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CHM1B_BOVIN
ID   CHM1B_BOVIN             Reviewed;         199 AA.
AC   Q5E994; Q2KJ31;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Charged multivesicular body protein 1b;
DE   AltName: Full=Chromatin-modifying protein 1b;
DE            Short=CHMP1b;
GN   Name=CHMP1B;
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) 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 and SPAST to the
CC       midbody of dividing cells (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. Interacts with CHMP1A.
CC       Interacts with VTA1; the interaction probably involves the open
CC       conformation of CHMP1B. Interacts with CHMP2A. Interacts with VPS4A;
CC       the interaction is direct. Interacts with VPS4B; the interaction is
CC       direct. Interacts with SPAST (via MIT domain); the interaction is
CC       direct. Interacts with IST1. Interacts with MITD1. Interacts with
CC       STAMBP (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Endosome
CC       {ECO:0000250}. Late endosome membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}. Note=Localizes to the midbody of
CC       dividing cells, colocalizing with CEP55 and CHMP5. Localized at the
CC       periphery of the Fleming body (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BT021026; AAX09043.1; -; mRNA.
DR   EMBL; BC105547; AAI05548.2; -; mRNA.
DR   RefSeq; NP_001014904.1; NM_001014904.1.
DR   AlphaFoldDB; Q5E994; -.
DR   SMR; Q5E994; -.
DR   PRIDE; Q5E994; -.
DR   GeneID; 512033; -.
DR   KEGG; bta:512033; -.
DR   CTD; 57132; -.
DR   InParanoid; Q5E994; -.
DR   OrthoDB; 1441797at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR10476; PTHR10476; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..199
FT                   /note="Charged multivesicular body protein 1b"
FT                   /id="PRO_0000211453"
FT   REGION          132..156
FT                   /note="Interaction with IST1"
FT                   /evidence="ECO:0000250"
FT   REGION          167..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          174..199
FT                   /note="Interaction with SPAST"
FT                   /evidence="ECO:0000250"
FT   REGION          180..199
FT                   /note="Interaction with VTA1"
FT                   /evidence="ECO:0000250"
FT   REGION          180..196
FT                   /note="Interaction with VPS4A, MITD1 and STAMBP"
FT                   /evidence="ECO:0000250"
FT   REGION          183..199
FT                   /note="Interaction with VPS4B"
FT                   /evidence="ECO:0000250"
FT   COILED          26..48
FT                   /evidence="ECO:0000255"
FT   COILED          178..199
FT                   /evidence="ECO:0000255"
FT   MOTIF           186..196
FT                   /note="MIT-interacting motif"
FT   COMPBIAS        168..186
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   199 AA;  22022 MW;  10A5E959205E8EAE CRC64;
     MSNMEKHLFN LKFAAKELGR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN
     QAVNFLRMSA RVDAVAARVQ TAVTMGKVTK SMAGVVKSMD ATLKTMNLEK ISALMDKFEH
     QFETLDVQTQ QMEDTMSSTT TLTTPQGQVD MLLQEMADEA GLDLNMELPQ GQTGSVGTSV
     ASAEQDELSQ RLARLRDQV
 
 
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