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CHM4C_RAT
ID   CHM4C_RAT               Reviewed;         232 AA.
AC   Q569C1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Charged multivesicular body protein 4c;
DE   AltName: Full=Chromatin-modifying protein 4c;
DE            Short=CHMP4c;
GN   Name=Chmp4c;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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. Key
CC       component of the cytokinesis checkpoint, a process required to delay
CC       abscission to prevent both premature resolution of intercellular
CC       chromosome bridges and accumulation of DNA damage: upon phosphorylation
CC       by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent
CC       VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC       checkpoint signaling is terminated at late cytokinesis. Deactivation of
CC       AURKB results in dephosphorylation of CHMP4C followed by its
CC       dissociation from ANCHR and VPS4 and subsequent abscission. ESCRT-III
CC       proteins are believed to mediate the necessary vesicle extrusion and/or
CC       membrane fission activities, possibly in conjunction with the AAA
CC       ATPase VPS4. CHMP4A/B/C are required for the exosomal release of SDCBP,
CC       CD63 and syndecan (By similarity). {ECO:0000250|UniProtKB:Q96CF2}.
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. Self-associates. Interacts with CHMP2A. Interacts
CC       with CHMP4A. Interacts with CHMP4B. Interacts with CHMP6. Interacts
CC       with VPS4A. Interacts with PDCD6IP; the interaction is direct (By
CC       similarity). {ECO:0000250|UniProtKB:Q96CF2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Late endosome
CC       membrane {ECO:0000250|UniProtKB:Q96CF2}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q96CF2}. Midbody, Midbody ring
CC       {ECO:0000250|UniProtKB:Q96CF2}. Note=Localizes to the midbody during
CC       late cytokinesis. During its recruitment, localizes initially to the
CC       midbody arms, before being directed to the central region, the midbody
CC       ring, also called Flemming body. Phosphorylation at Ser-210 by AURKB
CC       triggers localization to midbody ring. {ECO:0000250|UniProtKB:Q96CF2}.
CC   -!- DOMAIN: The acidic C-terminus and the basic N-terminus are thought to
CC       render the protein in a closed, soluble and inactive conformation
CC       through an autoinhibitory intramolecular interaction. The open and
CC       active conformation, which enables membrane binding and
CC       oligomerization, is achieved by interaction with other cellular binding
CC       partners, probably including other ESCRT components (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together
CC       with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent
CC       VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission
CC       checkpoint signaling is terminated at late cytokinesis.
CC       {ECO:0000250|UniProtKB:Q96CF2}.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; BC092576; AAH92576.1; -; mRNA.
DR   RefSeq; NP_001017466.2; NM_001017466.2.
DR   AlphaFoldDB; Q569C1; -.
DR   SMR; Q569C1; -.
DR   STRING; 10116.ENSRNOP00000013720; -.
DR   PaxDb; Q569C1; -.
DR   GeneID; 361916; -.
DR   KEGG; rno:361916; -.
DR   UCSC; RGD:1564543; rat.
DR   CTD; 92421; -.
DR   RGD; 1564543; Chmp4c.
DR   eggNOG; KOG1656; Eukaryota.
DR   InParanoid; Q569C1; -.
DR   OrthoDB; 1490465at2759; -.
DR   PhylomeDB; Q569C1; -.
DR   Reactome; R-RNO-1632852; Macroautophagy.
DR   Reactome; R-RNO-5620971; Pyroptosis.
DR   Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-RNO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR   PRO; PR:Q569C1; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:1904930; C:amphisome membrane; ISO:RGD.
DR   GO; GO:0000421; C:autophagosome membrane; ISO:RGD.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR   GO; GO:0090543; C:Flemming body; ISO:RGD.
DR   GO; GO:0000776; C:kinetochore; ISO:RGD.
DR   GO; GO:0005828; C:kinetochore microtubule; ISO:RGD.
DR   GO; GO:0005765; C:lysosomal membrane; ISO:RGD.
DR   GO; GO:0030496; C:midbody; ISO:RGD.
DR   GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR   GO; GO:0032585; C:multivesicular body membrane; ISO:RGD.
DR   GO; GO:0005643; C:nuclear pore; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0009838; P:abscission; ISS:UniProtKB.
DR   GO; GO:0097352; P:autophagosome maturation; ISO:RGD.
DR   GO; GO:0006914; P:autophagy; ISO:RGD.
DR   GO; GO:1902774; P:late endosome to lysosome transport; ISO:RGD.
DR   GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR   GO; GO:0061952; P:midbody abscission; ISO:RGD.
DR   GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; ISS:UniProtKB.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISO:RGD.
DR   GO; GO:0071985; P:multivesicular body sorting pathway; ISO:RGD.
DR   GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
DR   GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:0031468; P:nuclear membrane reassembly; ISO:RGD.
DR   GO; GO:0006997; P:nucleus organization; ISO:RGD.
DR   GO; GO:0001778; P:plasma membrane repair; ISO:RGD.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0010824; P:regulation of centrosome duplication; ISO:RGD.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:RGD.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISO:RGD.
DR   GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; ISO:RGD.
DR   GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR   GO; GO:0046761; P:viral budding from plasma membrane; ISO:RGD.
DR   GO; GO:0039702; P:viral budding via host ESCRT complex; ISO:RGD.
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.
FT   CHAIN           1..232
FT                   /note="Charged multivesicular body protein 4c"
FT                   /id="PRO_0000211497"
FT   REGION          1..153
FT                   /note="Intramolecular interaction with C-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..232
FT                   /note="Intramolecular interaction with N-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          172..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          21..50
FT                   /evidence="ECO:0000255"
FT   COILED          125..182
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        183..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         210
FT                   /note="Phosphoserine; by AURKB"
FT                   /evidence="ECO:0000250|UniProtKB:Q96CF2"
SQ   SEQUENCE   232 AA;  26324 MW;  CE924438BF9264AE CRC64;
     MSKLGKFFKG SRSSRARAAP SAQEALARLR EIEEMMAKKQ EYLENRIQRE LALAKKHGSQ
     NKRAALQALK RKKRFEKQLT QIDGTLSTIE FQREALENSH TNTEVLRNMG FAAKAMKAVH
     ENMDLNKIDD LMQDITEQQD IAQEISEAFS QRVQFADGFD EDELLAELEE LEQEELNKKM
     TSMELPNVPS SSLPAQPSRK AGVPSSVHRS RAASSRRAEE DDDFKQLAAW AT
 
 
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