DID4_SCHPO
ID DID4_SCHPO Reviewed; 210 AA.
AC O14177; Q9P6Q7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=ESCRT-III complex subunit did4;
DE AltName: Full=Vacuolar protein-sorting-associated protein 2;
GN Name=did4; Synonyms=vps2; ORFNames=SPAC4F8.01, SPAC644.03c;
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 DISRUPTION PHENOTYPE.
RX PubMed=17660439; DOI=10.1099/mic.0.2007/006072-0;
RA Iwaki T., Onishi M., Ikeuchi M., Kita A., Sugiura R., Giga-Hama Y.,
RA Fukui Y., Takegawa K.;
RT "Essential roles of class E Vps proteins for sorting into multivesicular
RT bodies in Schizosaccharomyces pombe.";
RL Microbiology 153:2753-2764(2007).
CC -!- FUNCTION: Required for the sorting and concentration of proteins
CC resulting in the entry of these proteins into the invaginating vesicles
CC of the multivesicular body (MVB). Acts a component of the ESCRT-III
CC complex, which appears to be critical for late steps in MVB sorting,
CC such as membrane invagination and final cargo sorting and recruitment
CC of late-acting components of the sorting machinery. The MVB pathway
CC requires the sequential function of ESCRT-O, -I,-II and -III complex
CC assemblies (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Core component of the ESCRT-III complex (endosomal sorting
CC required for transport complex III). ESCRT-III appears to be
CC sequentially assembled as a flat lattice on the endosome membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Leads to multivesicular bodies sorting defects.
CC {ECO:0000269|PubMed:17660439}.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11048.2; -; Genomic_DNA.
DR PIR; T38831; T38831.
DR RefSeq; NP_593871.3; NM_001019300.3.
DR AlphaFoldDB; O14177; -.
DR SMR; O14177; -.
DR BioGRID; 279939; 10.
DR STRING; 4896.SPAC4F8.01.1; -.
DR MaxQB; O14177; -.
DR PaxDb; O14177; -.
DR PRIDE; O14177; -.
DR EnsemblFungi; SPAC4F8.01.1; SPAC4F8.01.1:pep; SPAC4F8.01.
DR GeneID; 2543521; -.
DR KEGG; spo:SPAC4F8.01; -.
DR PomBase; SPAC4F8.01; did4.
DR VEuPathDB; FungiDB:SPAC4F8.01; -.
DR eggNOG; KOG3230; Eukaryota.
DR HOGENOM; CLU_069208_1_0_1; -.
DR InParanoid; O14177; -.
DR OMA; RYAKKFM; -.
DR PhylomeDB; O14177; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-SPO-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR PRO; PR:O14177; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000815; C:ESCRT III complex; ISO:PomBase.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
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; IMP:PomBase.
DR GO; GO:0006998; P:nuclear envelope organization; ISS:PomBase.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; ISO:PomBase.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:PomBase.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 3: Inferred from homology;
KW Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..210
FT /note="ESCRT-III complex subunit did4"
FT /id="PRO_0000116658"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 15..97
FT /evidence="ECO:0000255"
FT COMPBIAS 22..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 210 AA; 23928 MW; 02974A04321AE1A4 CRC64;
MGLTSWLFGG GKSPQEQLRA HQRSLGRAER ELDRERTKLD QRERALIQEI KGSAKAGNTG
AARIQARDLM RLRNSRKKMM NAKTQLQAIS LRLQTMRTSE QMMQSMRGAT RLLTGMNKSM
NIPAMARITQ QFERENEIME QRQEMIDENM DDALEEDDEE EADELVNKVL DEIGVDLSQG
LPDAATQIGT VPELKTEDNL QARLDELAKR
