ID   CHM2B_CHICK             Reviewed;         214 AA.
AC   Q5F3A2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Charged multivesicular body protein 2b;
DE   AltName: Full=Chromatin-modifying protein 2b;
DE            Short=CHMP2b;
GN   Name=CHMP2B; ORFNames=RCJMB04_25h19;
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 (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; AJ851748; CAH65382.1; -; mRNA.
DR   RefSeq; NP_001025963.1; NM_001030792.2.
DR   AlphaFoldDB; Q5F3A2; -.
DR   SMR; Q5F3A2; -.
DR   STRING; 9031.ENSGALP00000024944; -.
DR   PaxDb; Q5F3A2; -.
DR   GeneID; 418461; -.
DR   KEGG; gga:418461; -.
DR   CTD; 25978; -.
DR   VEuPathDB; HostDB:geneid_418461; -.
DR   eggNOG; KOG3231; Eukaryota.
DR   InParanoid; Q5F3A2; -.
DR   OrthoDB; 1480977at2759; -.
DR   PhylomeDB; Q5F3A2; -.
DR   PRO; PR:Q5F3A2; -.
DR   Proteomes; UP000000539; Unplaced.
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_0000211472"
FT   REGION          179..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          25..55
FT                   /evidence="ECO:0000255"
FT   MOTIF           202..212
FT                   /note="MIT-interacting motif"
SQ   SEQUENCE   214 AA;  24060 MW;  2269B70394DE5DBC CRC64;
     MASLFKKKTV DDIIKEQNRE LRGTQRTITR DRAALEKQER QLELEIKKMA KTGNKEACKV
     LAKQLVQLRK QKNRTYAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK
     TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DASDEEEESQ DIVNQVLDEI GIEISGKMAK
     APSAARGLPS ASTSKASTIS DEEIERQLKA LGVD