ID   CHMP3_DANRE             Reviewed;         221 AA.
AC   Q6NY88;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Charged multivesicular body protein 3;
DE   AltName: Full=Chromatin-modifying protein 3;
DE   AltName: Full=Vacuolar protein-sorting-associated protein 24;
GN   Name=chmp3; Synonyms=vps24; ORFNames=zgc:76972;
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=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-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. Involved in late stages of cytokinesis. Plays a role in
CC       endosomal sorting/trafficking of EGF receptor (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. Several assembly forms of ESCRT-III may exist that interact
CC       and act sequentially (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}. Endosome {ECO:0000250}. Late
CC       endosome membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BC066696; AAH66696.1; -; mRNA.
DR   RefSeq; NP_998485.1; NM_213320.1.
DR   AlphaFoldDB; Q6NY88; -.
DR   SMR; Q6NY88; -.
DR   STRING; 7955.ENSDARP00000055486; -.
DR   PaxDb; Q6NY88; -.
DR   PRIDE; Q6NY88; -.
DR   Ensembl; ENSDART00000055487; ENSDARP00000055486; ENSDARG00000038064.
DR   GeneID; 406621; -.
DR   KEGG; dre:406621; -.
DR   CTD; 51652; -.
DR   ZFIN; ZDB-GENE-040426-2600; chmp3.
DR   eggNOG; KOG3229; Eukaryota.
DR   GeneTree; ENSGT00950000182832; -.
DR   HOGENOM; CLU_069208_0_1_1; -.
DR   InParanoid; Q6NY88; -.
DR   OMA; INEMMDD; -.
DR   OrthoDB; 1418709at2759; -.
DR   PhylomeDB; Q6NY88; -.
DR   TreeFam; TF105848; -.
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:Q6NY88; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 17.
DR   Bgee; ENSDARG00000038064; Expressed in pharyngeal gill and 26 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR10476; PTHR10476; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Endosome; Lipoprotein; Membrane; Myristate;
KW   Protein transport; Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..221
FT                   /note="Charged multivesicular body protein 3"
FT                   /id="PRO_0000211484"
FT   REGION          59..64
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   REGION          168..169
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   REGION          181..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..206
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          220..221
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   COILED          22..54
FT                   /evidence="ECO:0000255"
FT   COILED          144..221
FT                   /evidence="ECO:0000255"
FT   MOTIF           200..210
FT                   /note="MIT-interacting motif"
FT   SITE            215
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   221 AA;  24807 MW;  B902180BD13DF373 CRC64;
     MGLFGKTQEK PPKDLINEWS LKIRKEMRVI DRQIRDIQRE EEKVKRSIKD AAKKGQKDVC
     IILAKEMIQS KRAINKLYAS KAQMNSVLLS MKNQLSVLRV AGALQKSTEV MKAMQSLVKI
     PEIQATMRDL SKEMMKAGII EEMLEDTLEG MDDEEEMEEA AEAEVDKILF EITAGALGKA
     PSKVTDLPDP VAIGATAAPE EESEEEEEIE EMQSRLAALR S