ID   CHM2B_XENTR             Reviewed;         214 AA.
AC   Q6NVL7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Charged multivesicular body protein 2b;
DE   AltName: Full=Chromatin-modifying protein 2b;
DE            Short=CHMP2b;
GN   Name=chmp2b;
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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-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 (By 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 (By similarity). {ECO:0000250}.
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; BC067988; AAH67988.1; -; mRNA.
DR   RefSeq; NP_998866.1; NM_213701.1.
DR   AlphaFoldDB; Q6NVL7; -.
DR   SMR; Q6NVL7; -.
DR   STRING; 8364.ENSXETP00000016617; -.
DR   PaxDb; Q6NVL7; -.
DR   DNASU; 407966; -.
DR   Ensembl; ENSXETT00000016617; ENSXETP00000016617; ENSXETG00000007638.
DR   GeneID; 407966; -.
DR   KEGG; xtr:407966; -.
DR   CTD; 25978; -.
DR   Xenbase; XB-GENE-948820; chmp2b.
DR   eggNOG; KOG3231; Eukaryota.
DR   HOGENOM; CLU_069208_1_2_1; -.
DR   InParanoid; Q6NVL7; -.
DR   OMA; TGNRDAC; -.
DR   OrthoDB; 1480977at2759; -.
DR   PhylomeDB; Q6NVL7; -.
DR   TreeFam; TF314163; -.
DR   Reactome; R-XTR-1632852; Macroautophagy.
DR   Reactome; R-XTR-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000007638; Expressed in egg cell and 14 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..214
FT                   /note="Charged multivesicular body protein 2b"
FT                   /id="PRO_0000211476"
FT   REGION          178..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          16..55
FT                   /evidence="ECO:0000255"
FT   MOTIF           202..212
FT                   /note="MIT-interacting motif"
SQ   SEQUENCE   214 AA;  23893 MW;  B975824685F87373 CRC64;
     MASLFKKKTV DDIIREQNKE LRGTQRAITR DRAALEKQEK QLEMEIKKMA KAGNKDACRV
     LAKQLVQLRK QKTRTYAVSS KVTSMSTQTK VMSSQMKMAG AMSTTAKTMQ AVNKKMDPQK
     TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DASDDEEESQ DIVNQVLDEI GIEISGKMAK
     APSAAKGLPS TSASKSSGIS DEEIERQLKA LGVD