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P39010 (AKR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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:
Palmitoyltransferase AKR1
EC=2.3.1.-
Alternative name(s):
Ankyrin repeat-containing protein AKR1
Gene names
Name:AKR1
Ordered Locus Names:YDR264C
ORF Names:D9954.9, YD9230B.03C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Palmitoyltransferase specific for casein kinase 1. Palmitoylates isoforms YCK1 and YCK2 at both C-terminal cysteine residues, which is required for their proper plasma membrane localization. Required for constitutive endocytosis of a-factor receptor STE3 and both constitutive and pheromone-induced endocytosis of alpha-factor receptor STE2. Ref.1 Ref.4 Ref.5 Ref.6 Ref.9

Catalytic activity

Palmitoyl-CoA + protein-cysteine = S-palmitoyl protein + CoA.

Subcellular location

Early endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein Ref.6 Ref.7.

Domain

The DHHC domain is required for palmitoyltransferase activity.

Miscellaneous

Present with 4072 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the DHHC palmitoyltransferase family. AKR/ZDHHC17 subfamily.

Contains 6 ANK repeats.

Contains 1 DHHC-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YCK1P232913EBI-2421,EBI-4718

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 764764Palmitoyltransferase AKR1
PRO_0000212934

Regions

Topological domain1 – 321321Cytoplasmic Ref.10 Ref.11
Transmembrane322 – 34120Helical; Potential
Topological domain342 – 3465Lumenal Ref.10 Ref.11
Transmembrane347 – 36418Helical; Potential
Topological domain365 – 38420Cytoplasmic Ref.10 Ref.11
Transmembrane385 – 40521Helical; Potential
Topological domain406 – 41813Lumenal Ref.10 Ref.11
Transmembrane419 – 43921Helical; Potential
Topological domain440 – 51374Cytoplasmic Ref.10 Ref.11
Transmembrane514 – 53421Helical; Potential
Topological domain535 – 57036Lumenal Ref.10 Ref.11
Transmembrane571 – 59121Helical; Potential
Topological domain592 – 764173Cytoplasmic Ref.10 Ref.11
Repeat72 – 10231ANK 1
Repeat108 – 13730ANK 2
Repeat142 – 17130ANK 3
Repeat175 – 20430ANK 4
Repeat213 – 24230ANK 5
Repeat246 – 27530ANK 6
Zinc finger470 – 52051DHHC-type

Sites

Active site5001S-palmitoyl cysteine intermediate Probable

Amino acid modifications

Modified residue511Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15
Modified residue571Phosphoserine Ref.12 Ref.14 Ref.15

Experimental info

Mutagenesis497 – 4982DH → AA: Abolishes YCK2 palmitoylation. Ref.6
Mutagenesis5001C → A: Abolishes YCK2 palmitoylation. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P39010 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 9C9759F0140CE3F6

FASTA76485,840
        10         20         30         40         50         60 
MVNELENVPR ASTLTNEEQT VDPSNNDSQE DISLGDSNEI TSLASLKAIR SGNEEESGNE 

        70         80         90        100        110        120 
QVNHNDEAEE DPLLTRYHTA CQRGDLATVK EMIHGKLLEV NNDGDSTEHI TGLHWASINN 

       130        140        150        160        170        180 
RLSVVDFLVS QGADVNARAG ALHATPLHWA ARYGYVYIVD FLLKHGADPT MTDDQGFNLL 

       190        200        210        220        230        240 
HLSVNSSNIM LVLYVLFNVV SKGLLDIDCR DPKGRTSLLW AAYQGDSLTV AELLKFGASI 

       250        260        270        280        290        300 
KIADTEGFTP LHWGTVKGQP HVLKYLIQDG ADFFQKTDTG KDCFAIAQEM NTVYSLREAL 

       310        320        330        340        350        360 
THSGFDYHGY PIKKWFKKSQ HAKLVTFITP FLFLGIAFAL FSHINPLFVI IVLFLLAIAT 

       370        380        390        400        410        420 
NKGLNKFVLP SYGRMGVHNV TLLRSPLLSG VFFGTLLWVT IVWFFKVMPR TFSDEQYTNI 

       430        440        450        460        470        480 
LMLVILVSVF YLFGQLVIMD PGCLPEETDH ENVRQTISNL LEIGKFDTKN FCIETWIRKP 

