STP22_YEAST
ID STP22_YEAST Reviewed; 385 AA.
AC P25604; D6VR04; P87010; P87279; Q86ZT3; Q8NIM6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease;
DE AltName: Full=ESCRT-I complex subunit VPS23;
DE AltName: Full=Vacuolar protein sorting-associated protein 23;
GN Name=STP22; Synonyms=VPS23; OrderedLocusNames=YCL008C; ORFNames=YCL8C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10207082; DOI=10.1128/mcb.19.5.3588;
RA Li Y., Kane T., Tipper C., Spatrick P., Jenness D.D.;
RT "Yeast mutants affecting possible quality control of plasma membrane
RT proteins.";
RL Mol. Cell. Biol. 19:3588-3599(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION.
RA Gromadka R.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-329.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11208108; DOI=10.1034/j.1600-0854.2000.010307.x;
RA Babst M., Odorizzi G., Estepa E.J., Emr S.D.;
RT "Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue,
RT Vps23p, both function in late endosomal trafficking.";
RL Traffic 1:248-258(2000).
RN [8]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF MET-85.
RX PubMed=11511343; DOI=10.1016/s0092-8674(01)00434-2;
RA Katzmann D.J., Babst M., Emr S.D.;
RT "Ubiquitin-dependent sorting into the multivesicular body pathway requires
RT the function of a conserved endosomal protein sorting complex, ESCRT-I.";
RL Cell 106:145-155(2001).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH VPS27.
RX PubMed=12900393; DOI=10.1083/jcb.200302136;
RA Katzmann D.J., Stefan C.J., Babst M., Emr S.D.;
RT "Vps27 recruits ESCRT machinery to endosomes during MVB sorting.";
RL J. Cell Biol. 162:413-423(2003).
RN [11]
RP IDENTIFICATION IN THE ESCRT-1 COMPLEX, AND INTERACTION WITH HSE1 AND VPS27.
RX PubMed=15086794; DOI=10.1111/j.1600-0854.2004.00169.x;
RA Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P.,
RA Stevens T.H.;
RT "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces
RT cerevisiae.";
RL Traffic 5:194-210(2004).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-161.
RX PubMed=15044434; DOI=10.1074/jbc.m400023200;
RA Teo H., Veprintsev D.B., Williams R.L.;
RT "Structural insights into endosomal sorting complex required for transport
RT (ESCRT-I) recognition of ubiquitinated proteins.";
RL J. Biol. Chem. 279:28689-28696(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 305-385 IN COMPLEX WITH VPS28 AND
RP SRN2.
RX PubMed=16615893; DOI=10.1016/j.cell.2006.01.047;
RA Teo H., Gill D.J., Sun J., Perisic O., Veprintsev D.B., Vallis Y.,
RA Emr S.D., Williams R.L.;
RT "ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in
RT linking to ESCRT-I and membranes.";
RL Cell 125:99-111(2006).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 322-385 IN COMPLEX WITH VPS28 AND
RP SRN2, AND MUTAGENESIS OF LEU-345 AND PHE-371.
RX PubMed=16615894; DOI=10.1016/j.cell.2006.01.049;
RA Kostelansky M.S., Sun J., Lee S., Kim J., Ghirlando R., Hierro A.,
RA Emr S.D., Hurley J.H.;
RT "Structural and functional organization of the ESCRT-I trafficking
RT complex.";
RL Cell 125:113-126(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-385, COMPOSITION OF THE
RP ESCRT-I COMPLEX, INTERACTION WITH MVB12 AND SRN2, AND MUTAGENESIS OF
RP MET-254 AND LEU-286.
RX PubMed=17442384; DOI=10.1016/j.cell.2007.03.016;
RA Kostelansky M.S., Schluter C., Tam Y.Y., Lee S., Ghirlando R., Beach B.,
RA Conibear E., Hurley J.H.;
RT "Molecular architecture and functional model of the complete yeast ESCRT-I
RT heterotetramer.";
RL Cell 129:485-498(2007).
RN [16]
RP COMPOSITION OF THE ESCRT-I COMPLEX.
