CHM4B_MOUSE
ID CHM4B_MOUSE Reviewed; 224 AA.
AC Q9D8B3; A2AVM1; Q3TXM7; Q91VM7; Q922P1;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Charged multivesicular body protein 4b;
DE AltName: Full=Chromatin-modifying protein 4b;
DE Short=CHMP4b;
GN Name=Chmp4b;
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, and NOD; TISSUE=Small intestine, and Spleen;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND LYS-6, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
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. Together
CC with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and
CC mitotic spindle disassembly during late anaphase. Plays a role in the
CC endosomal sorting pathway. ESCRT-III proteins are believed to mediate
CC the necessary vesicle extrusion and/or membrane fission activities,
CC possibly in conjunction with the AAA ATPase VPS4. When overexpressed,
CC membrane-assembled circular arrays of CHMP4B filaments can promote or
CC stabilize negative curvature and outward budding. CHMP4A/B/C are
CC required for the exosomal release of SDCBP, CD63 and syndecan.
CC {ECO:0000250|UniProtKB:Q9H444}.
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. Interacts with CHMP6 and CHMP4C. Interacts with
CC PDCD6IP; the interaction is direct. Interacts with VPS4A; the
CC interaction is direct. Interacts with VPS4B; the interaction is direct.
CC Interacts with CHMP7. Interacts with CFTR; the interaction requires
CC misfolded CFTR. Interacts with PTPN23 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H444}.
CC -!- INTERACTION:
CC Q9D8B3; Q8WUM4: PDCD6IP; Xeno; NbExp=2; IntAct=EBI-8322817, EBI-310624;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9H444}. Late endosome membrane
CC {ECO:0000250|UniProtKB:Q9H444}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9H444}. Midbody {ECO:0000250|UniProtKB:Q9H444}.
CC Nucleus envelope {ECO:0000250|UniProtKB:Q9H444}. Note=Recruited to the
CC nuclear envelope by CHMP7 during late anaphase. Localizes transiently
CC to the midbody arms immediately before abscission.
CC {ECO:0000250|UniProtKB:Q9H444}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: ISGylated. Isgylation weakens its interaction with VPS4A (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06905.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AK008205; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK008205; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK156473; BAE33724.1; -; mRNA.
DR EMBL; AK159193; BAE34888.1; -; mRNA.
DR EMBL; AL929557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006905; AAH06905.1; ALT_INIT; mRNA.
DR EMBL; BC011429; AAH11429.1; -; mRNA.
DR EMBL; BC059279; AAH59279.1; -; mRNA.
DR CCDS; CCDS16938.1; -.
DR RefSeq; NP_083638.1; NM_029362.3.
DR AlphaFoldDB; Q9D8B3; -.
DR SMR; Q9D8B3; -.
DR BioGRID; 217613; 95.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR DIP; DIP-61322N; -.
DR IntAct; Q9D8B3; 87.
DR MINT; Q9D8B3; -.
DR STRING; 10090.ENSMUSP00000036206; -.
DR iPTMnet; Q9D8B3; -.
DR PhosphoSitePlus; Q9D8B3; -.
DR EPD; Q9D8B3; -.
DR jPOST; Q9D8B3; -.
DR MaxQB; Q9D8B3; -.
DR PaxDb; Q9D8B3; -.
DR PeptideAtlas; Q9D8B3; -.
DR PRIDE; Q9D8B3; -.
DR ProteomicsDB; 281557; -.
DR Antibodypedia; 25737; 182 antibodies from 25 providers.
DR DNASU; 75608; -.
DR Ensembl; ENSMUST00000044277; ENSMUSP00000036206; ENSMUSG00000038467.
DR GeneID; 75608; -.
DR KEGG; mmu:75608; -.
DR UCSC; uc008njp.1; mouse.
DR CTD; 128866; -.
DR MGI; MGI:1922858; Chmp4b.
DR VEuPathDB; HostDB:ENSMUSG00000038467; -.
DR eggNOG; KOG1656; Eukaryota.
DR GeneTree; ENSGT00940000154663; -.
DR HOGENOM; CLU_071097_0_0_1; -.
DR InParanoid; Q9D8B3; -.
DR OMA; WSWFGGA; -.
DR OrthoDB; 1490465at2759; -.
DR PhylomeDB; Q9D8B3; -.
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; 75608; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Chmp4b; mouse.
DR PRO; PR:Q9D8B3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D8B3; protein.
DR Bgee; ENSMUSG00000038467; Expressed in vestibular membrane of cochlear duct and 254 other tissues.
DR Genevisible; Q9D8B3; MM.
DR GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; 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:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030117; C:membrane coat; 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:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
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:0036438; P:maintenance of lens transparency; ISO:MGI.
DR GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; 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:1902902; P:negative regulation of autophagosome assembly; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0031468; P:nuclear membrane reassembly; ISS:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; ISO:MGI.
DR GO; GO:0001778; P:plasma membrane repair; ISO:MGI.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR GO; GO:0010506; P:regulation of autophagy; IMP:ParkinsonsUK-UCL.
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:0099175; P:regulation of postsynapse organization; 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:0046755; P:viral budding; ISO:MGI.
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 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Endosome; Membrane; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..224
FT /note="Charged multivesicular body protein 4b"
FT /id="PRO_0000211490"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..153
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 154..224
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 185..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..183
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H444"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H444"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H444"
FT CONFLICT 167
FT /note="E -> K (in Ref. 1; AK008205)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24936 MW; DB1D79C3C9ECCB2F CRC64;
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE LTAAKKHGTK
NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN TNTEVLKNMG YAAKAMKAAH
DNMDIDKVDE LMQDIADQQE LAEEISTAIS KPVGFGEEFD EDELMAELEE LEQEELDKNL
LEISGPETVP LPNVPSVALP SKPAKKKEEE DDDMKELENW AGSM
