SST6_SCHPO
ID SST6_SCHPO Reviewed; 487 AA.
AC Q7Z992;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=ESCRT-I complex subunit vps23;
DE AltName: Full=Suppressor of ste12 deletion protein 6;
GN Name=sst6; Synonyms=cps23, vps23; ORFNames=SPAC11H11.01;
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 FUNCTION.
RX PubMed=12951513; DOI=10.1271/bbb.67.1772;
RA Onishi M., Nakamura Y., Koga T., Takegawa K., Fukui Y.;
RT "Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-
RT kinase deficient cells in Schizosaccharomyces pombe.";
RL Biosci. Biotechnol. Biochem. 67:1772-1779(2003).
RN [3]
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 [4]
RP FUNCTION.
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: Component of the ESCRT-I complex, a regulator of vesicular
CC trafficking process. Binds to ubiquitinated cargo proteins and is
CC required for the sorting of endocytic ubiquitinated cargos into
CC multivesicular bodies (MVBs). Mediates the association to the ESCRT-0
CC complex (By similarity). {ECO:0000250, ECO:0000269|PubMed:12951513,
CC ECO:0000269|PubMed:17660439}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Endosome
CC {ECO:0000269|PubMed:16823372}. Late endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
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DR EMBL; CU329670; CAD99129.2; -; Genomic_DNA.
DR RefSeq; NP_001018287.1; NM_001020147.2.
DR AlphaFoldDB; Q7Z992; -.
DR SMR; Q7Z992; -.
DR BioGRID; 280537; 26.
DR STRING; 4896.SPAC11H11.01.1; -.
DR iPTMnet; Q7Z992; -.
DR MaxQB; Q7Z992; -.
DR PaxDb; Q7Z992; -.
DR EnsemblFungi; SPAC11H11.01.1; SPAC11H11.01.1:pep; SPAC11H11.01.
DR GeneID; 3361461; -.
DR KEGG; spo:SPAC11H11.01; -.
DR PomBase; SPAC11H11.01; sst6.
DR VEuPathDB; FungiDB:SPAC11H11.01; -.
DR HOGENOM; CLU_607150_0_0_1; -.
DR InParanoid; Q7Z992; -.
DR OMA; WISQIRI; -.
DR PRO; PR:Q7Z992; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000813; C:ESCRT I complex; ISO:PomBase.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IMP:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:PomBase.
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; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR017916; SB_dom.
DR Pfam; PF09454; Vps23_core; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR PROSITE; PS51312; SB; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Endosome; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..487
FT /note="ESCRT-I complex subunit vps23"
FT /id="PRO_0000353847"
FT DOMAIN 428..487
FT /note="SB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
SQ SEQUENCE 487 AA; 55968 MW; 60DFA2E4E415B0AC CRC64;
MSDHAINEHP SRILNTIEKI RFWKNGLAEE LELLFRKQCE DTFTLQAINI EVDTQDENKI
EEVRIYLSTP AFDKTILTSA CITVRSYYPS QPPIVQLLDE KGGKHKYTSL LLQLWKNERS
VFNIYRLVQA LIKQDFEREH TSPPELPTKL VNTIEKLKVK EENEAPPVIP AKPFSSSSEQ
HFRKVPALPS KLPPKPLKIT ANSSLGQETN SNSSSFQSTL FSLNTAPFSA TSQQLVHDSV
SLRRPSSNIP AQKPIPPKPE QNEIIITKDT PSLKDKYSKP ALLPQKPKVS KGQIVQQVSV
FSTGKKIESQ SLLNLIDTDI ETPLKGSSEL LYSEDFKPNV DPVKIQQILH KQNKIIEEKW
ISQIRISKNL EVKQRLLDQE RHALETLAKN IENNRFILGK RRRKAREALQ KLDNLKDLSV
QELFIIPSER ELKYYELKRK DEKLDEGIRA LNQALHHESI MPASWLKGIK LLARQQFLIR
DEMLQYS
