CHMP5_MOUSE
ID CHMP5_MOUSE Reviewed; 219 AA.
AC Q9D7S9; Q3UI64;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Charged multivesicular body protein 5;
DE AltName: Full=Chromatin-modifying protein 5;
DE AltName: Full=SNF7 domain-containing protein 2;
GN Name=Chmp5; Synonyms=Snf7dc2;
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=Amnion, and Stomach;
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=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 [3]
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).
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to lysosomes
CC enabling degradation of membrane proteins, such as stimulated growth
CC factor receptors, lysosomal enzymes and lipids. The MVB pathway appears
CC to require the sequential function of ESCRT-O, -I,-II and -III
CC complexes. ESCRT-III proteins mostly dissociate from the invaginating
CC membrane before the ILV is released. The ESCRT machinery also functions
CC in topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis. ESCRT-III proteins are believed to
CC mediate the necessary vesicle extrusion and/or membrane fission
CC activities, possibly in conjunction with the AAA ATPase VPS4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III). ESCRT-III
CC components are thought to multimerize to form a flat lattice on the
CC perimeter membrane of the endosome. Several assembly forms of ESCRT-III
CC may exist that interact and act sequentially. Interacts with VTA1.
CC Interacts with CHMP2A. Interacts with VTA1; the interaction involves
CC soluble CHMP5 (By similarity). Interacts with NOD2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NZZ3}. Endosome membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Midbody
CC {ECO:0000250|UniProtKB:Q9NZZ3}. Note=Localizes to the midbody of
CC dividing cells. Localized in two distinct rings on either side of the
CC Flemming body. {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- PTM: ISGylated. Isgylation inhibits its interaction with VTA1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AK008911; BAB25962.1; -; mRNA.
DR EMBL; AK147058; BAE27642.1; -; mRNA.
DR EMBL; BC006947; AAH06947.1; -; mRNA.
DR CCDS; CCDS18053.1; -.
DR RefSeq; NP_084090.1; NM_029814.1.
DR AlphaFoldDB; Q9D7S9; -.
DR BMRB; Q9D7S9; -.
DR SMR; Q9D7S9; -.
DR BioGRID; 218428; 15.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR STRING; 10090.ENSMUSP00000030128; -.
DR iPTMnet; Q9D7S9; -.
DR PhosphoSitePlus; Q9D7S9; -.
DR EPD; Q9D7S9; -.
DR jPOST; Q9D7S9; -.
DR MaxQB; Q9D7S9; -.
DR PaxDb; Q9D7S9; -.
DR PeptideAtlas; Q9D7S9; -.
DR PRIDE; Q9D7S9; -.
DR ProteomicsDB; 281617; -.
DR Antibodypedia; 25186; 242 antibodies from 29 providers.
DR DNASU; 76959; -.
DR Ensembl; ENSMUST00000030128; ENSMUSP00000030128; ENSMUSG00000028419.
DR GeneID; 76959; -.
DR KEGG; mmu:76959; -.
DR UCSC; uc008sia.1; mouse.
DR CTD; 51510; -.
DR MGI; MGI:1924209; Chmp5.
DR VEuPathDB; HostDB:ENSMUSG00000028419; -.
DR eggNOG; KOG1655; Eukaryota.
DR GeneTree; ENSGT00550000074817; -.
DR HOGENOM; CLU_079409_1_0_1; -.
DR InParanoid; Q9D7S9; -.
DR OMA; MEQAQTM; -.
DR OrthoDB; 1301560at2759; -.
DR PhylomeDB; Q9D7S9; -.
DR TreeFam; TF300122; -.
DR Reactome; R-MMU-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR BioGRID-ORCS; 76959; 19 hits in 77 CRISPR screens.
DR ChiTaRS; Chmp5; mouse.
DR PRO; PR:Q9D7S9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D7S9; protein.
DR Bgee; ENSMUSG00000028419; Expressed in urinary bladder urothelium and 251 other tissues.
DR Genevisible; Q9D7S9; MM.
DR GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; 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:0005634; C:nucleus; IDA: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:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP: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:0007040; P:lysosome organization; IMP:MGI.
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; TAS:ParkinsonsUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
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:0001919; P:regulation of receptor recycling; IMP: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: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 Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..219
FT /note="Charged multivesicular body protein 5"
FT /id="PRO_0000211501"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..179
FT /evidence="ECO:0000255"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZZ3"
SQ SEQUENCE 219 AA; 24576 MW; 38D13A6AD601A040 CRC64;
MNRFFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM
VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY
KEVKIDQIED LQDQLEDMME DANEIQEALG RSYGTPELDE DDLEAELDAL GDELLADEDS
SYLDEAASAP AIPEGVPTDT KNKDGVLVDE FGLPQIPAS
