CHM4A_HUMAN
ID CHM4A_HUMAN Reviewed; 222 AA.
AC Q9BY43; Q14D22; Q32Q79; Q86SZ8; Q96QJ9; Q9P026;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Charged multivesicular body protein 4a;
DE AltName: Full=Chromatin-modifying protein 4a;
DE Short=CHMP4a;
DE AltName: Full=SNF7 homolog associated with Alix-2;
DE AltName: Full=SNF7-1;
DE Short=hSnf-1;
DE AltName: Full=Vacuolar protein sorting-associated protein 32-1;
DE Short=Vps32-1;
DE Short=hVps32-1;
GN Name=CHMP4A; Synonyms=C14orf123, SHAX2; ORFNames=CDA04, HSPC134;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PDCD6IP.
RC TISSUE=Cervix;
RX PubMed=12860994; DOI=10.1074/jbc.m301604200;
RA Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E.,
RA Yoshimori T., Maki M.;
RT "The ALG-2-interacting protein Alix associates with CHMP4b, a human
RT homologue of yeast Snf7 that is involved in multivesicular body sorting.";
RL J. Biol. Chem. 278:39104-39113(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-153, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6IP.
RC TISSUE=Squamous cell carcinoma;
RX PubMed=14583093; DOI=10.1042/bj20031347;
RA Peck J.W., Bowden E.T., Burbelo P.D.;
RT "Structure and function of human Vps20 and Snf7 proteins.";
RL Biochem. J. 377:693-700(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pheochromocytoma;
RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=B-cell;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ARG-153.
RC TISSUE=Brain, and Prostate;
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).
RN [8]
RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH PDCD6IP.
RX PubMed=14505569; DOI=10.1016/s0092-8674(03)00653-6;
RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in
RT virus budding.";
RL Cell 114:689-699(2003).
RN [9]
RP INTERACTION WITH CHMP4C; VPS4A AND PDCD6IP.
RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1;
RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
RT "The protein network of HIV budding.";
RL Cell 114:701-713(2003).
RN [10]
RP FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, AND INTERACTION WITH CHMP2A;
RP CHMP4B; CHMP4C; CHMP6 AND PDCD6IP.
RX PubMed=14519844; DOI=10.1073/pnas.2133846100;
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RT "Divergent retroviral late-budding domains recruit vacuolar protein sorting
RT factors by using alternative adaptor proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
RN [11]
RP ERRATUM OF PUBMED:14519844.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [12]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PDCD6IP.
RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
RA Katoh K., Shibata H., Hatta K., Maki M.;
RT "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix
RT among the three CHMP4 isoforms.";
RL Arch. Biochem. Biophys. 421:159-165(2004).
RN [13]
RP SUBCELLULAR LOCATION, AND LIPID-BINDING.
RX PubMed=15632132; DOI=10.1074/jbc.m413968200;
RA Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.;
RT "Interaction of the mammalian endosomal sorting complex required for
RT transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+
RT ATPase SKD1.";
RL J. Biol. Chem. 280:12799-12809(2005).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K.,
RA Sundquist W.I.;
RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and
RT function in cytokinesis.";
RL EMBO J. 26:4215-4227(2007).
RN [15]
RP AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP3, AND MUTAGENESIS OF
RP 182-ASP--SER-222.
RX PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x;
RA Shim S., Kimpler L.A., Hanson P.I.;
RT "Structure/function analysis of four core ESCRT-III proteins reveals common
RT regulatory role for extreme C-terminal domain.";
RL Traffic 8:1068-1079(2007).
RN [16]
RP FUNCTION, SELF-ASSOCIATION, AND STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=18209100; DOI=10.1083/jcb.200707031;
RA Hanson P.I., Roth R., Lin Y., Heuser J.E.;
RT "Plasma membrane deformation by circular arrays of ESCRT-III protein
RT filaments.";
RL J. Cell Biol. 180:389-402(2008).
RN [17]
RP FUNCTION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 210-222 IN COMPLEX WITH PDCD6IP,
RP AND MUTAGENESIS OF GLU-209; LEU-214; LEU-217 AND TRP-220.
RX PubMed=18511562; DOI=10.1073/pnas.0801567105;
RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
RT "ALIX-CHMP4 interactions in the human ESCRT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
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 (HIV-1 and other lentiviruses). 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. When overexpressed, membrane-assembled circular arrays of
CC CHMP4A filaments can promote or stabilize negative curvature and
CC outward budding. Via its interaction with PDCD6IP involved in HIV-1
CC p6- and p9-dependent virus release. CHMP4A/B/C are required for the
CC exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).
