Human Gene CHMP4C (uc003ycl.3) Description and Page Index
Description: Homo sapiens charged multivesicular body protein 4C (CHMP4C), mRNA. RefSeq Summary (NM_152284): CHMP4C belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006 [PubMed 16730941]).[supplied by OMIM, Mar 2008]. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Gene record to access additional publications. ##Evidence-Data-START## Transcript exon combination :: AK000049.1, SRR5189655.54306.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1968189, SAMEA1968540 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000297265.5/ ENSP00000297265.4 RefSeq Select criteria :: based on single protein-coding transcript ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr8:82,644,688-82,671,748 Size: 27,061 Total Exon Count: 5 Strand: + Coding Region Position: hg19 chr8:82,644,862-82,670,779 Size: 25,918 Coding Exon Count: 5
ID:CHM4C_HUMAN DESCRIPTION: RecName: Full=Charged multivesicular body protein 4c; AltName: Full=Chromatin-modifying protein 4c; Short=CHMP4c; AltName: Full=SNF7 homolog associated with Alix 3; AltName: Full=SNF7-3; Short=hSnf7-3; AltName: Full=Vacuolar protein sorting-associated protein 32-3; Short=Vps32-3; Short=hVps32-3; FUNCTION: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV- 1 p6- and p9-dependent virus release. SUBUNIT: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Self-associates. Interacts with CHMP2A. Interacts with CHMP4A. Interacts with CHMP4B. Interacts with CHMP6. Interacts with VPS4A. Interacts with PDCD6IP; the interaction is direct. SUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane; Peripheral membrane protein (Probable). TISSUE SPECIFICITY: Expressed in heart, spleen and kidney. DOMAIN: The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components (By similarity). MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release. SIMILARITY: Belongs to the SNF7 family.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q96CF2
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.