ID   CHMP3_XENLA             Reviewed;         220 AA.
AC   Q6NRM7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 68.
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;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-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; BC070719; AAH70719.1; -; mRNA.
DR   RefSeq; NP_001084828.1; NM_001091359.1.
DR   AlphaFoldDB; Q6NRM7; -.
DR   SMR; Q6NRM7; -.
DR   DNASU; 431872; -.
DR   GeneID; 431872; -.
DR   CTD; 431872; -.
DR   Xenbase; XB-GENE-6251759; chmp3.S.
DR   OMA; INEMMDD; -.
DR   OrthoDB; 1418709at2759; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   Bgee; 431872; Expressed in testis and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
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..220
FT                   /note="Charged multivesicular body protein 3"
FT                   /id="PRO_0000211485"
FT   REGION          168..169
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   REGION          181..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..207
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          219..220
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   COILED          22..54
FT                   /evidence="ECO:0000255"
FT   MOTIF           201..209
FT                   /note="MIT-interacting motif"
FT   SITE            214
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   220 AA;  24882 MW;  A150A6B9CA06462C CRC64;
     MGLFGKTQER PPKDLVNEWS LKIRKEMRVI DRQIRDIQRE QEKVKRSIKE SAKKGNREAC
     VILAKEVVQS KKAVNKLYAS KAHMNSVLMS MKNQLAVLRV SGSLQKSTEV MKAMQNLVKL
     PEIQATMREL SKEMMKAGII EEMLEDTFEG MEDQDEMEEQ AEMEIDRILF EVTAGALGKA
     PSKVTDALPE PEITGAMAAS DEEEEEDLEA MHSRLAALRS