ID   CHM4C_HUMAN             Reviewed;         233 AA.
AC   Q96CF2; B2RBZ1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   28-JAN-2026, entry version 178.
DE   RecName: Full=Charged multivesicular body protein 4c;
DE   AltName: Full=Chromatin-modifying protein 4c;
DE            Short=CHMP4c;
DE   AltName: Full=SNF7 homolog associated with Alix 3;
DE   AltName: Full=SNF7-3 {ECO:0000303|PubMed:14583093};
DE            Short=hSnf7-3 {ECO:0000303|PubMed:14583093};
DE   AltName: Full=Vacuolar protein sorting-associated protein 32-3;
DE            Short=Vps32-3;
DE            Short=hVps32-3;
GN   Name=CHMP4C; Synonyms=SHAX3;
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], TISSUE SPECIFICITY, AND INTERACTION WITH
RP   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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH PDCD6IP.
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].
RC   TISSUE=Small intestine;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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   [6]
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   [7]
RP   FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, AND INTERACTION WITH CHMPC4A;
RP   CHMPC4B; 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   [8]
RP   FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, AND INTERACTION WITH CHMP2A;
RP   CHMP4A; CHMP4B; 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   [9]
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   [10]
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   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-210, AND MUTAGENESIS
RP   OF SER-210.
RX   PubMed=22422861; DOI=10.1126/science.1217180;
RA   Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.;
RT   "ESCRT-III governs the Aurora B-mediated abscission checkpoint through
RT   CHMP4C.";
RL   Science 336:220-225(2012).
RN   [12]
RP   FUNCTION.
RX   PubMed=24814515; DOI=10.1038/ncb2959;
RA   Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K.,
RA   Andersen J.S., Raiborg C., Stenmark H.;
RT   "ANCHR mediates Aurora-B-dependent abscission checkpoint control through
RT   retention of VPS4.";
RL   Nat. Cell Biol. 16:550-560(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 221-233 IN COMPLEX WITH PDCD6IP.
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). 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
CC       (PubMed:22422861, PubMed:24814515). ESCRT-III proteins are believed to
CC       mediate the necessary vesicle extrusion and/or membrane fission
CC       activities, possibly in conjunction with the AAA ATPase VPS4. Involved
CC       in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required
CC       for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413).
CC       {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570,
CC       ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:22422861,
CC       ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:24814515}.
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.
CC       {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570,
CC       ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093,
CC       ECO:0000269|PubMed:14678797, ECO:0000269|PubMed:18511562}.
CC   -!- INTERACTION:
CC       Q96CF2; Q8WUM4: PDCD6IP; NbExp=3; IntAct=EBI-1221015, EBI-310624;
CC       Q96CF2; P40818: USP8; NbExp=2; IntAct=EBI-1221015, EBI-1050865;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane
CC       {ECO:0000305|PubMed:14583093}; Peripheral membrane protein
CC       {ECO:0000305}. Midbody, Midbody ring {ECO:0000269|PubMed:22422861}.
CC       Note=Localizes to the midbody during late cytokinesis. During its
CC       recruitment, localizes initially to the midbody arms, before being
CC       directed to the central region, the midbody ring, also called Flemming
CC       body. Phosphorylation at Ser-210 by AURKB triggers localization to
CC       midbody ring. {ECO:0000269|PubMed:22422861}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, spleen and kidney.
CC       {ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797}.
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:0000269|PubMed:22422861}.
CC   -!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
CC   -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR   EMBL; AB120734; BAC87888.1; -; mRNA.
DR   EMBL; AY329086; AAQ91195.1; -; mRNA.
DR   EMBL; AK314873; BAG37388.1; -; mRNA.
DR   EMBL; CH471068; EAW87107.1; -; Genomic_DNA.
DR   EMBL; BC014321; AAH14321.1; -; mRNA.
DR   CCDS; CCDS6233.1; -.
DR   RefSeq; NP_689497.1; NM_152284.4.
DR   PDB; 3C3R; X-ray; 2.02 A; B=221-233.
DR   PDB; 5MK3; X-ray; 2.00 A; E/F/G/H=216-233.
DR   PDB; 5V3R; X-ray; 1.91 A; B=216-233.
DR   PDB; 5WA1; X-ray; 1.87 A; B=216-233.
DR   PDBsum; 3C3R; -.
DR   PDBsum; 5MK3; -.
DR   PDBsum; 5V3R; -.
DR   PDBsum; 5WA1; -.
DR   AlphaFoldDB; Q96CF2; -.
DR   SMR; Q96CF2; -.
DR   BioGRID; 124946; 687.
DR   ComplexPortal; CPX-329; ESCRT-III complex.
DR   CORUM; Q96CF2; -.
DR   DIP; DIP-38342N; -.
DR   FunCoup; Q96CF2; 984.
DR   IntAct; Q96CF2; 17.
DR   MINT; Q96CF2; -.
DR   STRING; 9606.ENSP00000297265; -.
DR   GlyGen; Q96CF2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96CF2; -.
DR   PhosphoSitePlus; Q96CF2; -.
DR   BioMuta; CHMP4C; -.
DR   DMDM; 73917755; -.
