ID   CHMP7_DANRE             Reviewed;         457 AA.
AC   Q6PBQ2; Q6NYA6;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Charged multivesicular body protein 7;
DE   AltName: Full=Chromatin-modifying protein 7;
GN   Name=chmp7;
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 MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2003) 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; BC059625; AAH59625.1; -; mRNA.
DR   EMBL; BC066676; AAH66676.1; -; mRNA.
DR   RefSeq; NP_957075.1; NM_200781.1.
DR   AlphaFoldDB; Q6PBQ2; -.
DR   SMR; Q6PBQ2; -.
DR   STRING; 7955.ENSDARP00000060627; -.
DR   PaxDb; Q6PBQ2; -.
DR   GeneID; 393754; -.
DR   KEGG; dre:393754; -.
DR   CTD; 91782; -.
DR   ZFIN; ZDB-GENE-040426-1750; chmp7.
DR   eggNOG; KOG2911; Eukaryota.
DR   InParanoid; Q6PBQ2; -.
DR   OrthoDB; 832779at2759; -.
DR   PhylomeDB; Q6PBQ2; -.
DR   Reactome; R-DRE-1632852; Macroautophagy.
DR   Reactome; R-DRE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-DRE-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   PRO; PR:Q6PBQ2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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; 1.
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..457
FT                   /note="Charged multivesicular body protein 7"
FT                   /id="PRO_0000211520"
FT   REGION          381..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..457
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..266
FT                   /evidence="ECO:0000255"
FT   COILED          331..382
FT                   /evidence="ECO:0000255"
FT   CONFLICT        421
FT                   /note="M -> V (in Ref. 1; AAH66676)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   457 AA;  50980 MW;  5BA57FE18A6259FD CRC64;
     MSVSVEKRSA WFPPDWDDDE RMSFLFSAFK ENRDVDCTDW DGKIDFWSPL IIEHCRRCGS
     VCVNLQDLNE NFRRKGSVPL GLSTVIQSMI RSGKVQKESD FAANVDSGWL SWGVGLLLVR
     PLKWTLSALL GSGRVPLEES FVVIELVKEK AAELLAAYRG SALSARSLLS FQELRSLSSH
     ICPDESTLCM ALLQLQREKH VTVSLHEGEK LVKFSQAGQG RVSPVSEVDL GIYQLQCSEK
     LLEERVEALG HEAEKCKQQA KSLLKEGKKS QALRCLRGSK RVEKKADRLF AQLETVKGIL
     DRIANSQTDR LVMQAYQAGV AALRISLKGV TVERAENLVD QIQELCDTQD EVNQTLASGA
     PDAGEDSEDL EEELKSLMEK SVPENDLFPA VPTHPITPPR KTDLPDAAFV QFLPSVPNPG
     MNITDEELDR ELRRLTVSDK GLPRESVSPQ RRLEPAQ