CC {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569,
CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093,
CC ECO:0000269|PubMed:18209100, ECO:0000269|PubMed:22660413}.
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; overexpression leads to the
CC assembly of filaments that curve and associate to create circular
CC rings. Interacts with CHMP2A. Interacts with CHMP3; the interaction
CC requires the release of CHMP4A autoinhibition. Interacts with CHMP4B.
CC Interacts with CHMP4C. Interacts with CHMP6. Interacts with VPS4A.
CC Interacts with PDCD6IP; the interaction is direct.
CC {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569,
CC ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
CC ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797,
CC ECO:0000269|PubMed:17547705, ECO:0000269|PubMed:18511562}.
CC -!- INTERACTION:
CC Q9BY43; Q9H444: CHMP4B; NbExp=4; IntAct=EBI-747981, EBI-749627;
CC Q9BY43; Q8WUM4: PDCD6IP; NbExp=3; IntAct=EBI-747981, EBI-310624;
CC Q9BY43; Q9BSW7: SYT17; NbExp=6; IntAct=EBI-747981, EBI-745392;
CC Q9BY43-2; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-12178895, EBI-749627;
CC Q9BY43-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12178895, EBI-741158;
CC Q9BY43-2; P61970: NUTF2; NbExp=3; IntAct=EBI-12178895, EBI-591778;
CC Q9BY43-2; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-12178895, EBI-745392;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Late endosome
CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC Note=Membrane-associated. Localizes to large vesicle-like structures.
CC Localizes to the midbody of dividing cells. Localized in two distinct
CC rings on either side of the Fleming body.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BY43-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BY43-2; Sequence=VSP_056264;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC heart, kidney, liver and skeletal muscle. Also expressed in brain,
CC placenta, lung and pancreas. {ECO:0000269|PubMed:14678797}.
CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus 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 -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH10893.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI07700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD61949.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB100262; BAC79376.2; -; mRNA.
DR EMBL; AY329084; AAQ91193.1; -; mRNA.
DR EMBL; AF212243; AAK14928.1; -; mRNA.
DR EMBL; AF161483; AAF29098.1; -; mRNA.
DR EMBL; BX161512; CAD61949.1; ALT_INIT; mRNA.
DR EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010893; AAH10893.2; ALT_INIT; mRNA.
DR EMBL; BC107699; AAI07700.1; ALT_INIT; mRNA.
DR EMBL; BC113533; AAI13534.1; -; mRNA.
DR EMBL; BC113535; AAI13536.1; -; mRNA.
DR CCDS; CCDS9619.1; -. [Q9BY43-1]
DR RefSeq; NP_054888.2; NM_014169.3. [Q9BY43-1]
DR PDB; 3C3O; X-ray; 2.15 A; B=210-222.
DR PDB; 5MK1; X-ray; 2.50 A; E/F/H/K=205-222.
DR PDBsum; 3C3O; -.
DR PDBsum; 5MK1; -.
DR AlphaFoldDB; Q9BY43; -.
DR SMR; Q9BY43; -.
DR BioGRID; 118852; 66.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q9BY43; -.
DR DIP; DIP-39082N; -.
DR IntAct; Q9BY43; 25.
DR MINT; Q9BY43; -.
DR STRING; 9606.ENSP00000324205; -.
DR iPTMnet; Q9BY43; -.
DR PhosphoSitePlus; Q9BY43; -.
DR BioMuta; CHMP4A; -.
DR DMDM; 90152096; -.
DR EPD; Q9BY43; -.
DR jPOST; Q9BY43; -.
DR MassIVE; Q9BY43; -.
DR MaxQB; Q9BY43; -.
DR PaxDb; Q9BY43; -.
DR PeptideAtlas; Q9BY43; -.
DR PRIDE; Q9BY43; -.
DR ProteomicsDB; 60344; -.
DR ProteomicsDB; 79580; -. [Q9BY43-1]
DR Antibodypedia; 56042; 39 antibodies from 15 providers.
DR DNASU; 29082; -.
DR Ensembl; ENST00000347519.12; ENSP00000324205.11; ENSG00000254505.11. [Q9BY43-1]
DR Ensembl; ENST00000645308.4; ENSP00000495982.2; ENSG00000285302.5. [Q9BY43-1]
DR GeneID; 29082; -.
DR KEGG; hsa:29082; -.
DR MANE-Select; ENST00000347519.12; ENSP00000324205.11; NM_014169.5; NP_054888.3.
DR UCSC; uc001wni.4; human. [Q9BY43-1]
DR CTD; 29082; -.
