P25604 (STP22_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease

Alternative name(s):
ESCRT-I complex subunit VPS23
Vacuolar protein sorting-associated protein 23

Gene names

Name:	STP22
Synonyms:	VPS23
Ordered Locus Names:	YCL008C
ORF Names:	YCL8C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex. Required for vacuolar targeting of temperature-sensitive plasma membrane proteins STE2 and CAN1. Ref.1 Ref.7 Ref.8
Subunit structure	Component of the ESCRT-I complex (endosomal sorting complex required for transport I) which consists of STP22, VPS28, SRN2 and MVB12 in a 1:1:1:1 stoechiometry. Interacts with HSE1 and VPS27. Interactis with MVB12 and SRN2. Ref.8 Ref.10 Ref.11 Ref.15
Subcellular location	Cytoplasm. Endosome. Late endosome membrane; Peripheral membrane protein Probable Ref.1 Ref.7 Ref.8 Ref.10.
Domain	The UEV domain is required for the interaction of the complex with ubiquitin.
Miscellaneous	Present with 1360 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family. UEV subfamily. Contains 1 SB (steadiness box) domain. Contains 1 UEV (ubiquitin E2 variant) domain.
Sequence caution	The sequence CAC42964.1 differs from that shown. Reason: Frameshift at position 294.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
Domain	Coiled coil
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Inferred from electronic annotation. Source: InterPro late endosome to vacuole transport Inferred from mutant phenotype PubMed 17145965. Source: SGD protein targeting to membrane Inferred from mutant phenotype Ref.8. Source: UniProtKB protein targeting to vacuole Inferred from mutant phenotype Ref.8. Source: UniProtKB ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred by curator Ref.11. Source: SGD
Cellular_component	ESCRT I complex Inferred from direct assay Ref.12. Source: SGD internal side of plasma membrane Inferred from direct assay PubMed 20028738. Source: SGD late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	acid-amino acid ligase activity Inferred from electronic annotation. Source: InterPro ubiquitin binding Inferred from direct assay PubMed 19380877. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MVB12	P42939	6	EBI-411625,EBI-23478
SRN2	Q99176	5	EBI-411625,EBI-18076
VPS28	Q02767	2	EBI-411625,EBI-20387

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 385

385

Suppressor protein STP22 of temperature-sensitive alpha-factor receptor and arginine permease

PRO_0000082605

Regions

Domain

12 – 161

150

UEV

Domain

322 – 385

64

SB

Coiled coil

272 – 300

29

Potential

Compositional bias

155 – 201

47

Pro-rich

Experimental info

Mutagenesis

85

1

M → T: No interaction of the ESCRT-I complex with ubiquitin. Ref.8

Mutagenesis

254

1

M → D: Defective in ESCRT-I cargo sorting; reduces MVB12 localization to MVBs; abolishes interaction with MVB12; reduces interaction with SRN2. Ref.15

Mutagenesis

286

1

L → D: Defective in ESCRT-I cargo sorting. Ref.15

Mutagenesis

345

1

L → D: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVBs). Ref.14

Mutagenesis

371

1

F → D: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVBs). Ref.14

Secondary structure

1

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385

Helix Strand Turn

Details...

