CHM1A_PONAB
ID CHM1A_PONAB Reviewed; 196 AA.
AC Q5R605;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Charged multivesicular body protein 1a;
DE AltName: Full=Chromatin-modifying protein 1a;
DE Short=CHMP1a;
GN Name=CHMP1A; Synonyms=PCOLN3;
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=Brain cortex;
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. Involved in
CC cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody
CC of dividing cells. May also be involved in chromosome condensation.
CC Targets the Polycomb group (PcG) protein BMI1/PCGF4 to regions of
CC condensed chromatin. May play a role in stable cell cycle progression
CC and in PcG gene silencing (By similarity). {ECO:0000250}.
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. Self-associates.
CC Interacts with CHMP1B. Interacts with VPS4A. Interacts with VPS4B.
CC Interacts with PHF1. Interacts with IST1. Interacts with MITD1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus
CC matrix {ECO:0000250}. Note=The cytoplasmic form is partially membrane-
CC associated and localizes to early endosomes. The nuclear form remains
CC associated with the chromosome scaffold during mitosis. On
CC overexpression, it localizes to nuclear bodies characterized by
CC nuclease-resistant condensed chromatin (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; CR860695; CAH92811.1; -; mRNA.
DR RefSeq; NP_001126640.1; NM_001133168.1.
DR AlphaFoldDB; Q5R605; -.
DR SMR; Q5R605; -.
DR STRING; 9601.ENSPPYP00000008644; -.
DR GeneID; 100173638; -.
DR KEGG; pon:100173638; -.
DR CTD; 5119; -.
DR eggNOG; KOG3232; Eukaryota.
DR HOGENOM; CLU_080826_1_0_1; -.
DR InParanoid; Q5R605; -.
DR OMA; KFASKQM; -.
DR OrthoDB; 1441797at2759; -.
DR TreeFam; TF300076; -.
DR Proteomes; UP000001595; Chromosome 16.
DR GO; GO:1904930; C:amphisome membrane; IEA:UniProt.
DR GO; GO:0000815; C:ESCRT III complex; IEA:InterPro.
DR GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR GO; GO:0005828; C:kinetochore microtubule; IEA:UniProt.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProt.
DR GO; GO:0030496; C:midbody; IEA:UniProt.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProt.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProt.
DR GO; GO:0097352; P:autophagosome maturation; IEA:UniProt.
DR GO; GO:1902774; P:late endosome to lysosome transport; IEA:UniProt.
DR GO; GO:0061952; P:midbody abscission; IEA:UniProt.
DR GO; GO:0007076; P:mitotic chromosome condensation; IEA:InterPro.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:UniProt.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:UniProt.
DR GO; GO:0031468; P:nuclear membrane reassembly; IEA:UniProt.
DR GO; GO:0001778; P:plasma membrane repair; IEA:UniProt.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IEA:UniProt.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:UniProt.
DR GO; GO:0046761; P:viral budding from plasma membrane; IEA:UniProt.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProt.
DR InterPro; IPR029888; CHMP1A.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR PANTHER; PTHR10476:SF17; PTHR10476:SF17; 1.
DR Pfam; PF03357; Snf7; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome;
KW Membrane; Nucleus; Phosphoprotein; Protein transport; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Transport.
FT CHAIN 1..196
FT /note="Charged multivesicular body protein 1a"
FT /id="PRO_0000211450"
FT REGION 173..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..47
FT /evidence="ECO:0000255"
FT COILED 102..124
FT /evidence="ECO:0000255"
FT MOTIF 185..195
FT /note="MIT-interacting motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD42"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD42"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HD42"
SQ SEQUENCE 196 AA; 21703 MW; 85D0ED7D10828D60 CRC64;
MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALLQK NVECARVYAE NAIRKKNEGV
NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL STMDLQKVSS VMDRFEQQVQ
NLDVHTSVME DSMSSATTLT TPQEQVDSLI MQIAEENGLE VLDQLSQLPE GASAVGESSV
RSQEDQLSRR LAALRN
