CHM1A_MOUSE
ID CHM1A_MOUSE Reviewed; 196 AA.
AC Q921W0; Q3TW57;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Charged multivesicular body protein 1a;
DE AltName: Full=Chromatin-modifying protein 1a;
DE Short=CHMP1a;
GN Name=Chmp1a; Synonyms=Chmp1 {ECO:0000250|UniProtKB:Q9HD42}, Pcoln3;
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=Corpora quadrigemina;
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] {ECO:0000305, ECO:0000312|EMBL:AAH10524.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH10524.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH23807.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH36138.1}, and
RC Mammary gland {ECO:0000312|EMBL:AAH10524.1};
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] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH PHF1.
RX PubMed=11559747; DOI=10.1242/jcs.114.13.2383;
RA Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.;
RT "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and
RT cell-cycle progression.";
RL J. Cell Sci. 114:2383-2393(2001).
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. Involved
CC in cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the
CC midbody of dividing cells. May also be involved in chromosome
CC condensation. Targets the Polycomb group (PcG) protein BMI1/PCGF4 to
CC regions of condensed chromatin. May play a role in stable cell cycle
CC progression and in PcG gene silencing (By 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. Self-associates.
CC Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B.
CC Interacts with PHF1. Interacts with IST1. Interacts with MITD1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11559747}. Endosome
CC membrane {ECO:0000269|PubMed:11559747}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11559747}. Nucleus matrix
CC {ECO:0000269|PubMed:11559747}. Note=The cytoplasmic form is partially
CC membrane-associated and localizes to early endosomes. The nuclear form
CC remains associated with the chromosome scaffold during mitosis. On
CC overexpression, it localizes to nuclear bodies characterized by
CC nuclease-resistant condensed chromatin.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult heart, kidney and liver.
CC Expressed at lower levels in adult colon, spleen, lung, brain, testis
CC and muscle. Also expressed in myoblasts and embryo fibroblasts.
CC {ECO:0000269|PubMed:11559747}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000255}.
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DR EMBL; AK046416; BAC32719.1; -; mRNA.
DR EMBL; AK159830; BAE35409.1; -; mRNA.
DR EMBL; BC010524; AAH10524.1; -; mRNA.
DR EMBL; BC023807; AAH23807.1; -; mRNA.
DR EMBL; BC036138; AAH36138.1; -; mRNA.
DR EMBL; BC036152; AAH36152.1; -; mRNA.
DR CCDS; CCDS40509.1; -.
DR RefSeq; NP_663581.1; NM_145606.3.
DR AlphaFoldDB; Q921W0; -.
DR SMR; Q921W0; -.
DR BioGRID; 231588; 8.
DR ComplexPortal; CPX-332; ESCRT-III complex, variant Chmp1b1.
DR ComplexPortal; CPX-333; ESCRT-III complex, variant Chmp1b2.
DR STRING; 10090.ENSMUSP00000000759; -.
DR iPTMnet; Q921W0; -.
DR PhosphoSitePlus; Q921W0; -.
DR EPD; Q921W0; -.
DR MaxQB; Q921W0; -.
DR PaxDb; Q921W0; -.
DR PeptideAtlas; Q921W0; -.
DR PRIDE; Q921W0; -.
DR ProteomicsDB; 281213; -.
DR DNASU; 234852; -.
DR Ensembl; ENSMUST00000000759; ENSMUSP00000000759; ENSMUSG00000000743.
DR GeneID; 234852; -.
DR KEGG; mmu:234852; -.
DR UCSC; uc009nuk.2; mouse.
DR CTD; 5119; -.
DR MGI; MGI:1920159; Chmp1a.
DR VEuPathDB; HostDB:ENSMUSG00000000743; -.
DR eggNOG; KOG3232; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_080826_1_0_1; -.
DR InParanoid; Q921W0; -.
DR OMA; KFASKQM; -.
DR OrthoDB; 1441797at2759; -.
DR PhylomeDB; Q921W0; -.
DR TreeFam; TF300076; -.
DR BioGRID-ORCS; 234852; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Chmp1a; mouse.
DR PRO; PR:Q921W0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q921W0; protein.
DR Bgee; ENSMUSG00000000743; Expressed in dorsal pancreas and 254 other tissues.
DR Genevisible; Q921W0; MM.
DR GO; GO:1904930; C:amphisome membrane; ISO:MGI.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
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:0005815; C:microtubule organizing center; ISS:UniProtKB.
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:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific 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:0051301; P:cell division; ISO:MGI.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
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:0061952; P:midbody abscission; ISO:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; 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:0010629; P:negative regulation of gene expression; 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; 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:0016192; P:vesicle-mediated transport; 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; IPR029888; CHMP1A.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR PANTHER; PTHR10476:SF17; PTHR10476:SF17; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome;
KW Membrane; Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Transport.
FT CHAIN 1..196
FT /note="Charged multivesicular body protein 1a"
FT /id="PRO_0000211449"
FT COILED 5..42
FT /evidence="ECO:0000255"
FT COILED 102..124
FT /evidence="ECO:0000255"
FT MOTIF 185..195
FT /note="MIT-interacting motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD42"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD42"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD42"
SQ SEQUENCE 196 AA; 21608 MW; 19A01EB7C900E858 CRC64;
MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALQQK NVECARVYAE NAIRKKNEGV
NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL SAMDLQKVSA VMDRFEQQVQ
NLDVHTSVME DSVSSATTLT TPQEQVDSLI VQIAEENGLE VLDQLSQLPE GASAVGESSV
RSQEDQLSRR LAALRN