DR DisGeNET; 29082; -.
DR GeneCards; CHMP4A; -.
DR HGNC; HGNC:20274; CHMP4A.
DR HPA; ENSG00000254505; Low tissue specificity.
DR MIM; 610051; gene.
DR neXtProt; NX_Q9BY43; -.
DR OpenTargets; ENSG00000254505; -.
DR PharmGKB; PA134888743; -.
DR VEuPathDB; HostDB:ENSG00000254505; -.
DR eggNOG; KOG1656; Eukaryota.
DR GeneTree; ENSGT00940000163323; -.
DR HOGENOM; CLU_071097_0_1_1; -.
DR InParanoid; Q9BY43; -.
DR OMA; EHKIQQE; -.
DR OrthoDB; 1490465at2759; -.
DR PhylomeDB; Q9BY43; -.
DR TreeFam; TF314269; -.
DR PathwayCommons; Q9BY43; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR SignaLink; Q9BY43; -.
DR SIGNOR; Q9BY43; -.
DR BioGRID-ORCS; 29082; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; CHMP4A; human.
DR EvolutionaryTrace; Q9BY43; -.
DR GeneWiki; CHMP4A; -.
DR GenomeRNAi; 29082; -.
DR Pharos; Q9BY43; Tbio.
DR PRO; PR:Q9BY43; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BY43; protein.
DR Bgee; ENSG00000254505; Expressed in popliteal artery and 98 other tissues.
DR ExpressionAtlas; Q9BY43; baseline and differential.
DR Genevisible; Q9BY43; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IDA:ComplexPortal.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:ComplexPortal.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ComplexPortal.
DR GO; GO:0030117; C:membrane coat; IMP:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0010324; P:membrane invagination; IMP:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0061763; P:multivesicular body-lysosome fusion; IC:ComplexPortal.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:ComplexPortal.
DR GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IMP:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IDA:ComplexPortal.
DR GO; GO:0097320; P:plasma membrane tubulation; IMP:UniProtKB.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:ComplexPortal.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0006900; P:vesicle budding from membrane; IMP:UniProtKB.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC:ComplexPortal.
DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:ComplexPortal.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW Endosome; Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..222
FT /note="Charged multivesicular body protein 4a"
FT /id="PRO_0000211488"
FT REGION 1..150
FT /note="Intramolecular interaction with C-terminus"
FT /evidence="ECO:0000250"
FT REGION 1..116
FT /note="Interaction with phosphoinosides"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..222
FT /note="Intramolecular interaction with N-terminus"
FT /evidence="ECO:0000250"
FT REGION 180..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..105
FT /evidence="ECO:0000255"
FT COILED 155..180
FT /evidence="ECO:0000255"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MSRRRPEDGLGKAGPCVMRHHPPRSKAEVWRTLRGGGGRGELAM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056264"
FT VARIANT 153
FT /note="G -> R (in dbSNP:rs2295322)"
FT /evidence="ECO:0000269|PubMed:14583093,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023384"
FT MUTAGEN 182..222
FT /note="Missing: Membrane association; releases
FT autoinhibition."
FT /evidence="ECO:0000269|PubMed:17547705"
FT MUTAGEN 209
FT /note="E->A: Reduces interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18511562"
FT MUTAGEN 214
FT /note="L->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18511562"
FT MUTAGEN 217
FT /note="L->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18511562"
FT MUTAGEN 220
FT /note="W->A: Abolishes interaction with PDCD6IP."
FT /evidence="ECO:0000269|PubMed:18511562"
FT CONFLICT 16
FT /note="G -> R (in Ref. 4; AAF29098)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="L -> S (in Ref. 4; AAF29098)"
FT /evidence="ECO:0000305"
FT CONFLICT 152..153
FT /note="FG -> LLE (in Ref. 4; AAF29098)"
FT /evidence="ECO:0000305"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:3C3O"
SQ SEQUENCE 222 AA; 25098 MW; 6712BA6AAA1D7CB7 CRC64;
MSGLGRLFGK GKKEKGPTPE EAIQKLKETE KILIKKQEFL EQKIQQELQT AKKYGTKNKR
AALQALRRKK RFEQQLAQTD GTLSTLEFQR EAIENATTNA EVLRTMELAA QSMKKAYQDM
DIDKVDELMT DITEQQEVAQ QISDAISRPM GFGDDVDEDE LLEELEELEQ EELAQELLNV
GDKEEEPSVK LPSVPSTHLP AGPAPKVDED EEALKQLAEW VS
