ID   CHMP3_BOVIN             Reviewed;         222 AA.
AC   Q58CS7; Q29RQ4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 105.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) 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       Selectively binds to phosphatidylinositol 3,5-bisphosphate
CC       PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other
CC       phosphoinositides tested. Involved in late stages of cytokinesis. Plays
CC       a role in endosomal sorting/trafficking of EGF receptor (By
CC       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. Forms a metastable monomer in solution; its core
CC       structure (without part of the putative autoinhibitory C-terminal
CC       acidic region) oligomerizes into a flat lattice via two different
CC       dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not
CC       CHMP4) to form helical tubular structures that expose membrane-
CC       interacting sites on the outside whereas VPS4B can associate on the
CC       inside of the tubule. May interact with IGFBP7; the relevance of such
CC       interaction however remains unclear. Interacts with CHMP2A. Interacts
CC       with CHMP4A; the interaction requires the release of CHMP4A
CC       autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the
CC       interaction appears to relieve the autoinhibition of CHMP3 (By
CC       similarity). Interacts with VTA1 (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}. Note=Localizes to the midbody of
CC       dividing cells. {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.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BT021870; AAX46717.1; -; mRNA.
DR   EMBL; BC114072; AAI14073.1; -; mRNA.
DR   RefSeq; NP_001030223.2; NM_001035051.3.
DR   AlphaFoldDB; Q58CS7; -.
DR   SMR; Q58CS7; -.
DR   STRING; 9913.ENSBTAP00000018071; -.
DR   PaxDb; Q58CS7; -.
DR   PRIDE; Q58CS7; -.
DR   Ensembl; ENSBTAT00000018071; ENSBTAP00000018071; ENSBTAG00000013589.
DR   GeneID; 507722; -.
DR   KEGG; bta:507722; -.
DR   CTD; 51652; -.
DR   VEuPathDB; HostDB:ENSBTAG00000013589; -.
DR   eggNOG; KOG3229; Eukaryota.
DR   GeneTree; ENSGT00950000182832; -.
DR   HOGENOM; CLU_069208_0_1_1; -.
DR   InParanoid; Q58CS7; -.
DR   OMA; INEMMDD; -.
DR   OrthoDB; 1418709at2759; -.
DR   TreeFam; TF105848; -.
DR   Reactome; R-BTA-1632852; Macroautophagy.
DR   Reactome; R-BTA-5620971; Pyroptosis.
DR   Reactome; R-BTA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000013589; Expressed in adenohypophysis and 107 other tissues.
DR   ExpressionAtlas; Q58CS7; baseline and differential.
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; Isopeptide bond; Lipoprotein; Membrane;
KW   Myristate; Phosphoprotein; Protein transport; Reference proteome;
KW   Transport; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..222
FT                   /note="Charged multivesicular body protein 3"
FT                   /id="PRO_0000211478"
FT   REGION          2..113
FT                   /note="Intramolecular interaction with C-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          59..64
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   REGION          151..222
FT                   /note="Interaction with VPS4A"
FT                   /evidence="ECO:0000250"
FT   REGION          151..220
FT                   /note="Intramolecular interaction with N-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          168..169
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   REGION          180..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          196..222
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          203..207
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          221..222
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   COILED          22..54
FT                   /evidence="ECO:0000255"
FT   COILED          149..222
FT                   /evidence="ECO:0000255"
FT   MOTIF           201..211
FT                   /note="MIT-interacting motif"
FT                   /evidence="ECO:0000250"
FT   SITE            48
FT                   /note="Important for autoinhibitory function"
FT                   /evidence="ECO:0000250"
FT   SITE            216
FT                   /note="Interaction with STAMBP"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3E7"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        179
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y3E7"
SQ   SEQUENCE   222 AA;  25017 MW;  83B40B1402A9A0D7 CRC64;
     MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC
     VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI
     PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEA AEMEIDRILF EITAGALGKA
     PSKVTDALPE PEPLGAMAAS EDEEEEEEAL EAMQSRLATL RS