ID   CHMP6_DANRE             Reviewed;         206 AA.
AC   Q503V0; Q6DRE9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Charged multivesicular body protein 6;
DE   AltName: Full=Chromatin-modifying protein 6;
GN   Name=chmp6; Synonyms=chmp6l;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA   Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA   Hopkins N.;
RT   "Identification of 315 genes essential for early zebrafish development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=AB; TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAY-2005) 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. In the ESCRT-III complex, it probably serves as an acceptor
CC       for the ESCRT-II complex on endosomal membranes (By similarity).
CC       {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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}. Late endosome membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY648810; AAT68128.1; -; mRNA.
DR   EMBL; BC095171; AAH95171.1; -; mRNA.
DR   RefSeq; NP_001003874.1; NM_001003874.1.
DR   AlphaFoldDB; Q503V0; -.
DR   SMR; Q503V0; -.
DR   STRING; 7955.ENSDARP00000012210; -.
DR   PaxDb; Q503V0; -.
DR   Ensembl; ENSDART00000158043; ENSDARP00000130680; ENSDARG00000102024.
DR   Ensembl; ENSDART00000181861; ENSDARP00000150680; ENSDARG00000102024.
DR   GeneID; 445397; -.
DR   KEGG; dre:445397; -.
DR   CTD; 445397; -.
DR   ZFIN; ZDB-GENE-040924-2; chmp6b.
DR   eggNOG; KOG2910; Eukaryota.
DR   GeneTree; ENSGT00720000108863; -.
DR   InParanoid; Q503V0; -.
DR   OrthoDB; 1287094at2759; -.
DR   PhylomeDB; Q503V0; -.
DR   Reactome; R-DRE-1632852; Macroautophagy.
DR   Reactome; R-DRE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-DRE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   PRO; PR:Q503V0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 12.
DR   Bgee; ENSDARG00000102024; Expressed in muscle tissue and 22 other tissues.
DR   ExpressionAtlas; Q503V0; baseline.
DR   GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
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; Protein transport;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..206
FT                   /note="Charged multivesicular body protein 6"
FT                   /id="PRO_0000211512"
FT   REGION          167..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          11..103
FT                   /evidence="ECO:0000255"
FT   MOTIF           170..181
FT                   /note="Type-2 MIT-interacting motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        183..206
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        165
FT                   /note="Q -> H (in Ref. 1; AAT68128)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   206 AA;  23980 MW;  36FEDB1AD87ECDF8 CRC64;
     MGNLFGKKKA TRVTEQDRAV LQLKQQRDKL KQYQKRITLQ MDKERQLAKQ LLKDGKKDKA
     LLLLKKKRYQ DQLLEKTENQ ISNLERMVQD IEFAQIEMKV IEGLKVGNDC LKKMHEVLSI
     EEVEKIMDET HDAIEYQKQI DEMLAGSLTQ EDEEAVLAEL EAITQGEADL ELPEVPGEEL
     PEVPEQEPVR EKERVKKKPE REMVAV