSeq; XP_012545395.1; XM_012689941.1.
DR AlphaFoldDB; D0FH76; -.
DR SMR; D0FH76; -.
DR STRING; 7091.BGIBMGA006243-TA; -.
DR EnsemblMetazoa; BGIBMGA006243-RA; BGIBMGA006243-TA; BGIBMGA006243.
DR GeneID; 100313493; -.
DR KEGG; bmor:100313493; -.
DR CTD; 32777; -.
DR eggNOG; KOG0739; Eukaryota.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; D0FH76; -.
DR OMA; MFELNVG; -.
DR OrthoDB; 787710at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR GO; GO:0002165; P:instar larval or pupal development; IEP:UniProtKB.
DR GO; GO:0007552; P:metamorphosis; IEP:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cytoplasm; Endosome; Hydrolase;
KW Membrane; Nucleotide-binding; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..438
FT /note="Vacuolar protein sorting-associated protein 4"
FT /id="PRO_0000451716"
FT DOMAIN 7..73
FT /note="MIT"
FT /evidence="ECO:0000255"
FT REGION 76..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT MUTAGEN 174
FT /note="K->A: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:23053938"
FT MUTAGEN 229
FT /note="E->Q: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:23053938"
SQ SEQUENCE 438 AA; 48949 MW; 3E7BD351E37458A6 CRC64;
MTSSNTLQKA IDLVTKATEE DKNKNYEEAL RLYEHGVEYF LHAVKYEAQG ERAKESIRAK
CLQYLDRAEK LKEYLKKDQK KKPVKDGESK SDDKKSDSDS DSDDPEKKKL QGKLEGAIVV
EKPHVKWSDV AGLEAAKEAL KEAVILPIKF PHLFTGKRIP WKGILLFGPP GTGKSYLAKA
VATEANNSTF FSVSSSDLVS KWLGESEKLV KNLFDLARQH KPSIIFIDEI DSLCSSRSDN
ESESARRIKT EFLVQMQGVG NDMDGILVLG ATNIPWVLDS AIRRRFEKRI YIALPEEHAR
LDMFKLHLGN TRHQLSEQDM KLLAAKSEGY SGADISIVVR DALMQPVRKV QSATHFKKIS
GPSPTDPNVI VNDLLTPCSP GDPGAIEMTW IDVPSDKLGE PPVTMSDMLR SLAVSKPTVN
DDDMVKLRKF MEDFGQEG
