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 27-MAR-2024, entry version 103.
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; 9031-ENSGALP00000041343; -.
DR GeneID; 428673; -.
DR KEGG; gga:428673; -.
DR VEuPathDB; HostDB:geneid_428673; -.
DR eggNOG; KOG2910; Eukaryota.
DR HOGENOM; CLU_086201_3_1_1; -.
DR InParanoid; Q5ZL55; -.
DR OMA; QMLAGHL; -.
DR OrthoDB; 5398551at2759; -.
DR PhylomeDB; Q5ZL55; -.
DR Reactome; R-GGA-1632852; Macroautophagy.
DR Reactome; R-GGA-5620971; Pyroptosis.
DR Reactome; R-GGA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-GGA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:Q5ZL55; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000026428; Expressed in muscle tissue and 14 other cell types or 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; CHARGED MULTIVESICULAR BODY PROTEIN; 1.
DR PANTHER; PTHR22761:SF5; CHARGED MULTIVESICULAR BODY PROTEIN 6; 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
//