RX PubMed=17215868; DOI=10.1038/sj.emboj.7601501;
RA Gill D.J., Teo H., Sun J., Perisic O., Veprintsev D.B., Emr S.D.,
RA Williams R.L.;
RT "Structural insight into the ESCRT-I/-II link and its role in MVB
RT trafficking.";
RL EMBO J. 26:600-612(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. Required for vacuolar targeting of temperature-sensitive
CC plasma membrane proteins STE2 and CAN1. {ECO:0000269|PubMed:10207082,
CC ECO:0000269|PubMed:11208108, ECO:0000269|PubMed:11511343}.
CC -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting complex
CC required for transport I) which consists of STP22, VPS28, SRN2 and
CC MVB12 in a 1:1:1:1 stoichiometry. Interacts with HSE1 and VPS27.
CC Interacts with MVB12 and SRN2. {ECO:0000269|PubMed:11511343,
CC ECO:0000269|PubMed:12900393, ECO:0000269|PubMed:15086794,
CC ECO:0000269|PubMed:16615893, ECO:0000269|PubMed:16615894,
CC ECO:0000269|PubMed:17442384}.
CC -!- INTERACTION:
CC P25604; Q05080: HOF1; NbExp=2; IntAct=EBI-411625, EBI-5412;
CC P25604; P38753: HSE1; NbExp=3; IntAct=EBI-411625, EBI-1382;
CC P25604; P43603: LSB3; NbExp=3; IntAct=EBI-411625, EBI-22980;
CC P25604; P42939: MVB12; NbExp=12; IntAct=EBI-411625, EBI-23478;
CC P25604; P80667: PEX13; NbExp=2; IntAct=EBI-411625, EBI-13206;
CC P25604; Q99176: SRN2; NbExp=9; IntAct=EBI-411625, EBI-18076;
CC P25604; P40343: VPS27; NbExp=7; IntAct=EBI-411625, EBI-20380;
CC P25604; Q02767: VPS28; NbExp=4; IntAct=EBI-411625, EBI-20387;
CC P25604; P32793: YSC84; NbExp=2; IntAct=EBI-411625, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome. Late endosome membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- DOMAIN: The UEV domain is required for the interaction of the complex
CC with ubiquitin.
CC -!- MISCELLANEOUS: Present with 1360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UEV
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC42964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF004731; AAB62820.1; -; Genomic_DNA.
DR EMBL; X59720; CAC42964.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260880; AAP21748.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07473.1; -; Genomic_DNA.
DR PIR; S74288; S74288.
DR RefSeq; NP_009919.3; NM_001178657.1.
DR PDB; 1UZX; X-ray; 1.85 A; A=1-161.
DR PDB; 2CAZ; X-ray; 3.60 A; A/D=305-385.
DR PDB; 2F66; X-ray; 2.80 A; A/D=322-385.
DR PDB; 2F6M; X-ray; 2.10 A; A/C=322-385.
DR PDB; 2P22; X-ray; 2.70 A; A=215-385.
DR PDB; 3R3Q; X-ray; 1.45 A; A=1-160.
DR PDB; 3R42; X-ray; 1.87 A; A=1-160.
DR PDBsum; 1UZX; -.
DR PDBsum; 2CAZ; -.
DR PDBsum; 2F66; -.
DR PDBsum; 2F6M; -.
DR PDBsum; 2P22; -.
DR PDBsum; 3R3Q; -.
DR PDBsum; 3R42; -.
DR AlphaFoldDB; P25604; -.
DR SMR; P25604; -.
DR BioGRID; 30973; 484.
DR ComplexPortal; CPX-940; ESCRT-I complex.
DR DIP; DIP-5827N; -.
DR IntAct; P25604; 10.
DR MINT; P25604; -.
DR STRING; 4932.YCL008C; -.
DR TCDB; 3.A.31.1.1; the endosomal sorting complexes required for transport iii (escrt-iii) family.
DR iPTMnet; P25604; -.
DR MaxQB; P25604; -.
DR PaxDb; P25604; -.
DR PRIDE; P25604; -.
DR EnsemblFungi; YCL008C_mRNA; YCL008C; YCL008C.
DR GeneID; 850349; -.
DR KEGG; sce:YCL008C; -.
DR SGD; S000000514; STP22.
DR VEuPathDB; FungiDB:YCL008C; -.
DR eggNOG; KOG2391; Eukaryota.
