CHM4C_MOUSE
ID CHM4C_MOUSE Reviewed; 232 AA.
AC Q9D7F7; Q149R2; Q3TVD7; Q9CWH8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Charged multivesicular body protein 4c;
DE AltName: Full=Chromatin-modifying protein 4c;
DE Short=CHMP4c;
GN Name=Chmp4c;
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=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].
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).
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. Key
CC component of the cytokinesis checkpoint, a process required to delay
CC abscission to prevent both premature resolution of intercellular
CC chromosome bridges and accumulation of DNA damage: upon phosphorylation
CC by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent
CC VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC checkpoint signaling is terminated at late cytokinesis. Deactivation of
CC AURKB results in dephosphorylation of CHMP4C followed by its
CC dissociation from ANCHR and VPS4 and subsequent abscission. 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. CHMP4A/B/C are required for the exosomal release of SDCBP,
CC CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q96CF2}.
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. Self-associates. Interacts with CHMP2A. Interacts
CC with CHMP4A. Interacts with CHMP4B. Interacts with CHMP6. Interacts
CC with VPS4A. Interacts with PDCD6IP; the interaction is direct (By
CC similarity). {ECO:0000250|UniProtKB:Q96CF2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Late endosome
CC membrane {ECO:0000250|UniProtKB:Q96CF2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96CF2}. Midbody, Midbody ring
CC {ECO:0000250|UniProtKB:Q96CF2}. Note=Localizes to the midbody during
CC late cytokinesis. During its recruitment, localizes initially to the
CC midbody arms, before being directed to the central region, the midbody
CC ring, also called Flemming body. Phosphorylation at Ser-210 by AURKB
CC triggers localization to midbody ring. {ECO:0000250|UniProtKB:Q96CF2}.
CC -!- DOMAIN: The acidic C-terminus and the basic N-terminus 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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together
CC with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent
CC VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC checkpoint signaling is terminated at late cytokinesis.
CC {ECO:0000250|UniProtKB:Q96CF2}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AK009273; BAB26186.1; -; mRNA.
DR EMBL; AK010707; BAB27133.1; -; mRNA.
DR EMBL; AK160189; BAE35682.1; -; mRNA.
DR EMBL; BC115983; AAI15984.1; -; mRNA.
DR EMBL; BC117538; AAI17539.1; -; mRNA.
DR CCDS; CCDS17243.1; -.
DR RefSeq; NP_079795.1; NM_025519.2.
DR AlphaFoldDB; Q9D7F7; -.
DR SMR; Q9D7F7; -.
DR BioGRID; 211421; 12.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR IntAct; Q9D7F7; 11.
DR STRING; 10090.ENSMUSP00000029049; -.
DR iPTMnet; Q9D7F7; -.
DR PhosphoSitePlus; Q9D7F7; -.
DR MaxQB; Q9D7F7; -.
DR PaxDb; Q9D7F7; -.
DR PeptideAtlas; Q9D7F7; -.
DR PRIDE; Q9D7F7; -.
DR ProteomicsDB; 283909; -.
DR Antibodypedia; 12567; 74 antibodies from 18 providers.
DR DNASU; 66371; -.
DR Ensembl; ENSMUST00000029049; ENSMUSP00000029049; ENSMUSG00000027536.
DR GeneID; 66371; -.
DR KEGG; mmu:66371; -.
DR UCSC; uc008opu.1; mouse.
DR CTD; 92421; -.
DR MGI; MGI:1913621; Chmp4c.
DR VEuPathDB; HostDB:ENSMUSG00000027536; -.
DR eggNOG; KOG1656; Eukaryota.
DR GeneTree; ENSGT00940000159257; -.
DR HOGENOM; CLU_071097_0_1_1; -.
DR InParanoid; Q9D7F7; -.
DR OMA; FNELAAW; -.
DR OrthoDB; 1490465at2759; -.
DR PhylomeDB; Q9D7F7; -.
DR TreeFam; TF314269; -.
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; 66371; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Chmp4c; mouse.
DR PRO; PR:Q9D7F7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9D7F7; protein.
DR Bgee; ENSMUSG00000027536; Expressed in dorsal pancreas and 126 other tissues.
DR ExpressionAtlas; Q9D7F7; baseline and differential.
DR Genevisible; Q9D7F7; MM.
DR GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005828; C:kinetochore microtubule; 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:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0009838; P:abscission; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:1902774; P:late endosome to lysosome transport; ISO:MGI.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; ISO:MGI.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR GO; GO:0036258; P:multivesicular body assembly; IC:ComplexPortal.
DR GO; GO:0071985; P:multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; ISO:MGI.
DR GO; GO:0006997; P:nucleus organization; ISO:MGI.
DR GO; GO:0001778; P:plasma membrane repair; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010824; P:regulation of centrosome duplication; ISO:MGI.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; ISO:MGI.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC:ComplexPortal.
DR GO; GO:0046761; P:viral budding from plasma membrane; ISO:MGI.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:MGI.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..232
FT /note="Charged multivesicular body protein 4c"
FT /id="PRO_0000211496"
FT REGION 1..153
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..232
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 177..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..45
FT /evidence="ECO:0000255"
FT COILED 125..185
FT /evidence="ECO:0000255"
FT COMPBIAS 183..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 210
FT /note="Phosphoserine; by AURKB"
FT /evidence="ECO:0000250|UniProtKB:Q96CF2"
FT CONFLICT 88
FT /note="T -> I (in Ref. 1; BAB27133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 26280 MW; 8227EE2A3AD1F660 CRC64;
MSKLGKFFKG TRSSRARAAP SAQEALARLR ETEEMLAKKQ EYLENRIQRE LALAKKHGSQ
NKRAALQALK RKKRFEKQLT QVDGTLSTIE FQREALENSH TNTEVLRNMG FAAKAMKAVH
DNMDLNKIDD LMQDITEQQD IAQEISEAFS QRVQFADGFD EAELLAELEE LEQEELNKKM
TSLELPNVPS SSLPAQPSRK ASMPSSVHRS RAASSRRAEE DDDFKQLAAW AT
