CHMP3_XENTR
ID CHMP3_XENTR Reviewed; 220 AA.
AC Q5BKM3; Q28CN4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 4.
DT 03-AUG-2022, entry version 93.
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=TEgg091h16.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20431018; DOI=10.1126/science.1183670;
RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT "The genome of the Western clawed frog Xenopus tropicalis.";
RL Science 328:633-636(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-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. 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; CR926287; CAJ81451.1; -; mRNA.
DR EMBL; AAMC01068556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC091022; AAH91022.1; -; mRNA.
DR RefSeq; NP_001016229.2; NM_001016229.2.
DR AlphaFoldDB; Q5BKM3; -.
DR SMR; Q5BKM3; -.
DR STRING; 8364.ENSXETP00000016999; -.
DR PaxDb; Q5BKM3; -.
DR GeneID; 548983; -.
DR KEGG; xtr:548983; -.
DR CTD; 51652; -.
DR Xenbase; XB-GENE-1005141; chmp3.
DR eggNOG; KOG3229; Eukaryota.
DR HOGENOM; CLU_069208_0_1_1; -.
DR InParanoid; Q5BKM3; -.
DR OMA; RICHFAT; -.
DR TreeFam; TF105848; -.
DR Reactome; R-XTR-1632852; Macroautophagy.
DR Reactome; R-XTR-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000017980; Expressed in testis and 13 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..220
FT /note="Charged multivesicular body protein 3"
FT /id="PRO_0000211486"
FT REGION 168..169
FT /note="Important for autoinhibitory function"
FT /evidence="ECO:0000250"
FT REGION 196..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 COILED 197..220
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"
FT CONFLICT 29
FT /note="V -> L (in Ref. 3; AAH91022)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 220 AA; 24882 MW; DA7CCAD10C1FB0B9 CRC64;
MGLFGKTQER PPKDLVNEWS LKIRKEMRVI DRQIRDIQRE QEKVKRSIKE SAKKGNREAC
VILAKEVVHS KKAVNKLYAS KAHMNSVLMS MKNQLAVLRV SGSLQKSTEV MKAMQNLVKI
PEIQATMRDL SKEMMKAGII EEMLEDTFEG MEDQDEMEEQ AEMEIDRILF EITAGALGKA
PSKVTDALPE PEITGAMAAS DEEEEEDLEA MQSRLAALRS
