ID   CHM2B_DANRE             Reviewed;         214 AA.
AC   Q6NXD2; A2AVM3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Charged multivesicular body protein 2b;
DE   AltName: Full=Chromatin-modifying protein 2b;
DE            Short=CHMP2b;
GN   Name=chmp2b; ORFNames=si:ch211-106g5.3, zgc:77025;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) 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; AL929559; CAM13123.1; -; Genomic_DNA.
DR   EMBL; BC067142; AAH67142.1; -; mRNA.
DR   RefSeq; NP_998069.1; NM_212904.2.
DR   AlphaFoldDB; Q6NXD2; -.
DR   SMR; Q6NXD2; -.
DR   STRING; 7955.ENSDARP00000008354; -.
DR   PaxDb; Q6NXD2; -.
DR   PRIDE; Q6NXD2; -.
DR   Ensembl; ENSDART00000018472; ENSDARP00000008354; ENSDARG00000002190.
DR   GeneID; 405840; -.
DR   KEGG; dre:405840; -.
DR   CTD; 405840; -.
DR   ZFIN; ZDB-GENE-040426-2539; chmp2bb.
DR   eggNOG; KOG3231; Eukaryota.
DR   GeneTree; ENSGT00950000182832; -.
DR   HOGENOM; CLU_069208_1_2_1; -.
DR   InParanoid; Q6NXD2; -.
DR   OMA; TGNRDAC; -.
DR   OrthoDB; 1480977at2759; -.
DR   PhylomeDB; Q6NXD2; -.
DR   PRO; PR:Q6NXD2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 1.
DR   Bgee; ENSDARG00000002190; Expressed in mature ovarian follicle and 29 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_0000211473"
FT   REGION          178..199
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;  24017 MW;  9098730030EBE605 CRC64;
     MTSLFKKKTV DDVIKEQNKE LRGTQRQIAR DRTALEKQEK QLEMEIKKMA KTGNRDACKV
     LAKQLVQVRK QKTRTYAVSS KVTSMSTQTK LMNSQMKMAG AMATTTKTMQ AVNKKMDPKK
     TMQTLQNFQK ETAKMDMTEE MMNDTLDEIF EDSGDEEESQ DIVNQVLDEI GIEISGKMAH
     APSAARKTPS AATAKADGIS DEDIERQLKA LGVD