ID   CHM6B_XENLA             Reviewed;         200 AA.
AC   Q6NU11; Q0IHK5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Charged multivesicular body protein 6-B;
DE   AltName: Full=Chromatin-modifying protein 6-B;
GN   Name=chmp6-b;
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, and Fat body;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) 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. In the ESCRT-III complex, it probably serves as an acceptor
CC       for the ESCRT-II complex on endosomal membranes (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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}. Late endosome membrane {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BC068791; AAH68791.1; -; mRNA.
DR   EMBL; BC123113; AAI23114.1; -; mRNA.
DR   RefSeq; NP_001084537.1; NM_001091068.1.
DR   AlphaFoldDB; Q6NU11; -.
DR   SMR; Q6NU11; -.
DR   DNASU; 414484; -.
DR   GeneID; 414484; -.
DR   KEGG; xla:414484; -.
DR   CTD; 414484; -.
DR   Xenbase; XB-GENE-973532; chmp6.L.
DR   OMA; QNIESAQ; -.
DR   OrthoDB; 1287094at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 414484; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
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; Endosome; Lipoprotein; Membrane; Myristate; Protein transport;
KW   Reference proteome; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..200
FT                   /note="Charged multivesicular body protein 6-B"
FT                   /id="PRO_0000211514"
FT   REGION          165..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          9..102
FT                   /evidence="ECO:0000255"
FT   MOTIF           168..179
FT                   /note="Type-2 MIT-interacting motif"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   200 AA;  23353 MW;  7E071886983BADBF CRC64;
     MGNLFARKRR SRVTEQDKAV LQLKQQRDKL KQYQKKITLQ LQRERELAKQ LLHDGKKEKA
     KLLLKKKRYQ EQLLEKTDNQ ISNLEKMVDD IEFAQIEMKV IEGLKVGNEW LKKMHEVMSI
     EEVEKIMEET QEGIEYQRQI DEMLSGSLTA EDEEAILEEL EAITQEDLEL PEAPSEPLSD
     TVPEKQAVKN RPKPQLVAAS