CHMP7_SCHPO
ID CHMP7_SCHPO Reviewed; 449 AA.
AC O94730;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Charged multivesicular body protein 7 {ECO:0000305};
DE Short=Chmp7 {ECO:0000305};
DE AltName: Full=ESCRT III complex subunit Cmp7 {ECO:0000303|PubMed:28242692};
DE Short=Cmp7 {ECO:0000303|PubMed:28242692};
GN Name=cmp7 {ECO:0000312|PomBase:SPBC1604.18c};
GN ORFNames=SPBC1604.18c {ECO:0000312|PomBase:SPBC1604.18c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28242692; DOI=10.1073/pnas.1613916114;
RA Gu M., LaJoie D., Chen O.S., von Appen A., Ladinsky M.S., Redd M.J.,
RA Nikolova L., Bjorkman P.J., Sundquist W.I., Ullman K.S., Frost A.;
RT "LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission
RT yeast and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2166-E2175(2017).
CC -!- FUNCTION: ESCRT-III-like protein required to recruit the ESCRT-III
CC complex to the nuclear envelope during late anaphase (By similarity).
CC Plays a role in regulating nuclear envelope (NE) morphology and nuclear
CC integrity, particularly during spindle pole body (SPB) extrusion or
CC insertion through the NE, and perhaps during karyokinesis
CC (PubMed:28242692). {ECO:0000250|UniProtKB:Q8WUX9,
CC ECO:0000269|PubMed:28242692}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Suppresses slow growth rates of spores and severe
CC nuclear envelope (NE) morphology defects of vps4 mutants.
CC {ECO:0000269|PubMed:28242692}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA22351.1; -; Genomic_DNA.
DR PIR; T39496; T39496.
DR RefSeq; NP_596622.1; NM_001022543.2.
DR AlphaFoldDB; O94730; -.
DR SMR; O94730; -.
DR BioGRID; 276527; 2.
DR STRING; 4896.SPBC1604.18c.1; -.
DR iPTMnet; O94730; -.
DR MaxQB; O94730; -.
DR PaxDb; O94730; -.
DR PRIDE; O94730; -.
DR EnsemblFungi; SPBC1604.18c.1; SPBC1604.18c.1:pep; SPBC1604.18c.
DR GeneID; 2539983; -.
DR KEGG; spo:SPBC1604.18c; -.
DR PomBase; SPBC1604.18c; -.
DR VEuPathDB; FungiDB:SPBC1604.18c; -.
DR eggNOG; KOG2911; Eukaryota.
DR HOGENOM; CLU_021165_2_0_1; -.
DR InParanoid; O94730; -.
DR OMA; NEQMATT; -.
DR PhylomeDB; O94730; -.
DR PRO; PR:O94730; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000815; C:ESCRT III complex; ISM:PomBase.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0007084; P:mitotic nuclear membrane reassembly; IMP:PomBase.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..449
FT /note="Charged multivesicular body protein 7"
FT /id="PRO_0000303922"
FT REGION 421..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 50788 MW; 246DC90598A566D5 CRC64;
MGKKEKVNAL EFSVNKGIFT KTRLKSLYSD FTSLFIKNPE GFLANVNTWR EAIETSAWSG
KLNSRIILVF DETFESAFSS PALGRPLSLG AVAAYWIQQG VWLRKQDFLN DCKKGNLVRE
DGFSIFSILR WSFQKLGFQN QASSILSNRS PSGQYVIRKN IEKLACLVHN EAMRRCSSYT
SAIYTWDFFQ DTFGSLYWEE GKLNKDEMEC LLNWMCYQKH VLIFDSKIIK FLPNSQIDAQ
LASIDKSIDG SVADLIQARA SIAQRSEFLN EELEQLSQVL NQAVKKGEKT IAITYLRRKK
ILSKDLERKV SSRLQLDTII SNIDNAVDNK ILLIAMSSGS EALDAILAQM GGTEKVEDVL
ENVNDTLARS EEIDATIQTY NPQNIDLEDE AVEKEWQDLV AEEQKVEDIV STLGNVSLKT
PSDTFTLTNT DSDKKTSKPE KIQAELVEQ
