CHM2B_BOVIN
ID CHM2B_BOVIN Reviewed; 213 AA.
AC Q3SX42;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Charged multivesicular body protein 2b;
DE AltName: Full=Chromatin-modifying protein 2b;
DE Short=CHMP2b;
GN Name=CHMP2B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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. The MVB pathway appears to require the sequential function
CC of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC dissociate from the invaginating membrane before the ILV is released.
CC The ESCRT machinery also functions in topologically equivalent membrane
CC fission events, such as the terminal stages of cytokinesis and the
CC budding of enveloped viruses (lentiviruses). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or membrane
CC fission activities, possibly in conjunction with the AAA ATPase VPS4
CC (By similarity). {ECO:0000250}.
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. Several assembly forms of ESCRT-III may exist that interact
CC and act sequentially. Interacts with CHMP2A. Interacts with VPS4A.
CC Interacts with VPS4B; the interaction is direct (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Late endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; BC104514; AAI04515.1; -; mRNA.
DR RefSeq; NP_001030549.1; NM_001035472.1.
DR AlphaFoldDB; Q3SX42; -.
DR SMR; Q3SX42; -.
DR STRING; 9913.ENSBTAP00000010436; -.
DR PaxDb; Q3SX42; -.
DR PRIDE; Q3SX42; -.
DR Ensembl; ENSBTAT00000010436; ENSBTAP00000010436; ENSBTAG00000007939.
DR GeneID; 615954; -.
DR KEGG; bta:615954; -.
DR CTD; 25978; -.
DR VEuPathDB; HostDB:ENSBTAG00000007939; -.
DR VGNC; VGNC:27301; CHMP2B.
DR eggNOG; KOG3231; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_069208_1_2_1; -.
DR InParanoid; Q3SX42; -.
DR OMA; NMREFQM; -.
DR OrthoDB; 1480977at2759; -.
DR TreeFam; TF314163; -.
DR Reactome; R-BTA-1632852; Macroautophagy.
DR Reactome; R-BTA-5620971; Pyroptosis.
DR Reactome; R-BTA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000007939; Expressed in rumen papilla and 104 other tissues.
DR GO; GO:1904930; C:amphisome membrane; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
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:Ensembl.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
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:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
DR GO; GO:0050890; P:cognition; IEA:Ensembl.
DR GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:1902774; P:late endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0061952; P:midbody abscission; IEA:Ensembl.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IEA:Ensembl.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; 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; IBA:GO_Central.
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: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; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UQN3"
FT CHAIN 2..213
FT /note="Charged multivesicular body protein 2b"
FT /id="PRO_0000211468"
FT REGION 178..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 25..55
FT /evidence="ECO:0000255"
FT MOTIF 201..211
FT /note="MIT-interacting motif"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQN3"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQN3"
SQ SEQUENCE 213 AA; 23951 MW; AC45410D59E4489B CRC64;
MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACRV
LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK
TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK
APSAARSLPS ASTSKSTISD EEIERQLKAL GVD