Helix

11 – 21

11

Turn

22 – 24

3

Helix

28 – 41

14

Beta strand

45 – 53

9

Beta strand

59 – 70

12

Beta strand

73 – 76

4

Beta strand

80 – 86

7

Turn

89 – 93

5

Beta strand

97 – 100

4

Helix

102 – 104

3

Turn

107 – 109

3

Helix

116 – 119

4

Beta strand

124 – 126

3

Helix

129 – 132

4

Helix

136 – 138

3

Helix

141 – 150

10

Helix

219 – 246

28

Helix

248 – 251

4

Helix

254 – 289

36

Helix

291 – 303

13

Helix

314 – 316

3

Helix

323 – 351

29

Helix

356 – 381

26

Turn

382 – 384

3

Sequences

	Sequence		Length	Mass (Da)
	P25604 [UniParc]. Last modified October 24, 2003. Version 3. Checksum: FEDE3BE79F063BCE	FASTA	385	43,330
	10 20 30 40 50 60 MSANGKISVP EAVVNWLFKV IQPIYNDGRT TFHDSLALLD NFHSLRPRTR VFTHSDGTPQ 70 80 90 100 110 120 LLLSIYGTIS TGEDGSSPHS IPVIMWVPSM YPVKPPFISI NLENFDMNTI SSSLPIQEYI 130 140 150 160 170 180 DSNGWIALPI LHCWDPAAMN LIMVVQELMS LLHEPPQDQA PSLPPKPNTQ LQQEQNTPPL 190 200 210 220 230 240 PPKPKSPHLK PPLPPPPPPQ PASNALDLMD MDNTDISPTN HHEMLQNLQT VVNELYREDV 250 260 270 280 290 300 DYVADKILTR QTVMQESIAR FHEIIAIDKN HLRAVEQAIE QTMHSLNAQI DVLTANRAKV 310 320 330 340 350 360 QQFSSTSHVD DEDVNSIAVA KTDGLNQLYN LVAQDYALTD TIECLSRMLH RGTIPLDTFV 370 380 KQGRELARQQ FLVRWHIQRI TSPLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast mutants affecting possible quality control of plasma membrane proteins." Li Y., Kane T., Tipper C., Spatrick P., Jenness D.D. Mol. Cell. Biol. 19:3588-3599(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Gromadka R. Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[4]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO N-TERMINUS.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii." Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A., Gates K., Gaffney T.D., Philippsen P. Genome Biol. 4:R45.1-R45.13(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-329. Strain: ATCC 204508 / S288c.
[7]	"Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking." Babst M., Odorizzi G., Estepa E.J., Emr S.D. Traffic 1:248-258(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I." Katzmann D.J., Babst M., Emr S.D. Cell 106:145-155(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-85.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Vps27 recruits ESCRT machinery to endosomes during MVB sorting." Katzmann D.J., Stefan C.J., Babst M., Emr S.D. J. Cell Biol. 162:413-423(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH VPS27.
[11]	"Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae." Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H. Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE ESCRT-1 COMPLEX, INTERACTION WITH HSE1 AND VPS27.
[12]	"Structural insights into endosomal sorting complex required for transport (ESCRT-I) recognition of ubiquitinated proteins." Teo H., Veprintsev D.B., Williams R.L. J. Biol. Chem. 279:28689-28696(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-161.
[13]	"ESCRT-I core and ESCRT-II GLUE domain structures reveal role for GLUE in linking to ESCRT-I and membranes." Teo H., Gill D.J., Sun J., Perisic O., Veprintsev D.B., Vallis Y., Emr S.D., Williams R.L. Cell 125:99-111(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 305-385 IN COMPLEX WITH VPS28 AND SRN2.
[14]	"Structural and functional organization of the ESCRT-I trafficking complex." Kostelansky M.S., Sun J., Lee S., Kim J., Ghirlando R., Hierro A., Emr S.D., Hurley J.H. Cell 125:113-126(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 322-385 IN COMPLEX WITH VPS28 AND SRN2, MUTAGENESIS OF LEU-345 AND PHE-371.
[15]	"Molecular architecture and functional model of the complete yeast ESCRT-I heterotetramer." Kostelansky M.S., Schluter C., Tam Y.Y., Lee S., Ghirlando R., Beach B., Conibear E., Hurley J.H. Cell 129:485-498(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 215-385, COMPOSITION OF THE ESCRT-I COMPLEX, INTERACTION WITH MVB12 AND SRN2, MUTAGENESIS OF MET-254 AND LEU-286.
[16]	"Structural insight into the ESCRT-I/-II link and its role in MVB trafficking." Gill D.J., Teo H., Sun J., Perisic O., Veprintsev D.B., Emr S.D., Williams R.L. EMBO J. 26:600-612(2007) [PubMed] [Europe PMC] [Abstract] Cited for: COMPOSITION OF THE ESCRT-I COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF004731 Genomic DNA. Translation: AAB62820.1.
X59720 Genomic DNA. Translation: CAC42964.1. Frameshift.
AY260880 Genomic DNA. Translation: AAP21748.1.
BK006937 Genomic DNA. Translation: DAA07473.1.

PIR

S74288.

RefSeq

NP_009919.3. NM_001178657.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UZX	X-ray	1.85	A	1-161	[»]
2CAZ	X-ray	3.60	A/D	305-385	[»]
2F66	X-ray	2.80	A/D	322-385	[»]
2F6M	X-ray	2.10	A/C	322-385	[»]
2P22	X-ray	2.70	A	215-385	[»]
3R3Q	X-ray	1.45	A	1-160	[»]
3R42	X-ray	1.87	A	1-160	[»]

ProteinModelPortal

P25604.

SMR

P25604. Positions 8-160, 218-385.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5827N.

IntAct

P25604. 5 interactions.

MINT

MINT-468287.

Proteomic databases

PaxDb

P25604.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YCL008C; YCL008C; YCL008C.

GeneID

850349.

KEGG

sce:YCL008C.

Organism-specific databases

CYGD

YCL008c.

SGD

S000000514. STP22.

Phylogenomic databases

eggNOG

NOG317261.

GeneTree

ENSGT00530000064004.

HOGENOM

HOG000057121.

KO

K12183.

OMA

PRTRVFT.

OrthoDB

EOG42Z80M.

Enzyme and pathway databases

BioCyc

YEAST:G3O-29278-MONOMER.

Gene expression databases

Genevestigator

P25604.

GermOnline

YCL008C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR017916. Steadiness_box.
IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
IPR008883. UEV_N.
[Graphical view]

Pfam

PF05743. UEV. 1 hit.
PF09454. Vps23_core. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS51312. SB. 1 hit.
PS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
PS51322. UEV. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25604.

NextBio

965809.

Entry information

Entry name

STP22_YEAST

Accession

Primary (citable) accession number: P25604
Secondary accession number(s): D6VR04 , P87010, P87279, Q86ZT3, Q8NIM6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 24, 2003
Last modified:	May 29, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program