DR   jPOST; Q96CF2; -.
DR   MassIVE; Q96CF2; -.
DR   PaxDb; 9606-ENSP00000297265; -.
DR   PeptideAtlas; Q96CF2; -.
DR   ProteomicsDB; 76183; -.
DR   Pumba; Q96CF2; -.
DR   Antibodypedia; 12567; 71 antibodies from 17 providers.
DR   DNASU; 92421; -.
DR   Ensembl; ENST00000297265.5; ENSP00000297265.4; ENSG00000164695.5.
DR   GeneID; 92421; -.
DR   KEGG; hsa:92421; -.
DR   MANE-Select; ENST00000297265.5; ENSP00000297265.4; NM_152284.4; NP_689497.1.
DR   UCSC; uc003ycl.4; human.
DR   AGR; HGNC:30599; -.
DR   ClinPGx; PA142672113; -.
DR   CTD; 92421; -.
DR   DisGeNET; 92421; -.
DR   GeneCards; CHMP4C; -.
DR   HGNC; HGNC:30599; CHMP4C.
DR   HPA; ENSG00000164695; Tissue enhanced (intestine).
DR   MIM; 610899; gene.
DR   OpenTargets; ENSG00000164695; -.
DR   VEuPathDB; HostDB:ENSG00000164695; -.
DR   eggNOG; KOG1656; Eukaryota.
DR   GeneTree; ENSGT00940000159257; -.
DR   HOGENOM; CLU_071097_0_1_1; -.
DR   InParanoid; Q96CF2; -.
DR   OMA; DKIDDMM; -.
DR   OrthoDB; 5592979at2759; -.
DR   PAN-GO; Q96CF2; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; Q96CF2; -.
DR   PathwayCommons; Q96CF2; -.
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; Q96CF2; -.
DR   SIGNOR; Q96CF2; -.
DR   Agora; ENSG00000164695; -.
DR   BioGRID-ORCS; 92421; 17 hits in 1155 CRISPR screens.
DR   EvolutionaryTrace; Q96CF2; -.
DR   GeneWiki; CHMP4C; -.
DR   GenomeRNAi; 92421; -.
DR   Pharos; Q96CF2; Tbio.
DR   PRO; PR:Q96CF2; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q96CF2; protein.
DR   Bgee; ENSG00000164695; Expressed in amniotic fluid and 138 other cell types or tissues.
DR   GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR   GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000815; C:ESCRT III complex; IBA:GO_Central.
DR   GO; GO:0090543; C:Flemming body; 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: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:0005886; C:plasma membrane; IDA:ComplexPortal.
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; NAS:ComplexPortal.
DR   GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR   GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; 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; NAS:ComplexPortal.
DR   GO; GO:0032466; P:negative regulation of cytokinesis; 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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR   GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR   GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR   GO; GO:0051469; P:vesicle fusion with vacuole; NAS: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:ComplexPortal.
DR   FunFam; 1.10.287.1060:FF:000001; Charged multivesicular body protein 4b; 1.
DR   Gene3D; 6.10.250.1710; -; 1.
DR   Gene3D; 1.10.287.1060; ESAT-6-like; 1.
DR   InterPro; IPR005024; Snf7_fam.
DR   PANTHER; PTHR22761; CHARGED MULTIVESICULAR BODY PROTEIN; 1.
DR   PANTHER; PTHR22761:SF77; CHARGED MULTIVESICULAR BODY PROTEIN 4C; 1.
DR   Pfam; PF03357; Snf7; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Proteomics identification; Reference proteome;
KW   Transport.
FT   CHAIN           1..233
FT                   /note="Charged multivesicular body protein 4c"
FT                   /id="PRO_0000211495"
FT   REGION          1..153
FT                   /note="Intramolecular interaction with C-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..233
FT                   /note="Intramolecular interaction with N-terminus"
FT                   /evidence="ECO:0000250"
FT   REGION          173..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          125..183
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        204..216
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         210
FT                   /note="Phosphoserine; by AURKB"
FT                   /evidence="ECO:0000269|PubMed:22422861"
FT   VARIANT         232
FT                   /note="A -> T (in dbSNP:rs35094336)"
FT                   /id="VAR_052028"
FT   MUTAGEN         210
FT                   /note="S->A: Abolishes localization to the Flemming body
FT                   and ability to delay abscission."
FT                   /evidence="ECO:0000269|PubMed:22422861"
FT   HELIX           222..229
FT                   /evidence="ECO:0007829|PDB:5WA1"
SQ   SEQUENCE   233 AA;  26411 MW;  C18050F0A6C4C899 CRC64;
     MSKLGKFFKG GGSSKSRAAP SPQEALVRLR ETEEMLGKKQ EYLENRIQRE IALAKKHGTQ
     NKRAALQALK RKKRFEKQLT QIDGTLSTIE FQREALENSH TNTEVLRNMG FAAKAMKSVH
     ENMDLNKIDD LMQEITEQQD IAQEISEAFS QRVGFGDDFD EDELMAELEE LEQEELNKKM
     TNIRLPNVPS SSLPAQPNRK PGMSSTARRS RAASSQRAEE EDDDIKQLAA WAT
//