ID   CHM2A_XENLA             Reviewed;         220 AA.
AC   Q6IP52; Q3KPQ0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Charged multivesicular body protein 2a;
DE   AltName: Full=Chromatin-modifying protein 2a;
DE            Short=CHMP2a;
GN   Name=chmp2a;
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=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2005) 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: Late endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC       Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BC072066; AAH72066.1; -; mRNA.
DR   EMBL; BC106618; AAI06619.1; -; mRNA.
DR   RefSeq; NP_001085225.1; NM_001091756.1.
DR   RefSeq; XP_018079949.1; XM_018224460.1.
DR   RefSeq; XP_018079950.1; XM_018224461.1.
DR   AlphaFoldDB; Q6IP52; -.
DR   SMR; Q6IP52; -.
DR   MaxQB; Q6IP52; -.
DR   DNASU; 432320; -.
DR   GeneID; 432320; -.
DR   KEGG; xla:432320; -.
DR   CTD; 432320; -.
DR   Xenbase; XB-GENE-6255415; chmp2a.L.
DR   OMA; RYAKKFM; -.
DR   OrthoDB; 1254120at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 432320; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISS:UniProtKB.
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; 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..220
FT                   /note="Charged multivesicular body protein 2a"
FT                   /id="PRO_0000211466"
FT   REGION          196..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          12..53
FT                   /evidence="ECO:0000255"
FT   COILED          198..219
FT                   /evidence="ECO:0000255"
FT   MOTIF           208..218
FT                   /note="MIT-interacting motif"
FT   COMPBIAS        206..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   220 AA;  25015 MW;  A71F31F46807D4D2 CRC64;
     MEFLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLEQQE KKIIADIKKM AKQGQMDAVK
     IMAKDLVRTR RYVKKFIMMR ANIQAVSLKI QTLKSNNSMA QAMKGVTKAM ATMNRQLKLP
     QIQKIMMEFE KQSEIMDMKE EMMNDAIDDA MGDEDDEEES DAVVSQVLDE LGLTLTDELS
     NLPSTGGSLS VAGAKKGEAT AALADADADL EERLNNLRRD