DR GeneTree; ENSGT00940000153903; -.
DR HOGENOM; CLU_046554_0_0_1; -.
DR InParanoid; P25604; -.
DR OMA; YMNFPQP; -.
DR BioCyc; YEAST:G3O-29278-MON; -.
DR Reactome; R-SCE-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR EvolutionaryTrace; P25604; -.
DR PRO; PR:P25604; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25604; protein.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0000813; C:ESCRT I complex; IDA:SGD.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:1904669; P:ATP export; IMP:SGD.
DR GO; GO:0008333; P:endosome to lysosome transport; IBA:GO_Central.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:1902915; P:negative regulation of protein polyubiquitination; IMP:SGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IDA:SGD.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR037202; ESCRT_assembly_dom.
DR InterPro; IPR017916; SB_dom.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR InterPro; IPR008883; UEV_N.
DR Pfam; PF05743; UEV; 1.
DR Pfam; PF09454; Vps23_core; 1.
DR SUPFAM; SSF140111; SSF140111; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS51312; SB; 1.
DR PROSITE; PS51322; UEV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Cytoplasm; Endosome; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..385
FT /note="Suppressor protein STP22 of temperature-sensitive
FT alpha-factor receptor and arginine permease"
FT /id="PRO_0000082605"
FT DOMAIN 12..161
FT /note="UEV"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00652"
FT DOMAIN 322..385
FT /note="SB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00644"
FT REGION 155..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 272..300
FT /evidence="ECO:0000255"
FT COMPBIAS 177..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 85
FT /note="M->T: No interaction of the ESCRT-I complex with
FT ubiquitin."
FT /evidence="ECO:0000269|PubMed:11511343"
FT MUTAGEN 254
FT /note="M->D: Defective in ESCRT-I cargo sorting; reduces
FT MVB12 localization to MVBs; abolishes interaction with
FT MVB12; reduces interaction with SRN2."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 286
FT /note="L->D: Defective in ESCRT-I cargo sorting."
FT /evidence="ECO:0000269|PubMed:17442384"
FT MUTAGEN 345
FT /note="L->D: Abolishes ESCRT-I complex assembly; class E
FT phenotype (malformed late MVBs)."
FT /evidence="ECO:0000269|PubMed:16615894"
FT MUTAGEN 371
FT /note="F->D: Abolishes ESCRT-I complex assembly; class E
FT phenotype (malformed late MVBs)."
FT /evidence="ECO:0000269|PubMed:16615894"
FT HELIX 11..21
FT /evidence="ECO:0007829|PDB:3R3Q"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:3R3Q"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:3R3Q"
FT STRAND 59..70
FT /evidence="ECO:0007829|PDB:3R3Q"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:3R42"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:3R3Q"
FT TURN 89..93
FT /evidence="ECO:0007829|PDB:3R3Q"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3R3Q"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:3R3Q"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:3R3Q"
FT HELIX 219..246
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 248..251
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 254..289
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:2P22"
FT HELIX 323..351
FT /evidence="ECO:0007829|PDB:2F6M"
FT HELIX 356..381
FT /evidence="ECO:0007829|PDB:2F6M"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:2F6M"
SQ SEQUENCE 385 AA; 43330 MW; FEDE3BE79F063BCE CRC64;
MSANGKISVP EAVVNWLFKV IQPIYNDGRT TFHDSLALLD NFHSLRPRTR VFTHSDGTPQ
LLLSIYGTIS TGEDGSSPHS IPVIMWVPSM YPVKPPFISI NLENFDMNTI SSSLPIQEYI
DSNGWIALPI LHCWDPAAMN LIMVVQELMS LLHEPPQDQA PSLPPKPNTQ LQQEQNTPPL
PPKPKSPHLK PPLPPPPPPQ PASNALDLMD MDNTDISPTN HHEMLQNLQT VVNELYREDV
DYVADKILTR QTVMQESIAR FHEIIAIDKN HLRAVEQAIE QTMHSLNAQI DVLTANRAKV
QQFSSTSHVD DEDVNSIAVA KTDGLNQLYN LVAQDYALTD TIECLSRMLH RGTIPLDTFV
KQGRELARQQ FLVRWHIQRI TSPLS
