ID   CHMP3_MOUSE             Reviewed;         224 AA.
AC   Q9CQ10; Q9D2Z2; Q9D7A5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   24-JAN-2024, entry version 149.
DE   RecName: Full=Charged multivesicular body protein 3;
DE   AltName: Full=Chromatin-modifying protein 3;
DE   AltName: Full=Vacuolar protein sorting-associated protein 24;
GN   Name=Chmp3; Synonyms=Vps24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17331679; DOI=10.1016/j.gene.2006.12.039;
RA   Khoury C.M., Yang Z., Ismail S., Greenwood M.T.;
RT   "Characterization of a novel alternatively spliced human transcript
RT   encoding an N-terminally truncated Vps24 protein that suppresses the
RT   effects of Bax in an ESCRT independent manner in yeast.";
RL   Gene 391:233-241(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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}.
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:0000250}. Membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endosome {ECO:0000250}. Late
CC       endosome membrane {ECO:0000250}. Note=Localizes to the midbody of
CC       dividing cells. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in lung, testis, heart, spleen, skeletal
CC       muscle, kidney, liver and brain. {ECO:0000269|PubMed:17331679}.
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; AK009414; BAB26273.1; -; mRNA.
DR   EMBL; AK014818; BAB29566.1; -; mRNA.
DR   EMBL; AK016677; BAB30375.1; -; mRNA.
DR   EMBL; AK018611; BAB31306.1; -; mRNA.
DR   EMBL; AK083562; BAC38951.1; -; mRNA.
DR   EMBL; BC049964; AAH49964.1; -; mRNA.
DR   CCDS; CCDS20232.1; -.
DR   RefSeq; NP_080059.2; NM_025783.3.
DR   AlphaFoldDB; Q9CQ10; -.
DR   SMR; Q9CQ10; -.
DR   BioGRID; 211654; 27.
DR   ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR   ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR   IntAct; Q9CQ10; 22.
DR   MINT; Q9CQ10; -.
DR   STRING; 10090.ENSMUSP00000109815; -.
DR   ChEMBL; CHEMBL4879506; -.
DR   iPTMnet; Q9CQ10; -.
DR   PhosphoSitePlus; Q9CQ10; -.
DR   EPD; Q9CQ10; -.
DR   jPOST; Q9CQ10; -.
DR   MaxQB; Q9CQ10; -.
DR   PaxDb; 10090-ENSMUSP00000109815; -.
DR   PeptideAtlas; Q9CQ10; -.
DR   ProteomicsDB; 281464; -.
DR   Pumba; Q9CQ10; -.
DR   DNASU; 66700; -.
DR   Ensembl; ENSMUST00000059462.12; ENSMUSP00000109815.4; ENSMUSG00000053119.12.
DR   Ensembl; ENSMUST00000065364.5; ENSMUSP00000068410.3; ENSMUSG00000053119.12.
DR   GeneID; 66700; -.
DR   KEGG; mmu:66700; -.
DR   UCSC; uc009cgw.1; mouse.
DR   AGR; MGI:1913950; -.
DR   CTD; 51652; -.
DR   MGI; MGI:1913950; Chmp3.
DR   VEuPathDB; HostDB:ENSMUSG00000053119; -.
DR   eggNOG; KOG3229; Eukaryota.
DR   GeneTree; ENSGT00950000182832; -.
DR   HOGENOM; CLU_069208_0_1_1; -.
DR   InParanoid; Q9CQ10; -.
DR   OMA; INEMMDD; -.
DR   OrthoDB; 8622at2759; -.
DR   PhylomeDB; Q9CQ10; -.
DR   TreeFam; TF105848; -.
DR   Reactome; R-MMU-1632852; Macroautophagy.
DR   Reactome; R-MMU-5620971; Pyroptosis.
DR   Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   BioGRID-ORCS; 66700; 22 hits in 84 CRISPR screens.
DR   ChiTaRS; Chmp3; mouse.
DR   PRO; PR:Q9CQ10; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9CQ10; Protein.
DR   Bgee; ENSMUSG00000053119; Expressed in granulocyte and 258 other cell types or tissues.
DR   ExpressionAtlas; Q9CQ10; baseline and differential.
DR   GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR   GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0000815; C:ESCRT III complex; ISO:MGI.
DR   GO; GO:0000776; C:kinetochore; ISO:MGI.
DR   GO; GO:0005828; C:kinetochore microtubule; ISO:MGI.
DR   GO; GO:0005770; C:late endosome; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0032585; C:multivesicular body membrane; ISO:MGI.
DR   GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0140678; F:molecular function inhibitor activity; ISO:MGI.
DR   GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR   GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISO:MGI.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
DR   GO; GO:0097352; P:autophagosome maturation; ISO:ComplexPortal.
DR   GO; GO:0006914; P:autophagy; ISO:ComplexPortal.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
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:ComplexPortal.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR   GO; GO:0090148; P:membrane fission; NAS:ComplexPortal.
DR   GO; GO:0061952; P:midbody abscission; ISO:ComplexPortal.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISO:ComplexPortal.
DR   GO; GO:0036258; P:multivesicular body assembly; NAS:ComplexPortal.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; ISO:ComplexPortal.
DR   GO; GO:0061763; P:multivesicular body-lysosome fusion; NAS:ComplexPortal.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISO:ComplexPortal.
DR   GO; GO:0006997; P:nucleus organization; ISO:ComplexPortal.
DR   GO; GO:0001778; P:plasma membrane repair; ISO:ComplexPortal.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; ISO:MGI.
DR   GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR   GO; GO:2000641; P:regulation of early endosome to late endosome transport; IEA:Ensembl.
DR   GO; GO:0051036; P:regulation of endosome size; ISO:MGI.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:ComplexPortal.
DR   GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:ComplexPortal.
DR   GO; GO:0051469; P:vesicle fusion with vacuole; NAS:ComplexPortal.
DR   GO; GO:0046761; P:viral budding from plasma membrane; ISO:ComplexPortal.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:ComplexPortal.
DR   Gene3D; 6.10.140.1230; -; 1.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR10476; CHARGED MULTIVESICULAR BODY PROTEIN; 1.
DR   PANTHER; PTHR10476:SF1; CHARGED MULTIVESICULAR BODY PROTEIN 3; 1.
DR   Pfam; PF03357; Snf7; 1.
DR   Genevisible; Q9CQ10; MM.
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..224
FT                   /note="Charged multivesicular body protein 3"
FT                   /id="PRO_0000211481"
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..224
FT                   /note="Interaction with VPS4A"
FT                   /evidence="ECO:0000250"
FT   REGION          151..222
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..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..224
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          205..209
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          223..224
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   COILED          22..54
FT                   /evidence="ECO:0000255"
FT   COILED          149..224
FT                   /evidence="ECO:0000255"
FT   MOTIF           201..213
FT                   /note="MIT-interacting motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        199..213
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            48
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   SITE            218
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15345747"
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   CONFLICT        7
FT                   /note="T -> S (in Ref. 1; BAB26273)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="A -> V (in Ref. 1; BAB31306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="F -> L (in Ref. 1; BAB31306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   224 AA;  25219 MW;  DC1A566E86D82A07 CRC64;
     MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKEVC
     VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI
     PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEA AEMEIDRILF EITAGALGKA
     PSKVTDALPE PEPAGAMAAS EEGEEEEDEE DLEAMQSRLA TLRS
//