Q99176 (SRN2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein SRN2

Alternative name(s):
ESCRT-I complex subunit VPS37
Vacuolar protein sorting-associated protein 37

Gene names

Name:	SRN2
Synonyms:	SRN10, VPS37
Ordered Locus Names:	YLR119W
ORF Names:	L2958, L9233.5

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	213 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. Required for normal endocytic and biosynthetic traffic to the yeast vacuole.
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 STP22 and MVB12. Ref.1 Ref.7
Subcellular location	Cytoplasm. Endosome Probable. Late endosome membrane; Peripheral membrane protein Probable Ref.1.
Sequence similarities	Belongs to the VPS37 family. Contains 1 VPS37 C-terminal domain.
Sequence caution	The sequence AAB88577.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasm Endosome Membrane
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein targeting to membrane Inferred from mutant phenotype. Source: SGD protein targeting to vacuole Inferred from physical interaction. Source: SGD ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Inferred by curator. Source: SGD
Cellular component	ESCRT I complex Inferred from direct assay. Source: SGD late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction Ref.6Ref.7. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MVB12	P42939	4	EBI-18076,EBI-23478
STP22	P25604	5	EBI-18076,EBI-411625

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 213

213

Protein SRN2

PRO_0000072191

Regions

Domain

128 – 213

86

VPS37 C-terminal

Experimental info

Mutagenesis

67

1

L → D: Defective in ESCRT-I cargo sorting. Ref.7

Mutagenesis

75

1

L → D: Defective in ESCRT-I cargo sorting. Ref.7

Mutagenesis

79

1

V → D: Defective in ESCRT-I cargo sorting. Ref.7

Mutagenesis

88

1

F → D: Defective in ESCRT-I cargo sorting; when associated with D-99. Ref.7

Mutagenesis

92

1

I → D: Defective in ESCRT-I cargo sorting; when associated with D-102. Ref.7

Mutagenesis

95

1

F → D: Defective in ESCRT-I cargo sorting; when associated with D-99. Ref.7

Mutagenesis

99

1

F → D: Defective in ESCRT-I cargo sorting; when associated with D-88. Ref.7

Mutagenesis

99

1

F → D: Defective in ESCRT-I cargo sorting; when associated with D-95.

Mutagenesis

102

1

L → D: Defective in ESCRT-I cargo sorting; when associated with D-92. Ref.7

Mutagenesis

181

1

L → R: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVB); when associated with R-185. Ref.6

Mutagenesis

185

1

I → R: Abolishes ESCRT-I complex assembly; class E phenotype (malformed late MVB); when associated with R-181. Ref.6

Sequence conflict

90

1

G → E in AAB88577. Ref.1

Sequence conflict

140

1

E → D in AAB88577. Ref.1

Sequence conflict

143

1

K → E in AAB88577. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

213

Helix Strand Turn

Details...

Helix

23 – 33

11

Helix

55 – 57

3

Helix

62 – 70

9

Helix

72 – 78

7

Helix

79 – 82

4

Helix

86 – 141

56

Helix

145 – 171

27

Helix

178 – 202

25

Sequences

	Sequence		Length	Mass (Da)
	Q99176 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 4E99806CED03E345	FASTA	213	25,101
	10 20 30 40 50 60 MKVKATKLRI KQRRKNKGLN ISRLDIIRAE MDVVPSPGLP EKVNEKSKNI PLPEGINLLS 70 80 90 100 110 120 SKEIIDLIQT HRHQLELYVT KFNPLTDFAG KIHAFRDQFK QLEENFEDLH EQKDKVQALL 130 140 150 160 170 180 ENCRILESKY VASWQDYHSE FSKKYGDIAL KKKLEQNTKK LDEESSQLET TTRSIDSADD 190 200 210 LDQFIKNYLD IRTQYHLRRE KLATWDKQGN LKY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of an extragenic suppressor of the rna1-1 mutation in Saccharomyces cerevisiae." Hong S.J., Yi Y.S., Koh S.S., Park O.K., Kang H.S. Mol. Gen. Genet. 259:404-413(1998) [PubMed: 9790597] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH RNA1, SUBCELLULAR LOCATION.
[2]	"Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found." Verhasselt P., Volckaert G. Yeast 13:241-250(1997) [PubMed: 9090053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 90840 / EAY235 / FY23.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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: 16615893] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 130-213 IN COMPLEX WITH STP22 AND VPS28.
[6]	"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: 16615894] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 132-213 IN COMPLEX WITH STP22 AND VPS28, MUTAGENESIS OF LEU-181 AND ILE-185.
[7]	"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: 17442384] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-213, COMPOSITION OF THE ESCRT-I COMPLEX, INTERACTION WITH STP22 AND MVB12, MUTAGENESIS OF LEU-67; LEU-75; VAL-79; PHE-88; ILE-92; PHE-95; PHE-99 AND LEU-102.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U40562 Genomic DNA. Translation: AAB88577.1. Different initiation.
X89514 Genomic DNA. Translation: CAA61698.1.
U53877 Genomic DNA. Translation: AAB82366.1.
Z73291 Genomic DNA. Translation: CAA97687.1.
BK006945 Genomic DNA. Translation: DAA09433.1.

PIR

S64956.

RefSeq

NP_013220.1. NM_001182006.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CAZ	X-ray	3.60	C/F	130-213	[»]
2F66	X-ray	2.80	C/F	132-213	[»]
2P22	X-ray	2.70	C	22-213	[»]

ProteinModelPortal

Q99176.

SMR

Q99176. Positions 22-213.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2130N.

IntAct

Q99176. 4 interactions.

MINT

MINT-505977.

STRING

Q99176.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR119W; YLR119W; YLR119W.

GeneID

850810.

KEGG

sce:YLR119W.

NMPDR

fig|4932.3.peg.4212.

Organism-specific databases

CYGD

YLR119w.

SGD

S000004109. SRN2.

Phylogenomic databases

eggNOG

fuNOG12763.

OMA

VILESEY.

OrthoDB

EOG45MRFJ.

Gene expression databases

ArrayExpress

Q99176.

Genevestigator

Q99176.

GermOnline

YLR119W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR017435. ESCRT-1_cplx_Vps37_fungi.
IPR009851. Mod_r.
[Graphical view]

Pfam

PF07200. Mod_r. 1 hit.
[Graphical view]

PIRSF

PIRSF038214. ESCRT1_Vps37_fungi. 1 hit.

PROSITE

PS51314. VPS37_C. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967046.

Entry information

Entry name

SRN2_YEAST

Accession

Primary (citable) accession number: Q99176
Secondary accession number(s): D6VYB7, Q02806

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program