ID   CHMP6_PONAB             Reviewed;         201 AA.
AC   Q5R861;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Charged multivesicular body protein 6;
DE   AltName: Full=Chromatin-modifying protein 6;
GN   Name=CHMP6;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 and the
CC       budding of enveloped viruses (lentiviruses). ESCRT-III proteins are
CC       believed to mediate the necessary vesicle extrusion and/or membrane
CC       fission activities, possibly in conjunction with the AAA ATPase VPS4.
CC       In the ESCRT-III complex, it probably serves as an acceptor for the
CC       ESCRT-II complex on endosomal membrane (By similarity). {ECO:0000250}.
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. Interacts with VPS4A; the interaction is direct.
CC       Interacts with VPS4B; the interaction is direct. Interacts with CHMP4A,
CC       CHMP4B and CHMP4C. Interacts with SNF8, VPS25 and VPS36 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Endosome
CC       membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Late endosome
CC       membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:Q96FZ7}; Lipid-
CC       anchor {ECO:0000250|UniProtKB:Q96FZ7}. Note=Localizes to endosomal
CC       membranes. {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens its
CC       interaction with VPS4A (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; CR859893; CAH92049.1; -; mRNA.
DR   RefSeq; NP_001126191.1; NM_001132719.1.
DR   AlphaFoldDB; Q5R861; -.
DR   SMR; Q5R861; -.
DR   Ensembl; ENSPPYT00000010182; ENSPPYP00000009791; ENSPPYG00000008725.
DR   GeneID; 100173157; -.
DR   KEGG; pon:100173157; -.
DR   CTD; 79643; -.
DR   GeneTree; ENSGT00720000108863; -.
DR   InParanoid; Q5R861; -.
DR   Proteomes; UP000001595; Chromosome 17.
DR   GO; GO:1904930; C:amphisome membrane; IEA:Ensembl.
DR   GO; GO:0000815; C:ESCRT III complex; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0005828; C:kinetochore microtubule; IEA:Ensembl.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR   GO; GO:0030496; C:midbody; IEA:Ensembl.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:Ensembl.
DR   GO; GO:0005643; C:nuclear pore; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
DR   GO; GO:1902774; P:late endosome to lysosome transport; IEA:Ensembl.
DR   GO; GO:0061952; P:midbody abscission; IEA:Ensembl.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; IEA:Ensembl.
DR   GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IEA:Ensembl.
DR   GO; GO:0031468; P:nuclear membrane reassembly; IEA:Ensembl.
DR   GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:Ensembl.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
DR   GO; GO:0046761; P:viral budding from plasma membrane; IEA:Ensembl.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:Ensembl.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR22761; PTHR22761; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endosome; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FZ7"
FT   CHAIN           2..201
FT                   /note="Charged multivesicular body protein 6"
FT                   /id="PRO_0000211510"
FT   REGION          171..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..145
FT                   /evidence="ECO:0000255"
FT   MOTIF           168..179
FT                   /note="Type-2 MIT-interacting motif"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0A3"
FT   MOD_RES         130
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FZ7"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96FZ7"
SQ   SEQUENCE   201 AA;  23486 MW;  00246C4DE047DC02 CRC64;
     MGNLFGRKKQ SRVTEQDKAI LQLKQQRDKL RQYQKRIAQQ LERERALARQ LLRDGRKERA
     KLLLKKKRYQ EQLLDRTENQ ISSLEAMVQS IEFTQIEMKV MEGLQFGNEC LNKMHQVMSI
     EEVERILDET QEAVEYQRQI DELLAGSFTQ EDEDAILEEL SAITQEQIEL PEVPSEPLPE
     KIPEDVPVKA RPRQAELVAA S