ID   CHM1B_XENTR             Reviewed;         199 AA.
AC   Q6DF27; Q28HP5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Charged multivesicular body protein 1b;
DE   AltName: Full=Chromatin-modifying protein 1b;
DE            Short=CHMP1b;
GN   Name=chmp1b; ORFNames=TTpA009p13.1;
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=Tadpole;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable peripherally associated component of the endosomal
CC       sorting required for transport complex III (ESCRT-III) which is
CC       involved in multivesicular bodies (MVBs) formation and sorting of
CC       endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC       (ILVs) that are generated by invagination and scission from the
CC       limiting membrane of the endosome and mostly are delivered to lysosomes
CC       enabling degradation of membrane proteins, such as stimulated growth
CC       factor receptors, lysosomal enzymes and lipids.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome
CC       {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; CR760798; CAJ82909.1; -; mRNA.
DR   EMBL; BC076916; AAH76916.1; -; mRNA.
DR   RefSeq; NP_001005047.1; NM_001005047.1.
DR   AlphaFoldDB; Q6DF27; -.
DR   SMR; Q6DF27; -.
DR   STRING; 8364.ENSXETP00000047854; -.
DR   PaxDb; Q6DF27; -.
DR   DNASU; 448582; -.
DR   Ensembl; ENSXETT00000089621; ENSXETP00000099570; ENSXETG00000022122.
DR   GeneID; 448582; -.
DR   KEGG; xtr:448582; -.
DR   CTD; 57132; -.
DR   Xenbase; XB-GENE-5822036; chmp1b.
DR   eggNOG; KOG3232; Eukaryota.
DR   HOGENOM; CLU_080826_0_1_1; -.
DR   InParanoid; Q6DF27; -.
DR   OrthoDB; 1441797at2759; -.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000022122; Expressed in ovary and 17 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; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..199
FT                   /note="Charged multivesicular body protein 1b"
FT                   /id="PRO_0000211460"
FT   REGION          167..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          15..42
FT                   /evidence="ECO:0000255"
FT   COILED          178..199
FT                   /evidence="ECO:0000255"
FT   MOTIF           186..196
FT                   /note="MIT-interacting motif"
FT   COMPBIAS        168..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22229 MW;  66A9CE841D17978D CRC64;
     MSSMEKNLFN LKFAAKELHR NAKKCEKEEK TEKAKIKKAI QKGNTEIARI HAENAIRQKN
     QGINFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD TTLKSMNLEK ISALMDKFEH
     QFETLDVQTQ QMEDTMSNTT TLTTPQNQVD NLLHEMADEA GLDLNMELPQ GQTGSVGTSV
     ASTEQDELSQ RLARLRDQV