ID   CHMP6_CHICK             Reviewed;         200 AA.
AC   Q5ZL55;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Charged multivesicular body protein 6;
DE   AltName: Full=Chromatin-modifying protein 6;
GN   Name=CHMP6; ORFNames=RCJMB04_7k13;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719879; CAG31538.1; -; mRNA.
DR   RefSeq; NP_001026700.1; NM_001031529.1.
DR   AlphaFoldDB; Q5ZL55; -.
DR   SMR; Q5ZL55; -.
DR   STRING; 9031.ENSGALP00000041343; -.
DR   PaxDb; Q5ZL55; -.
DR   Ensembl; ENSGALT00000044736; ENSGALP00000041343; ENSGALG00000026428.
DR   GeneID; 428673; -.
DR   KEGG; gga:428673; -.
DR   CTD; 79643; -.
DR   VEuPathDB; HostDB:geneid_428673; -.
DR   eggNOG; KOG2910; Eukaryota.
DR   GeneTree; ENSGT00720000108863; -.
DR   HOGENOM; CLU_086201_3_1_1; -.
DR   InParanoid; Q5ZL55; -.
DR   OMA; GTIEFKL; -.
DR   OrthoDB; 1287094at2759; -.
DR   PhylomeDB; Q5ZL55; -.
DR   PRO; PR:Q5ZL55; -.
DR   Proteomes; UP000000539; Chromosome 18.
DR   Bgee; ENSGALG00000026428; Expressed in muscle tissue and 14 other tissues.
DR   ExpressionAtlas; Q5ZL55; baseline and differential.
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:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
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"
FT                   /id="PRO_0000211511"
FT   REGION          169..200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          10..94
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;  23259 MW;  47A57E583BD99B14 CRC64;
     MGNLFGRKRR SRVTEQDKAV LQLKQQRDKL RQYQKRISLG LERERELARQ LLKEGKKEKA
     MLLLKKKRYQ EQLLDKTDNQ ISNLERMVQD IEFTQIEMKV IEGLKIGNEC LNKMHQVMSI
     EEVERIIGET QDAVEYQRQI DEILAGSLTE EDEDAILEEL NAITQEQLEL PDVPSEPLPE
     EPPEATPVKN RPKPELVAAS