CHMP7_PONAB
ID CHMP7_PONAB Reviewed; 453 AA.
AC Q5R812;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Charged multivesicular body protein 7;
DE AltName: Full=Chromatin-modifying protein 7;
GN Name=CHMP7;
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: ESCRT-III-like protein required to recruit the ESCRT-III
CC complex to the nuclear envelope (NE) during late anaphase (By
CC similarity). Together with SPAST, the ESCRT-III complex promotes NE
CC sealing and mitotic spindle disassembly during late anaphase (By
CC similarity). Recruited to the reforming NE during anaphase by LEMD2 (By
CC similarity). Plays a role in the endosomal sorting pathway (By
CC similarity). {ECO:0000250|UniProtKB:Q8WUX9}.
CC -!- SUBUNIT: Interacts with CHMP4B, but not with VPS25 (By similarity).
CC Interacts with LEMD2 (via C-terminus) (By similarity).
CC {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 reforming nuclear envelope on chromatin disks during
CC late anaphase. {ECO:0000250|UniProtKB:Q8WUX9}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; CR859943; CAH92098.1; -; mRNA.
DR RefSeq; NP_001126224.1; NM_001132752.2.
DR AlphaFoldDB; Q5R812; -.
DR SMR; Q5R812; -.
DR STRING; 9601.ENSPPYP00000020659; -.
DR GeneID; 100173193; -.
DR KEGG; pon:100173193; -.
DR CTD; 91782; -.
DR eggNOG; KOG2911; Eukaryota.
DR InParanoid; Q5R812; -.
DR OrthoDB; 832779at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:1904930; C:amphisome membrane; IEA:UniProt.
DR GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
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:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProt.
DR GO; GO:0097352; P:autophagosome maturation; IEA:UniProt.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:1902774; P:late endosome to lysosome transport; IEA:UniProt.
DR GO; GO:0045324; P:late endosome to vacuole transport; ISS:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; IEA:UniProt.
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; ISS:UniProtKB.
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; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..453
FT /note="Charged multivesicular body protein 7"
FT /id="PRO_0000211518"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..312
FT /evidence="ECO:0000255"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R1T1"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WUX9"
SQ SEQUENCE 453 AA; 50764 MW; 947C7AAF824E0C89 CRC64;
MWSPEREAEA PAGGDPAGLL PPEWEEDEER MSFLFSAFKR SREVNSTDWD SKMGFWAPLV
LSHSRRQGVV RLRLRDLQEA FQRKGSVPLG LATVLQDLLR RGELQRESDF MASVDSSWIS
WGVGVFLLKP LKWTLSNMLG DNKVPAEEVL VAVELLKEKA EEVYRLYQSS PLSSHPVVAL
SELSTLCANS CPDERTFYLV LLQLQKEKRV TVLEQNGEKI VKFARGPHAK VSPVNDVDVG
VYQLMQSEQL LSRKVESLSQ EAERCKEEAR RACRAGKKQL ALRSLKAKQR TEKRIEALHA
KLDTVQGILD RIYASQTDQM VFNAYQAGVG ALKLSMKDVT VEKAESLVDQ IQELCDTQDE
VSQTLAGGVT NGLDFDSEEL EKELDILLQD TTKEPLDLPD NPRDRHFTNS VPNPRISDAG
LEAELEKLSL SEGGLVPSGK SPKRQLEPTL KPL
