CHMP5_PONAB
ID CHMP5_PONAB Reviewed; 219 AA.
AC Q5RBR3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Charged multivesicular body protein 5;
DE AltName: Full=Chromatin-modifying protein 5;
GN Name=CHMP5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III) which is
CC involved in multivesicular bodies (MVBs) formation and sorting of
CC endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC (ILVs) that are generated by invagination and scission from the
CC limiting membrane of the endosome and mostly are delivered to lysosomes
CC enabling degradation of membrane proteins, such as stimulated growth
CC factor receptors, lysosomal enzymes and lipids. The MVB pathway appears
CC to require the sequential function of ESCRT-O, -I,-II and -III
CC complexes. ESCRT-III proteins mostly dissociate from the invaginating
CC membrane before the ILV is released. The ESCRT machinery also functions
CC in topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis and the budding of enveloped viruses
CC (lentiviruses). ESCRT-III proteins are believed to mediate the
CC necessary vesicle extrusion and/or membrane fission activities,
CC possibly in conjunction with the AAA ATPase VPS4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- SUBUNIT: Probable peripherally associated component of the endosomal
CC sorting required for transport complex III (ESCRT-III). ESCRT-III
CC components are thought to multimerize to form a flat lattice on the
CC perimeter membrane of the endosome. Several assembly forms of ESCRT-III
CC may exist that interact and act sequentially. Interacts with VTA1.
CC Interacts with CHMP2A. Interacts with VTA1; the interaction involves
CC soluble CHMP5 (By similarity). Interacts with NOD2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9NZZ3}. Endosome membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Midbody
CC {ECO:0000250|UniProtKB:Q9NZZ3}. Note=Localizes to the midbody of
CC dividing cells. Localized in two distinct rings on either side of the
CC Flemming body. {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- PTM: ISGylated. Isgylation inhibits its interaction with VTA1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9NZZ3}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; CR858575; CAH90797.1; -; mRNA.
DR RefSeq; NP_001125453.1; NM_001131981.1.
DR AlphaFoldDB; Q5RBR3; -.
DR BMRB; Q5RBR3; -.
DR SMR; Q5RBR3; -.
DR STRING; 9601.ENSPPYP00000021442; -.
DR Ensembl; ENSPPYT00000022310; ENSPPYP00000021442; ENSPPYG00000019137.
DR GeneID; 100172361; -.
DR KEGG; pon:100172361; -.
DR CTD; 51510; -.
DR eggNOG; KOG1655; Eukaryota.
DR GeneTree; ENSGT00550000074817; -.
DR HOGENOM; CLU_079409_1_0_1; -.
DR InParanoid; Q5RBR3; -.
DR OMA; MEQAQTM; -.
DR OrthoDB; 1301560at2759; -.
DR TreeFam; TF300122; -.
DR Proteomes; UP000001595; Chromosome 9.
DR GO; GO:1904930; C:amphisome membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:Ensembl.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:Ensembl.
DR GO; GO:0005643; C:nuclear pore; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:1902774; P:late endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0007040; P:lysosome organization; IEA:Ensembl.
DR GO; GO:0061952; P:midbody abscission; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:0031468; P:nuclear membrane reassembly; IEA:Ensembl.
DR GO; GO:0001778; P:plasma membrane repair; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0001919; P:regulation of receptor recycling; IEA:Ensembl.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Ensembl.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:Ensembl.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:Ensembl.
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; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..219
FT /note="Charged multivesicular body protein 5"
FT /id="PRO_0000211502"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 26..179
FT /evidence="ECO:0000255"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZZ3"
SQ SEQUENCE 219 AA; 24571 MW; C99695F66FD7E126 CRC64;
MNRLFGKAKP KAPPPSLTDC IGTVDSRAES IDKKISRLDA ELVKYKDQIK KMREGPAKNM
VKQKALRVLK QKRMYEQQRD NLAQQSFNME QANYTIQSLK DTKTTVDAMK LGVKEMKKAY
KQVKIDQIED LQDQLEDMME DANEIQEALS RSYGTPELDE DDLEAELDAL GDELLADEDS
SYLDEAASAP AIPEGVPTDT KNKDGVLVDE FGLPQIPAS
