CHMP3_RAT
ID CHMP3_RAT Reviewed; 223 AA.
AC Q8CGS4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Charged multivesicular body protein 3;
DE AltName: Full=Chromatin-modifying protein 3;
DE AltName: Full=Vacuolar protein sorting-associated protein 24;
DE Short=rVps24p;
GN Name=Chmp3; Synonyms=Vps24;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF LYS-49.
RC STRAIN=Wistar;
RX PubMed=12878588; DOI=10.1074/jbc.m306864200;
RA Whitley P., Reaves B.J., Hashimoto M., Riley A.M., Potter B.V.L.,
RA Holman G.D.;
RT "Identification of mammalian Vps24p as an effector of phosphatidylinositol
RT 3,5-bisphosphate-dependent endosome compartmentalization.";
RL J. Biol. Chem. 278:38786-38795(2003).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Probable core component of the endosomal sorting required for
CC transport complex III (ESCRT-III) which is involved in multivesicular
CC bodies (MVBs) formation and sorting of endosomal cargo proteins into
CC MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by
CC invagination and scission from the limiting membrane of the endosome
CC and mostly are delivered to lysosomes enabling degradation of membrane
CC proteins, such as stimulated growth factor receptors, lysosomal enzymes
CC and lipids. The MVB pathway appears to require the sequential function
CC of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC dissociate from the invaginating membrane before the ILV is released.
CC The ESCRT machinery also functions in topologically equivalent membrane
CC fission events, such as the terminal stages of cytokinesis. ESCRT-III
CC proteins are believed to mediate the necessary vesicle extrusion and/or
CC membrane fission activities, possibly in conjunction with the AAA
CC ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate
CC PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other
CC phosphoinositides tested. Involved in late stages of cytokinesis. Plays
CC a role in endosomal sorting/trafficking of EGF receptor (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:12878588}.
CC -!- SUBUNIT: Probable core component of the endosomal sorting required for
CC transport complex III (ESCRT-III). ESCRT-III components are thought to
CC multimerize to form a flat lattice on the perimeter membrane of the
CC endosome. Several assembly forms of ESCRT-III may exist that interact
CC and act sequentially. Forms a metastable monomer in solution; its core
CC structure (without part of the putative autoinhibitory C-terminal
CC acidic region) oligomerizes into a flat lattice via two different
CC dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not
CC CHMP4) to form helical tubular structures that expose membrane-
CC interacting sites on the outside whereas VPS4B can associate on the
CC inside of the tubule. May interact with IGFBP7; the relevance of such
CC interaction however remains unclear. Interacts with CHMP2A. Interacts
CC with CHMP4A; the interaction requires the release of CHMP4A
CC autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the
CC interaction appears to relieve the autoinhibition of CHMP3 (By
CC similarity). Interacts with VTA1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12878588}.
CC Membrane {ECO:0000269|PubMed:12878588}; Lipid-anchor
CC {ECO:0000269|PubMed:12878588}. Endosome {ECO:0000269|PubMed:12878588}.
CC Late endosome membrane {ECO:0000250}. Note=Localizes to the midbody of
CC dividing cells. {ECO:0000250}.
CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus are thought to
CC render the protein in a closed, soluble and inactive conformation
CC through an autoinhibitory intramolecular interaction. The open and
CC active conformation, which enables membrane binding and
CC oligomerization, is achieved by interaction with other cellular binding
CC partners, probably including other ESCRT components.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AY150169; AAN74982.1; -; mRNA.
DR RefSeq; NP_758834.1; NM_172331.1.
DR AlphaFoldDB; Q8CGS4; -.
DR SMR; Q8CGS4; -.
DR STRING; 10116.ENSRNOP00000010253; -.
DR iPTMnet; Q8CGS4; -.
DR PhosphoSitePlus; Q8CGS4; -.
DR jPOST; Q8CGS4; -.
DR PaxDb; Q8CGS4; -.
DR PRIDE; Q8CGS4; -.
DR Ensembl; ENSRNOT00000010253; ENSRNOP00000010253; ENSRNOG00000007356.
DR GeneID; 282834; -.
DR KEGG; rno:282834; -.
DR UCSC; RGD:708556; rat.
DR CTD; 51652; -.
DR RGD; 708556; Chmp3.
DR eggNOG; KOG3229; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_069208_0_1_1; -.
DR InParanoid; Q8CGS4; -.
DR OMA; INEMMDD; -.
DR OrthoDB; 1418709at2759; -.
DR PhylomeDB; Q8CGS4; -.
DR TreeFam; TF105848; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR Reactome; R-RNO-5620971; Pyroptosis.
DR Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-RNO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:Q8CGS4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000007356; Expressed in lung and 19 other tissues.
DR GO; GO:1904930; C:amphisome membrane; ISO:RGD.
DR GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0000815; C:ESCRT III complex; ISO:RGD.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0005828; C:kinetochore microtubule; ISO:RGD.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR GO; GO:0030496; C:midbody; IDA:RGD.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; ISO:RGD.
DR GO; GO:0005643; C:nuclear pore; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:RGD.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:RGD.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR GO; GO:0006914; P:autophagy; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:RGD.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:1902774; P:late endosome to lysosome transport; ISO:RGD.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0061952; P:midbody abscission; ISO:RGD.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:RGD.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR GO; GO:0031468; P:nuclear membrane reassembly; ISO:RGD.
DR GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR GO; GO:0001778; P:plasma membrane repair; ISO:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:RGD.
DR GO; GO:0051258; P:protein polymerization; ISO:RGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:RGD.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0051036; P:regulation of endosome size; IMP:RGD.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:RGD.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:RGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:RGD.
DR GO; GO:0046761; P:viral budding from plasma membrane; ISO:RGD.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:RGD.
DR GO; GO:0019076; P:viral release from host cell; ISO:RGD.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome;
KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..223
FT /note="Charged multivesicular body protein 3"
FT /id="PRO_0000211483"
FT REGION 2..113
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 59..64
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT REGION 151..223
FT /note="Interaction with VPS4A"
FT /evidence="ECO:0000250"
FT REGION 151..221
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 168..169
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT REGION 180..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..223
FT /note="Interaction with STAMBP"
FT /evidence="ECO:0000250"
FT REGION 204..208
FT /note="Interaction with STAMBP"
FT REGION 222..223
FT /note="Interaction with STAMBP"
FT COILED 22..54
FT /evidence="ECO:0000255"
FT COILED 149..223
FT /evidence="ECO:0000255"
FT MOTIF 201..212
FT /note="MIT-interacting motif"
FT /evidence="ECO:0000250"
FT SITE 48
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT SITE 217
FT /note="Interaction with STAMBP"
FT /evidence="ECO:0000250"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT CROSSLNK 179
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y3E7"
FT MUTAGEN 49
FT /note="K->D: Strongly reduces binding to PtdIns(3,5)P2."
FT /evidence="ECO:0000269|PubMed:12878588"
SQ SEQUENCE 223 AA; 25062 MW; 203CCA75C78E4586 CRC64;
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKEVC
VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI
PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEA AEMEIDRILF EITAGALGKA
PSKVTDALPE PEPAGAMAAS EGDEEDDEED LEAMQSRLAT LRS
