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CHM4B_DANRE
ID   CHM4B_DANRE             Reviewed;         220 AA.
AC   Q7ZVC4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Charged multivesicular body protein 4b;
DE   AltName: Full=Chromatin-modifying protein 4b;
DE            Short=CHMP4b;
GN   Name=chmp4b; ORFNames=zgc:56112;
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].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JAN-2003) 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|UniProtKB:Q9H444}.
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|UniProtKB:Q9H444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9H444}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9H444}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9H444}. Midbody {ECO:0000250|UniProtKB:Q9H444}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BC045919; AAH45919.1; -; mRNA.
DR   RefSeq; NP_956489.1; NM_200195.1.
DR   AlphaFoldDB; Q7ZVC4; -.
DR   SMR; Q7ZVC4; -.
DR   STRING; 7955.ENSDARP00000017897; -.
DR   PaxDb; Q7ZVC4; -.
DR   GeneID; 393164; -.
DR   KEGG; dre:393164; -.
DR   CTD; 393164; -.
DR   ZFIN; ZDB-GENE-040426-906; chmp4ba.
DR   eggNOG; KOG1656; Eukaryota.
DR   InParanoid; Q7ZVC4; -.
DR   OrthoDB; 1490465at2759; -.
DR   PhylomeDB; Q7ZVC4; -.
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:Q7ZVC4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IGI:ZFIN.
DR   GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0090148; P:membrane fission; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; 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: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; Endosome; Membrane; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..220
FT                   /note="Charged multivesicular body protein 4b"
FT                   /id="PRO_0000211492"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          21..88
FT                   /evidence="ECO:0000255"
FT   COILED          123..181
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   220 AA;  24796 MW;  747F523B7F88EA81 CRC64;
     MSLFGKMFGS GGKGGKSASP QEAIQRLRET EEMLTKKQEF LEKKIEQELV TAKKNGTKNK
     RAALQALKRK KRYEKQLAQI DGTLSTIEFQ REALENAHTN TEVIKNMGYA AKAMKAAHDN
     MDIDKVDELM QDIIEQQELA QEISDAISKP VGFGEEFDED ELLAELEELE QEELDKNLLE
     IGDNVPLPNV PSTSLPSRPA KKKEEEDEDD MKDLEAWAAN
 
 
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