Q03337 (TRS31_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trafficking protein particle complex subunit 31
Short name=TRAPP subunit 31

Alternative name(s):
Transport protein particle 31 kDa subunit

Gene names

Name:	TRS31
Ordered Locus Names:	YDR472W

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	283 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the TRAPP I, TRAPP II and TRAPP III complexes which act as guanine nucleotide exchange factors (GEF) for YPT1. TRAPP I plays a key role in the late stages of endoplasmic reticulum to Golgi traffic. TRAPP II plays a role in intra-Golgi transport. TRAPP III plays a role in autophagosome formation. Ref.3 Ref.4 Ref.7 Ref.8
Subunit structure	Part of the multisubunit TRAPP (transport protein particle) I complex composed of BET3, BET5, TRS20, TRS23, TRS31 and TRS33. Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS85, TRS120 and TRS130. Part of the multisubunit TRAPP (transport protein particle) III complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33 and TRS85. Ref.3 Ref.4 Ref.7 Ref.8
Subcellular location	Golgi apparatus › cis-Golgi network. Endoplasmic reticulum. Preautophagosomal structure Ref.4 Ref.8.
Miscellaneous	Present with 8350 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the TRAPP small subunits family. BET3 subfamily.

Ontologies

Keywords
Biological process	Autophagy ER-Golgi transport Transport
Cellular component	Endoplasmic reticulum Golgi apparatus
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi vesicle-mediated transport Inferred from mutant phenotype Ref.4. Source: SGD autophagy Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	TRAPP complex Inferred from direct assay PubMed 10727015. Source: SGD endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell pre-autophagosomal structure Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BET3	P36149	13	EBI-38770,EBI-3567
TRS20	P38334	5	EBI-38770,EBI-19468

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 283

283

Trafficking protein particle complex subunit 31

PRO_0000211585

Amino acid modifications

Modified residue

109

1

Phosphoserine Ref.6

Modified residue

125

1

Phosphoserine Ref.6

Modified residue

126

1

Phosphoserine Ref.6

Secondary structure

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283

Helix Strand Turn

Details...

Beta strand

56 – 58

3

Helix

59 – 76

18

Helix

83 – 89

7

Helix

97 – 101

5

Beta strand

170 – 172

3

Helix

176 – 183

8

Helix

187 – 190

4

Beta strand

197 – 201

5

Beta strand

209 – 215

7

Beta strand

217 – 219

3

Helix

228 – 231

4

Turn

241 – 243

3

Beta strand

251 – 253

3

Beta strand

264 – 267

4

Helix

272 – 277

6

Sequences

	Sequence		Length	Mass (Da)
	Q03337 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 857BBA3E03423D42	FASTA	283	31,722
	10 20 30 40 50 60 MSQRIIQPSA SDQQFPGKSD GYEYTVGPKQ AITSEASTTY IPSRIYSESL LFKRQEASLS 70 80 90 100 110 120 AMAFLFQEMI SQLHRTCKTA GDFETKLSDY GHNIGIRLLE LLNFRASVSP SSLPRASAFL 130 140 150 160 170 180 SQNESSSKLS NASNSPGMLA NSSTATSASA NERLQEKQTE SLSNYITKMR RRDLKILDIL 190 200 210 220 230 240 QFIHGTLWSY LFNHVSDDLV KSSERDNEYM IVDNFPTLTQ FIPGENVSCE YFVCGIIKGF 250 260 270 280 LFNAGFPCGV TAHRMPQGGH SQRTVYLIQF DRQVLDREGL RFG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion." Sacher M., Jiang Y., Barrowman J., Scarpa A., Burston J., Zhang L., Schieltz D., Yates J.R. III, Abeliovich H., Ferro-Novick S. EMBO J. 17:2494-2503(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE TRAPP II COMPLEX.
[4]	"TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport." Sacher M., Barrowman J., Wang W., Horecka J., Zhang Y., Pypaert M., Ferro-Novick S. Mol. Cell 7:433-442(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE TRAPP II COMPLEX, IDENTIFICATION IN THE TRAPP II COMPLEX, FUNCTION OF THE TRAPP I COMPLEX, IDENTIFICATION IN THE TRAPP I COMPLEX, SUBCELLULAR LOCATION.
[5]	"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].
[6]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-125 AND SER-126, MASS SPECTROMETRY.
[7]	"Molecular architecture of the TRAPPII complex and implications for vesicle tethering." Yip C.K., Berscheminski J., Walz T. Nat. Struct. Mol. Biol. 17:1298-1304(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TRAP II COMPLEX, FUNCTION OF THE TRAP II COMPLEX.
[8]	"Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote autophagy." Lynch-Day M.A., Bhandari D., Menon S., Huang J., Cai H., Bartholomew C.R., Brumell J.H., Ferro-Novick S., Klionsky D.J. Proc. Natl. Acad. Sci. U.S.A. 107:7811-7816(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE TRAPP III COMPLEX, SUBCELLULAR LOCATION, FUNCTION OF THE TRAPP III COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U33050 Genomic DNA. Translation: AAB64914.1.
BK006938 Genomic DNA. Translation: DAA12306.1.

PIR

S69639.

RefSeq

NP_010760.3. NM_001180780.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CUE	X-ray	3.70	B/H/N/T	1-283	[»]

ProteinModelPortal

Q03337.

SMR

Q03337. Positions 55-104, 116-282.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1709N.

IntAct

Q03337. 9 interactions.

MINT

MINT-401389.

STRING

4932.YDR472W.

Proteomic databases

PaxDb

Q03337.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR472W; YDR472W; YDR472W.

GeneID

852083.

KEGG

sce:YDR472W.
sce:YDR477W.

Organism-specific databases

CYGD

YDR472w.

SGD

S000002880. TRS31.

Phylogenomic databases

eggNOG

COG5128.

GeneTree

ENSGT00390000000976.

HOGENOM

HOG000176758.

KO

K12761.

OMA

RDEENEY.

OrthoDB

EOG47WRZ1.

Gene expression databases

Genevestigator

Q03337.

GermOnline

YDR472W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR024096. NO_sig/Golgi_transp_ligand-bd.
IPR016696. TRAPP-I_Trs31.
IPR007194. TRAPP_component.
[Graphical view]

PANTHER

PTHR20902. PTHR20902. 1 hit.

Pfam

PF04051. TRAPP. 1 hit.
[Graphical view]

PIRSF

PIRSF017479. TRAPP_I_complex_Trs31. 1 hit.

SUPFAM

SSF111126. Haem_NO-bd. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q03337.

NextBio

970397.

Entry information

Entry name

TRS31_YEAST

Accession

Primary (citable) accession number: Q03337
Secondary accession number(s): D6VT96

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program