CHM4C_XENLA
ID CHM4C_XENLA Reviewed; 227 AA.
AC Q6GNN8;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Charged multivesicular body protein 4c;
DE AltName: Full=Chromatin-modifying protein 4c;
DE Short=CHMP4c;
GN Name=chmp4c;
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=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-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. Key component of the cytokinesis checkpoint, a process
CC required to delay abscission to prevent both premature resolution of
CC intercellular chromosome bridges and accumulation of DNA damage (By
CC similarity). {ECO:0000250|UniProtKB:Q96CF2}.
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 (By similarity). {ECO:0000250|UniProtKB:Q96CF2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Late endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; BC073466; AAH73466.1; -; mRNA.
DR RefSeq; NP_001085880.1; NM_001092411.1.
DR AlphaFoldDB; Q6GNN8; -.
DR SMR; Q6GNN8; -.
DR BioGRID; 102470; 1.
DR IntAct; Q6GNN8; 1.
DR DNASU; 444307; -.
DR GeneID; 444307; -.
DR KEGG; xla:444307; -.
DR CTD; 444307; -.
DR Xenbase; XB-GENE-954324; chmp4c.L.
DR OMA; FNELAAW; -.
DR OrthoDB; 1490465at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 444307; Expressed in intestine and 14 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:0009838; P:abscission; ISS:UniProtKB.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
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; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..227
FT /note="Charged multivesicular body protein 4c"
FT /id="PRO_0000211499"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..94
FT /evidence="ECO:0000255"
FT COILED 129..187
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 227 AA; 25480 MW; 0933D2FC9E6DD1D0 CRC64;
MSKITKLFKS SGGSGSSSKN RKGPSAQEAL FKLRETEEML TKKQEYLEKK IELELATAKK
HGTKNKRAAL QALKKKKRLE KQLAQIDGTL STIEFQREAL ENSHTNTEVL KNMGYAAKAM
KAAHENMDLE KIDDLMQDIH EQQDVAQEIS DAISRPVGFG DEFDEDELLE ELEELEQEDL
NSQMANVNLP SVPSSKLPST KLPSRPASSR KKVEDDDDMQ MLAAWAT