ID   CHMP7_XENTR             Reviewed;         468 AA.
AC   Q5FW14;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Charged multivesicular body protein 7;
DE   AltName: Full=Chromatin-modifying protein 7;
GN   Name=chmp7;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III
CC       complex to the nuclear envelope during late anaphase. Together with
CC       SPAST, the ESCRT-III complex promotes nuclear envelope sealing and
CC       mitotic spindle disassembly during late anaphase. Plays a role in the
CC       endosomal sorting pathway. {ECO:0000250|UniProtKB:Q8WUX9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WUX9}. Nucleus
CC       envelope {ECO:0000250|UniProtKB:Q8WUX9}. Note=Diffused localization,
CC       with some punctate distribution, especially in the perinuclear area.
CC       Localizes to the nucleus envelope during late anaphase.
CC       {ECO:0000250|UniProtKB:Q8WUX9}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BC089669; AAH89669.1; -; mRNA.
DR   RefSeq; NP_001015735.1; NM_001015735.1.
DR   AlphaFoldDB; Q5FW14; -.
DR   DNASU; 548452; -.
DR   GeneID; 548452; -.
DR   KEGG; xtr:548452; -.
DR   CTD; 91782; -.
DR   Xenbase; XB-GENE-5867894; chmp7.
DR   InParanoid; Q5FW14; -.
DR   OrthoDB; 832779at2759; -.
DR   Reactome; R-XTR-1632852; Macroautophagy.
DR   Reactome; R-XTR-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0045324; P:late endosome to vacuole transport; ISS:UniProtKB.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISS:UniProtKB.
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; 2.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nucleus; Protein transport; Reference proteome;
KW   Transport.
FT   CHAIN           1..468
FT                   /note="Charged multivesicular body protein 7"
FT                   /id="PRO_0000211522"
FT   REGION          428..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          233..303
FT                   /evidence="ECO:0000255"
FT   COILED          353..379
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        441..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  52908 MW;  1F9D571B5C1DC831 CRC64;
     MAALSCYPPE WDDDERMSFL FSAFKQTRDV NTSDWDGKMK FWIPLILKHA RAQGLLSISL
     SQLERDFRRK GFAPLGLRIV IQEMMRQGTL RKESDYVSNV SSGWLSWGMR QLVIRPLRWT
     IGTVLGSQMG PDEPLVIPEI IKERAALVLQ RYQSSPLRAL PLLSEEEVRT LCAEICPNPS
     ALNLVLLQLQ GDKKICVLER AGKKLVKFVR VSVGQVDPIS ESDLGIYELQ QSEKLLSERL
     QSAGEESDRL TEEARTYNRA GNKHQALRCL RKRKLLERRI TELQNKQDTV QGILERIAAA
     ETDRKVVSAY QMGVSALKLA LKDVTMEKAE SIVDQIQEYC DLQDDLSQTL ASVSDADIDS
     EDLEKELNDI LQNKEMIVDL PDVPSGPVVI SPQRPTEWET DQDIDSEDLE KELNDILQKE
     EMIVDLPDVP SGPVVISPQR PTEWKTDQAS RSPADGSFSR SVPEPVLQ