P32893 (TRS65_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Trafficking protein particle complex II-specific subunit 65
Short name=TRAPP II-specific subunit 65

Alternative name(s):
Beta-glucan synthesis-associated protein TRS65
Killer toxin-resistance protein 11
Transport protein particle 65 kDa subunit

Gene names

Name:	TRS65
Synonyms:	KRE11
Ordered Locus Names:	YGR166W

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

General annotation (Comments)

Function	Specific subunit of the TRAPP II complex, a highly conserved vesicle tethering complex that functions in the late Golgi as a guanine nucleotide exchanger (GEF) for the Golgi YPT1 GTPase. TRS65 plays a role in the YPT GEF activity of TRAPP II in concert with the two other TRAPP II-specific subunits TRS120 and TRS130. Involved in cell wall (1-->6)-beta-glucan synthesis. Ref.6 Ref.9 Ref.11
Pathway	Glycan metabolism; beta-glucan biosynthesis.
Subunit structure	Part of the multisubunit TRAPP (transport protein particle) II complex composed of BET3, BET5, TRS20, TRS23, TRS31, TRS33, TRS65, TRS120 and TRS130. Interacts directly with TRS120 and TRS130. Ref.5 Ref.6 Ref.9 Ref.11
Subcellular location	Cytoplasm. Golgi apparatus › cis-Golgi network Ref.6 Ref.9.
Miscellaneous	Present with 1660 molecules/cell in log phase SD medium.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Transport
Cellular component	Cytoplasm Golgi apparatus
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	beta-glucan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway intra-Golgi vesicle-mediated transport Inferred from genetic interaction Ref.9. Source: SGD protein complex assembly Inferred from genetic interaction Ref.9. Source: SGD
Cellular_component	TRAPP complex Inferred from direct assay PubMed 10727015. Source: SGD trans-Golgi network Inferred from direct assay Ref.9. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 560	560	Trafficking protein particle complex II-specific subunit 65		PRO_0000084328
Amino acid modifications
	Modified residue	221	1	Phosphoserine Ref.8
	Modified residue	393	1	Phosphoserine Ref.10
	Modified residue	398	1	Phosphoserine Ref.8 Ref.10
	Modified residue	401	1	Phosphoserine Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P32893 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 9039A2CEBB1F8316	FASTA	560	63,368
	10 20 30 40 50 60 MECFVPLRCD LDGSNIEQLR QSHLSRKFII FDEQLNLWLW FQGNSQENKR FVLQNMIILI 70 80 90 100 110 120 NEAQVTRTST IDDYFTQVEN NENLWRLKND CCSKILFKSN VVMNNGYNNQ IKFVFEYKSV 130 140 150 160 170 180 DANFNNQDSL QDPQAKYTLD KYSSEEILPS FEPVYSWSSA ATKSSKNTNN HLEKNNRATH 190 200 210 220 230 240 RVSSKNSEVH EADVSRNPNT FTLKLQYPIF SLLNMRLRNI SLKSEHCILS SLDFQTSKAS 250 260 270 280 290 300 EQLTKKFIYP QEHNSFLKLN FQEISYKLID GTSQIELDPI CPLKVPLTAF SYDSISATFK 310 320 330 340 350 360 LVLLPKSTQP HRVKITLAYE LELHPNLKLP VRTSWETEVT LKRSMPISST SSQYSSNNNN 370 380 390 400 410 420 TNHSASFNGA ANNVNSGGLA NLRLGGVSSS RFSLGAASTT SLVNSKLSNV KFKFINSNIK 430 440 450 460 470 480 VIKGEKFTMR LQIINSSSSP LDLVVYYNNT INPIPSANNV RNSNGINNCG MNNGTIPNSP 490 500 510 520 530 540 LTLENQYQLH NKYRKIAEGI ILLSNDYKIP VVPPRETYFA DLRFIGIMSG YYGTLSGLKV 550 560 LDLNTNELIE VGNGASVLIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mutational analysis of killer toxin resistance in Saccharomyces cerevisiae identifies new genes involved in cell wall (1-->6)-beta-glucan synthesis." Brown J.L., Kossaczka Z., Jiang B., Bussey H. Genetics 133:837-849(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"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: IDENTIFICATION IN THE TRAPP II COMPLEX.
[6]	"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, SUBCELLULAR LOCATION.
[7]	"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].
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-398, MASS SPECTROMETRY. Strain: YAL6B.
[9]	"The role of Trs65 in the Ypt/Rab guanine nucleotide exchange factor function of the TRAPP II complex." Liang Y., Morozova N., Tokarev A.A., Mulholland J.W., Segev N. Mol. Biol. Cell 18:2533-2541(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TRS120 AND TRS130.
[10]	"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-393; SER-398 AND SER-401, MASS SPECTROMETRY.
[11]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L10667 Genomic DNA. Translation: AAA34727.1. Z72951 Genomic DNA. Translation: CAA97191.1. BK006941 Genomic DNA. Translation: DAA08260.1.
PIR	S42158.
RefSeq	NP_011682.1. NM_001181295.1.
3D structure databases
ProteinModelPortal	P32893.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5104N.
IntAct	P32893. 6 interactions.
MINT	MINT-528179.
STRING	4932.YGR166W.
Proteomic databases
PaxDb	P32893.
PeptideAtlas	P32893.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGR166W; YGR166W; YGR166W.
GeneID	853076.
KEGG	sce:YGR166W.
Organism-specific databases
CYGD	YGR166w.
SGD	S000003398. TRS65.
Phylogenomic databases
eggNOG	NOG46088.
OMA	SNDYKIP.
OrthoDB	EOG4H1F40.
Enzyme and pathway databases
UniPathway	UPA00636.
Gene expression databases
Genevestigator	P32893.
GermOnline	YGR166W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR024662. TRAPP_II_complex_Trs65. [Graphical view]
Pfam	PF12735. Trs65. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	973035.

Entry information

Entry name

TRS65_YEAST

Accession

Primary (citable) accession number: P32893
Secondary accession number(s): D6VUU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program