CHMP7_MOUSE
ID CHMP7_MOUSE Reviewed; 451 AA.
AC Q8R1T1; Q8CFW4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Charged multivesicular body protein 7;
DE AltName: Full=Chromatin-modifying protein 7;
GN Name=Chmp7;
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] (ISOFORMS 1 AND 2).
RC STRAIN=FVB/N; TISSUE=Eye, and Liver;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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: ESCRT-III-like protein required to recruit the ESCRT-III
CC complex to the nuclear envelope (NE) during late anaphase (By
CC similarity). Together with SPAST, the ESCRT-III complex promotes NE
CC sealing and mitotic spindle disassembly during late anaphase (By
CC similarity). Recruited to the reforming NE during anaphase by LEMD2 (By
CC similarity). Plays a role in the endosomal sorting pathway (By
CC similarity). {ECO:0000250|UniProtKB:Q8WUX9}.
CC -!- SUBUNIT: Interacts with CHMP4B, but not with VPS25 (By similarity).
CC Interacts with LEMD2 (via C-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:Q8WUX9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus
CC envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization,
CC with some punctate distribution, especially in the perinuclear area.
CC Localizes to the reforming nuclear envelope on chromatin disks during
CC late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R1T1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R1T1-2; Sequence=VSP_015343, VSP_015344;
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; BC024115; AAH24115.1; -; mRNA.
DR EMBL; BC033365; AAH33365.1; -; mRNA.
DR CCDS; CCDS27242.1; -. [Q8R1T1-1]
DR RefSeq; NP_598839.2; NM_134078.4. [Q8R1T1-1]
DR AlphaFoldDB; Q8R1T1; -.
DR SMR; Q8R1T1; -.
DR BioGRID; 222870; 1.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR STRING; 10090.ENSMUSP00000047700; -.
DR iPTMnet; Q8R1T1; -.
DR PhosphoSitePlus; Q8R1T1; -.
DR EPD; Q8R1T1; -.
DR jPOST; Q8R1T1; -.
DR MaxQB; Q8R1T1; -.
DR PaxDb; Q8R1T1; -.
DR PeptideAtlas; Q8R1T1; -.
DR PRIDE; Q8R1T1; -.
DR ProteomicsDB; 281465; -. [Q8R1T1-1]
DR ProteomicsDB; 281466; -. [Q8R1T1-2]
DR Antibodypedia; 22730; 83 antibodies from 19 providers.
DR DNASU; 105513; -.
DR Ensembl; ENSMUST00000036381; ENSMUSP00000047700; ENSMUSG00000034190. [Q8R1T1-1]
DR GeneID; 105513; -.
DR KEGG; mmu:105513; -.
DR UCSC; uc007ums.2; mouse. [Q8R1T1-1]
DR CTD; 91782; -.
DR MGI; MGI:1913922; Chmp7.
DR VEuPathDB; HostDB:ENSMUSG00000034190; -.
DR eggNOG; KOG2911; Eukaryota.
DR GeneTree; ENSGT00720000108860; -.
DR HOGENOM; CLU_044768_0_0_1; -.
DR InParanoid; Q8R1T1; -.
DR OMA; NFMFSDF; -.
DR PhylomeDB; Q8R1T1; -.
DR TreeFam; TF312851; -.
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; 105513; 10 hits in 71 CRISPR screens.
DR ChiTaRS; Chmp7; mouse.
DR PRO; PR:Q8R1T1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8R1T1; protein.
DR Bgee; ENSMUSG00000034190; Expressed in cortical plate and 265 other tissues.
DR Genevisible; Q8R1T1; 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; ISO:MGI.
DR GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
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:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; 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:0045324; P:late endosome to vacuole transport; ISS:UniProtKB.
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: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: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:0071168; P:protein localization to chromatin; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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: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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..451
FT /note="Charged multivesicular body protein 7"
FT /id="PRO_0000211517"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 248..312
FT /evidence="ECO:0000255"
FT COMPBIAS 435..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT VAR_SEQ 322..370
FT /note="FNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVSQTLAGGVT ->
FT ATPLRALWSQSPTLQLPPLWSAVSGNPGFFQRVAGFSFLLGSLTSLGVR (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015343"
FT VAR_SEQ 371..451
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015344"
SQ SEQUENCE 451 AA; 50633 MW; F52C0B3F72CBA827 CRC64;
MWSPEREAQA PTGGDPAGLL PPEWEEDEER MSFLFSAFKR SREVNSTDWD SKMGFWAPLV
LSHSRRQGVV RLRLRDLQEA FQRKGSVPLG LATVLQDLLR RGELQRESDF MASVDSSWIS
WGVGVFLLKP LKWTLSNMLG DHKVPAEEVL VAVELLKEKA EEVYRLYQNS PLSSHPVVAL
SELSALCANS CPDERTFYLV LLQLQKEKRV TVLEQNGEKI VKFARGPHAK VSPVNDVDVG
VYQLMQSEQL LSRKVESLSQ ESERCKEEAR RACRAGKKQL ALRSLKAKQR TEKRIEALHA
KLDTVQGILD RIYASQTDQM VFNAYQAGVG ALKLSMKDVT VEKAESLVDQ IQELCDTQDE
VSQTLAGGVT NGLDFDSEEL EKELDILLQD TTTEPLSLLE TPQETTLYTN SVPKPRILDA
ELEAELEKLS LSEGGLIPSS KSPKRQLEPT L