       490        500        510        520        530        540 
LRSKFSPLNN AVVARFDHYC PWIFNDVGLK NHKAFIFFIT LMESGIFTFL ALCLEYFDEL 

       550        560        570        580        590        600 
EDAHEDTSQK NGKCFILGAS DLCSGLIYDR FVFLILLWAL LQSIWVASLI FVQAFQICKG 

       610        620        630        640        650        660 
MTNTEFNVLM KESKSIGPDG LSFNENFNTT PEGFAPSIDP GEESNDTVLA PVPGSTIRKP 

       670        680        690        700        710        720 
RTCFGVCYAV TGMDQWLAVI KETIGIKDST GHNVYSITSR IPTNYGWKRN VKDFWLTSDI 

       730        740        750        760 
NAPLWRRILY PPSGSKALLN GIEVDYFKLY KLPNKDVEQG NDMV

« Hide

References

« Hide 'large scale' references
[1]"Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae."
Kao L.-R., Peterson J., Ji R., Bender L., Bender A.
Mol. Cell. Biol. 16:168-178(1996) [PubMed: 8524293] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"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. expand/collapse author list , 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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors."
Givan S.A., Sprague G.F. Jr.
Mol. Biol. Cell 8:1317-1327(1997) [PubMed: 9243510] [Abstract]
Cited for: FUNCTION.
[5]"Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane."
Feng Y., Davis N.G.
Mol. Cell. Biol. 20:5350-5359(2000) [PubMed: 10866691] [Abstract]
Cited for: FUNCTION.
[6]"The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase."
Roth A.F., Feng Y., Chen L., Davis N.G.
J. Cell Biol. 159:23-28(2002) [PubMed: 12370247] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIVE SITE, MUTAGENESIS OF 497-ASP--HIS-498 AND CYS-500.
[7]"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: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Akr1p-dependent palmitoylation of Yck2p yeast casein kinase 1 is necessary and sufficient for plasma membrane targeting."
Babu P., Deschenes R.J., Robinson L.C.
J. Biol. Chem. 279:27138-27147(2004) [PubMed: 15105419] [Abstract]
Cited for: FUNCTION.
[10]"Transmembrane topology of the protein palmitoyl transferase Akr1."
Politis E.G., Roth A.F., Davis N.G.
J. Biol. Chem. 280:10156-10163(2005) [PubMed: 15632165] [Abstract]
Cited for: TOPOLOGY.
[11]"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: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[12]"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: 17330950] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, MASS SPECTROMETRY.
Strain: ADR376.
[13]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, MASS SPECTROMETRY.
[14]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, MASS SPECTROMETRY.
[15]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-57, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L31407 Genomic DNA. Translation: AAC41676.1.
U51030 Genomic DNA. Translation: AAB64454.1.
Z70202 Genomic DNA. Translation: CAA94103.1.
Z68290 Genomic DNA. Translation: CAA92582.1.
BK006938 Genomic DNA. Translation: DAA12108.1.
PIRS48521.
RefSeqNP_010550.1. NM_001180572.1.

3D structure databases

ProteinModelPortalP39010.
SMRP39010. Positions 72-307.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1145N.
IntActP39010. 46 interactions.
MINTMINT-544657.
STRINGP39010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR264C; YDR264C; YDR264C.
GeneID851857.
KEGGsce:YDR264C.
NMPDRfig|4932.3.peg.1312.

Organism-specific databases

CYGDYDR264c.
SGDS000002672. AKR1.

Phylogenomic databases

eggNOGfuNOG05713.
GeneTreeEFGT00070000008731.
HOGENOMHBG395499.
OMALEYFDEL.
OrthoDBEOG4K3Q4F.

Gene expression databases

ArrayExpressP39010.
GenevestigatorP39010.
GermOnlineYDR264C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001594. Znf_DHHC_palmitoyltrfase.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
KOK06867.
PfamPF00023. Ank. 3 hits.
PF01529. zf-DHHC. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. ANK. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS50216. ZF_DHHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969791.

Entry information

Entry nameAKR1_YEAST
AccessionPrimary (citable) accession number: P39010
Secondary accession number(s): D6VSP8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 14, 2011
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents