CHM4A_BOVIN
ID CHM4A_BOVIN Reviewed; 222 AA.
AC A2VDY3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Charged multivesicular body protein 4a;
DE AltName: Full=Chromatin-modifying protein 4a;
DE Short=CHMP4a;
GN Name=CHMP4A;
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].
RC STRAIN=Hereford; TISSUE=Fetal lung;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) 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 When overexpressed, membrane-assembled circular arrays of CHMP4A
CC filaments can promote or stabilize negative curvature and outward
CC budding. CHMP4A/B/C are required for the exosomal release of SDCBP,
CC CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q9BY43}.
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. Self-associates; overexpression leads to the
CC assembly of filaments that curve and associate to create circular
CC rings. Interacts with CHMP2A. Interacts with CHMP3; the interaction
CC requires the release of CHMP4A autoinhibition. Interacts with CHMP4B.
CC Interacts with CHMP4C. Interacts with CHMP6. Interacts with VPS4A.
CC Interacts with PDCD6IP; the interaction is direct (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000250}. Late
CC endosome membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}. Note=Membrane-associated. Localizes to large vesicle-
CC like structures. Localizes to the midbody of dividing cells. Localized
CC in two distinct rings on either side of the Fleming body (By
CC similarity). {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 -!- 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; BC133471; AAI33472.2; -; mRNA.
DR RefSeq; NP_001121976.1; NM_001128504.2.
DR AlphaFoldDB; A2VDY3; -.
DR SMR; A2VDY3; -.
DR STRING; 9913.ENSBTAP00000008352; -.
DR PaxDb; A2VDY3; -.
DR PRIDE; A2VDY3; -.
DR Ensembl; ENSBTAT00000008352; ENSBTAP00000008352; ENSBTAG00000039415.
DR GeneID; 613647; -.
DR KEGG; bta:613647; -.
DR CTD; 29082; -.
DR VEuPathDB; HostDB:ENSBTAG00000039415; -.
DR VGNC; VGNC:27302; CHMP4A.
DR eggNOG; KOG1656; Eukaryota.
DR GeneTree; ENSGT00940000163323; -.
DR HOGENOM; CLU_071097_0_0_1; -.
DR InParanoid; A2VDY3; -.
DR OMA; EHKIQQE; -.
DR OrthoDB; 1490465at2759; -.
DR TreeFam; TF314269; -.
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 10.
DR Bgee; ENSBTAG00000039415; Expressed in pons and 104 other tissues.
DR GO; GO:1904930; C:amphisome membrane; IEA:Ensembl.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
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:0030117; C:membrane coat; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:Ensembl.
DR GO; GO:0005643; C:nuclear pore; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; 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:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0010324; P:membrane invagination; 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:1902902; P:negative regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; 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:0097320; P:plasma membrane tubulation; IEA:Ensembl.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
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; Cytoplasmic vesicle; Endosome; Lipid-binding; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..222
FT /note="Charged multivesicular body protein 4a"
FT /id="PRO_0000328394"
FT REGION 1..150
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 1..116
FT /note="Interaction with phosphoinosides"
FT /evidence="ECO:0000250"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..222
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 177..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..105
FT /evidence="ECO:0000255"
FT COILED 155..180
FT /evidence="ECO:0000255"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BY43"
SQ SEQUENCE 222 AA; 24948 MW; 41B7A62D925CBB3C CRC64;
MSGLGRLFGR GKKEKGPTPE EAIQKLKETE KILIKKQEFL EQKIEQELQA AKKHGTKNKR
AALQALRRKK RLEQQLAQTD GTLSTLEFQR EAIENATTNA EVLRTMELAA QGLKKAYQDM
DIDKVDELMA DITEQQEVAQ QISDAISRPV GFGDDVDEDE LLEELEELEQ EELARELLHV
GDEEEEPPVA LPSAPSTHLP AEPAPKADED EAELKQLAEW VS
