CHM2A_MOUSE
ID CHM2A_MOUSE Reviewed; 222 AA.
AC Q9DB34;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Charged multivesicular body protein 2a;
DE AltName: Full=Chromatin-modifying protein 2a;
DE Short=CHMP2a;
DE AltName: Full=Vacuolar protein sorting-associated protein 2;
DE Short=mVps2;
GN Name=Chmp2a;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH VPS4B.
RX PubMed=15173323; DOI=10.1242/jcs.01170;
RA Fujita H., Umezuki Y., Imamura K., Ishikawa D., Uchimura S., Nara A.,
RA Yoshimori T., Hayashizaki Y., Kawai J., Ishidoh K., Tanaka Y., Himeno M.;
RT "Mammalian class E Vps proteins, SBP1 and mVps2/CHMP2A, interact with and
RT regulate the function of an AAA-ATPase SKD1/Vps4B.";
RL J. Cell Sci. 117:2997-3009(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Lung, 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).
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. Recruited to the
CC reforming nuclear envelope (NE) during anaphase by LEMD2 (By
CC similarity). ESCRT-III proteins are believed to mediate the necessary
CC vesicle extrusion and/or membrane fission activities, possibly in
CC conjunction with the AAA ATPase VPS4. {ECO:0000250|UniProtKB:O43633}.
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. In vitro, heteromerizes with CHMP3 (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. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A,
CC CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is
CC direct. Interacts with VPS4B; the interaction is direct. Interacts with
CC MITD1. Interacts with VTA1; the interaction probably involves the open
CC conformation of CHMP2A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:O43633}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43633}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:O43633}. Cytoplasm
CC {ECO:0000269|PubMed:15173323}. Nucleus envelope
CC {ECO:0000250|UniProtKB:O43633}. Note=Localizes to the midbody of
CC dividing cells. Localized in two distinct rings on either side of the
CC Fleming body. Localizes to the reforming nuclear envelope on chromatin
CC disks during late anaphase (By similarity).
CC {ECO:0000250|UniProtKB:O43633}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart,
CC liver and kidney. {ECO:0000269|PubMed:15173323}.
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 -!- PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and
CC inhibits its interactions with VPS4A and VTA1 respectively (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AK005267; BAB23919.1; -; mRNA.
DR EMBL; BC012230; AAH12230.1; -; mRNA.
DR CCDS; CCDS20824.1; -.
DR RefSeq; NP_081161.1; NM_026885.3.
DR RefSeq; XP_006540408.1; XM_006540345.3.
DR AlphaFoldDB; Q9DB34; -.
DR SMR; Q9DB34; -.
DR BioGRID; 213137; 23.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR IntAct; Q9DB34; 10.
DR MINT; Q9DB34; -.
DR STRING; 10090.ENSMUSP00000005711; -.
DR iPTMnet; Q9DB34; -.
DR PhosphoSitePlus; Q9DB34; -.
DR EPD; Q9DB34; -.
DR jPOST; Q9DB34; -.
DR MaxQB; Q9DB34; -.
DR PaxDb; Q9DB34; -.
DR PeptideAtlas; Q9DB34; -.
DR PRIDE; Q9DB34; -.
DR ProteomicsDB; 281214; -.
DR Antibodypedia; 33353; 173 antibodies from 24 providers.
DR DNASU; 68953; -.
DR Ensembl; ENSMUST00000005711; ENSMUSP00000005711; ENSMUSG00000033916.
DR Ensembl; ENSMUST00000210587; ENSMUSP00000148218; ENSMUSG00000033916.
DR GeneID; 68953; -.
DR KEGG; mmu:68953; -.
DR UCSC; uc009ffc.2; mouse.
DR CTD; 27243; -.
DR MGI; MGI:1916203; Chmp2a.
DR VEuPathDB; HostDB:ENSMUSG00000033916; -.
DR eggNOG; KOG3230; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_069208_1_0_1; -.
DR InParanoid; Q9DB34; -.
DR OMA; RYAKKFM; -.
DR OrthoDB; 1254120at2759; -.
DR PhylomeDB; Q9DB34; -.
DR TreeFam; TF300118; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
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; 68953; 22 hits in 74 CRISPR screens.
DR ChiTaRS; Chmp2a; mouse.
DR PRO; PR:Q9DB34; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DB34; protein.
DR Bgee; ENSMUSG00000033916; Expressed in substantia propria of cornea and 269 other tissues.
DR ExpressionAtlas; Q9DB34; baseline and differential.
DR Genevisible; Q9DB34; MM.
DR GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA: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:0005765; C:lysosomal membrane; ISO:MGI.
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:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0031210; F:phosphatidylcholine binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0045184; P:establishment of protein localization; 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:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0010324; P:membrane invagination; ISO:MGI.
DR GO; GO:0061952; P:midbody abscission; ISO:MGI.
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:1903723; P:negative regulation of centriole elongation; 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:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
DR GO; GO:0051258; P:protein polymerization; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
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: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 GO; GO:0019076; P:viral release from host cell; ISO:MGI.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 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 CHAIN 1..222
FT /note="Charged multivesicular body protein 2a"
FT /id="PRO_0000211463"
FT REGION 56..222
FT /note="Interaction with VPS4B"
FT /evidence="ECO:0000250"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..222
FT /note="Interaction with VTA1"
FT /evidence="ECO:0000250"
FT COILED 12..53
FT /evidence="ECO:0000255"
FT COILED 195..222
FT /evidence="ECO:0000255"
FT MOTIF 210..220
FT /note="MIT-interacting motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43633"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43633"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43633"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43633"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43633"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43633"
SQ SEQUENCE 222 AA; 25134 MW; F2B86C623832E29E CRC64;
MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM AKQGQMDAVR
IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA QAMKGVTKAM GTMNRQLKLP
QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA MGDEEDEEES DAVVSQVLDE LGLSLTDELS
NLPSTGGSLS VAAGGKKAEA TASALADADA DLEERLKNLR RD
