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P53283 (TPO2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyamine transporter 2
Gene names
Name:TPO2
Ordered Locus Names:YGR138C
ORF Names:G6417
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell membrane polyamine/proton antiporter, involved in the detoxification of excess polyamines in the cytoplasm. Recognizes spermine, but not spermidine. Ref.3 Ref.4

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.4 Ref.5.

Induction

By transcription factor HAA1 in response to acetaldehyde accumulation. Ref.6

Sequence similarities

Belongs to the major facilitator superfamily. DHA1 family. Polyamines/proton antiporter (TC 2.A.1.2.16) subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 614614Polyamine transporter 2
PRO_0000173439

Regions

Topological domain1 – 173173Cytoplasmic Potential
Transmembrane174 – 19421Helical; Potential
Topological domain195 – 20612Extracellular Potential
Transmembrane207 – 22721Helical; Potential
Topological domain228 – 2369Cytoplasmic Potential
Transmembrane237 – 25721Helical; Potential
Topological domain258 – 2669Extracellular Potential
Transmembrane267 – 28721Helical; Potential
Topological domain288 – 29710Cytoplasmic Potential
Transmembrane298 – 31821Helical; Potential
Topological domain319 – 3268Extracellular Potential
Transmembrane327 – 34721Helical; Potential
Topological domain348 – 40760Cytoplasmic Potential
Transmembrane408 – 42821Helical; Potential
Topological domain429 – 4379Extracellular Potential
Transmembrane438 – 45821Helical; Potential
Topological domain459 – 47820Cytoplasmic Potential
Transmembrane479 – 49921Helical; Potential
Topological domain500 – 5034Extracellular Potential
Transmembrane504 – 52421Helical; Potential
Topological domain525 – 54117Cytoplasmic Potential
Transmembrane542 – 56221Helical; Potential
Topological domain563 – 57412Extracellular Potential
Transmembrane575 – 59521Helical; Potential
Topological domain596 – 61419Cytoplasmic Potential

Amino acid modifications

Modified residue501Phosphoserine Ref.9 Ref.10

Sequences

Sequence LengthMass (Da)Tools
P53283 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: C6B9D48720D4F2D2

FASTA61467,589
        10         20         30         40         50         60 
MSDQESVVSF NSQNTSMVDV EGQQPQQYVP SKTNSRANQL KLTKTETVKS LQDLGVTSAA 

        70         80         90        100        110        120 
PVPDINAPQT AKNNIFPEEY TMETPSGLVP VATLQSMGRT ASALSRTRTK QLNRTATNSS 

       130        140        150        160        170        180 
STGKEEMEEE ETEEREDQSG ENELDPEIEF VTFVTGDPEN PHNWPSWVRW SYTVLLSILV 

       190        200        210        220        230        240 
ICVAYGSACI SGGLGTVEKK YHVGMEAAIL SCSLMVIGFS LGPLIWSPVS DLYGRRVAYF 

       250        260        270        280        290        300 
VSMGLYVIFN IPCALAPNLG CLLACRFLCG VWSSSGLCLV GGSIADMFPS ETRGKAIAFF 

       310        320        330        340        350        360 
AFAPYVGPVV GPLVNGFISV STGRMDLIFW VNMAFAGVMW IISSAIPETY APVILKRKAA 

       370        380        390        400        410        420 
RLRKETGNPK IMTEQEAQGV SMSEMMRACL LRPLYFAVTE PVLVATCFYV CLIYSLLYAF 

       430        440        450        460        470        480 
FFAFPVIFGE LYGYKDNLVG LMFIPIVIGA LWALATTFYC ENKYLQIVKQ RKPTPEDRLL 

       490        500        510        520        530        540 
GAKIGAPFAA IALWILGATA YKHIIWVGPA SAGLAFGFGM VLIYYSLNNY IIDCYVQYAS 

       550        560        570        580        590        600 
SALATKVFLR SAGGAAFPLF TIQMYHKLNL HWGSWLLAFI STAMIALPFA FSYWGKGLRH 

       610 
KLSKKDYSID SVEM 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Multiple polyamine transport systems on the vacuolar membrane in yeast."
Tomitori H., Kashiwagi K., Asakawa T., Kakinuma Y., Michael A.J., Igarashi K.
Biochem. J. 353:681-688(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Localization and function of the yeast multidrug transporter Tpo1p."
Albertsen M., Bellahn I., Kraemer R., Waffenschmidt S.
J. Biol. Chem. 278:12820-12825(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[6]"Exposure of Saccharomyces cerevisiae to acetaldehyde induces sulfur amino acid metabolism and polyamine transporter genes, which depend on Met4p and Haa1p transcription factors, respectively."
Aranda A., del Olmo M.
Appl. Environ. Microbiol. 70:1913-1922(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[8]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[9]"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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z72923 Genomic DNA. Translation: CAA97151.1.
BK006941 Genomic DNA. Translation: DAA08230.1.
PIRS64447.
RefSeqNP_011654.1. NM_001181267.1.

3D structure databases

ProteinModelPortalP53283.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33385. 42 interactions.
DIPDIP-7902N.
IntActP53283. 24 interactions.
MINTMINT-4487428.
STRING4932.YGR138C.

Protein family/group databases

TCDB2.A.1.2.67. the major facilitator superfamily (mfs).

Proteomic databases

PaxDbP53283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR138C; YGR138C; YGR138C.
GeneID853039.
KEGGsce:YGR138C.

Organism-specific databases

CYGDYGR138c.
SGDS000003370. TPO2.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00620000088227.
HOGENOMHOG000160689.
OMASANNYLI.
OrthoDBEOG77M8XK.

Enzyme and pathway databases

BioCycYEAST:G3O-30843-MONOMER.

Gene expression databases

GenevestigatorP53283.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972941.

Entry information

Entry nameTPO2_YEAST
AccessionPrimary (citable) accession number: P53283
Secondary accession number(s): D6VUR9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families