Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q12013 (AKR2_YEAST)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable palmitoyltransferase AKR2
    EC=2.3.1.-
Alternative name(s):
    Ankyrin repeat-containing protein AKR2
Gene names
Name: AKR2
Ordered Locus Names: YOR034C
ORF Names: OR26.25
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in constitutive endocytosis of a-factor receptor STE3. Ref.2

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein.

Domain

The DHHC domain is required for palmitoyltransferase activity By similarity.

Miscellaneous

Present with 815 molecules/cell in log phase SD medium. Ref.4

Sequence similarities

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

Contains 6 ANK repeats.

Contains 1 DHHC-type zinc finger.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Ontologies

Keywords
   Cellular componentMembrane
   DomainANK repeat
Repeat
Transmembrane
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionAcyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionacyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LCB4Q122461EBI-34438,EBI-38830
YPT35P388151EBI-34438,EBI-24665

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Probable palmitoyltransferase AKR2
PRO_0000212936

Regions

Topological domain1 – 306306Cytoplasmic Potential
Transmembrane307 – 32721 Potential
Transmembrane328 – 34821 Potential
Topological domain349 – 36012Cytoplasmic Potential
Transmembrane361 – 38121 Potential
Topological domain382 – 39211Extracellular Potential
Transmembrane393 – 41321 Potential
Topological domain414 – 48976Cytoplasmic Potential
Transmembrane490 – 51021 Potential
Topological domain511 – 54636Extracellular Potential
Transmembrane547 – 56721 Potential
Topological domain568 – 749182Cytoplasmic Potential
Repeat49 – 7931ANK 1
Repeat83 – 11230ANK 2
Repeat117 – 14630ANK 3
Repeat150 – 18334ANK 4
Repeat189 – 21830ANK 5
Repeat222 – 25130ANK 6
Zinc finger446 – 49651DHHC-type

Sites

Active site4761S-palmitoyl cysteine intermediate By similarity

Amino acid modifications

Glycosylation5341N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q12013-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 887F5A02B9EE030A

FASTA74985,236
        10         20         30         40         50         60 
MTSMSIIDDE NVKKTSNGAA VVTDVAQHAV SDSDNNKAQL LGDGSNTEYV VDIFIEAAKD 

        70         80         90        100        110        120 
GDLKVVKDVV ESGAVDINND RIDELSGLHW ACINNRFSVA KFLLLRGANP NQAAGPGGAT 

       130        140        150        160        170        180 
ALHWAARYGN IYIVDLLLKH GADPTLKDEQ GLNIMHFSVY SSNILLVVYV LYFVVNNNDN 

       190        200        210        220        230        240 
VDIDSKDNNN RTPLLWAAYQ GDFLTVELLL KFGSTVAWTD NRGFNALHCA LVGGDQRVIC 

       250        260        270        280        290        300 
DLILSGANFY ERNNQKQDCF DLAEGMGTKS LFEQALQHHG YDRLGNQKDK LFKKSSHAQF 

       310        320        330        340        350        360 
TIFLSPFLLM VYIYLISLVL SPVLAIMLSL LVTVVMVNTL KKFVLPCLPR KNTYKVSLTR 

       370        380        390        400        410        420 
TPFFSGLFLS TFCFLIYIWT KKLYPYSVSD YTMKNVQFLV TSFLTVVLFL RLVRSDPGCL 

       430        440        450        460        470        480 
KTDDSLTSIQ ETIKQLIDLG KFDRENFCVE TLERKPLRSK YSFFSGALVA RYDHYCPWIY 

       490        500        510        520        530        540 
NDVGLKNHKL FVFFAVTVQY HMFLFMWLCL AYFKKTNYIY EQVEEYARCA LLKNETLCKG 

       550        560        570        580        590        600 
SNYDPSTFFL FIWISVNFIW LGAMLIVQFF QILKGITTPE LFILIKEEHK AKFINLIPFE 

       610        620        630        640        650        660 
NSIYTSESKG VEDSDMIPEG PSATTITHTI SIDGLEPRNR RRAILSACFS MMGINQWLVT 

       670        680        690        700        710        720 
IKEIVGITHI LHGQVPQQHH SSLLRSFLVT NHWKTNLTDF WLNSDVTAPL WQRFFYSSDT 

       730        740 
SKAMLGGTEV DYYELYEYPA REGEVLRPN 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"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.
[3]"Sequencing and comparison of yeast species to identify genes and regulatory elements."
Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
Nature 423:241-254(2003) [PubMed: 12748633] [Abstract]
Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
[4]"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].
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

X87331 Genomic DNA. Translation: CAA60751.1.
Z74942 Genomic DNA. Translation: CAA99224.1.
PIRS62171.
RefSeqNP_014677.1.

3D structure databases

HSSPHSSP built from PDB template 1SW6 based on UniProtKB P09959.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1882N.
IntActQ12013. 8 interactions.

Genome annotation databases

EnsemblYOR034C. Saccharomyces cerevisiae. [Contig view]
GeneID854199.
GenomeReviewsGene locus YOR034C in contig Y13140_GR.
KEGGsce:YOR034C.
NMPDRfig|4932.3.peg.5776.

Organism-specific databases

CYGDYOR034c.
SGDS000005560. AKR2.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ12013.
OMAQ12013. TITHTIS.

Gene expression databases

ArrayExpressQ12013.
GermOnlineYOR034C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002110. ANK.
IPR001594. Znf_DHHC.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 4 hits.
PF01529. zf-DHHC. 1 hit.
[Graphical view]
ProDomPD003041. Znf_DHHC. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00248. ANK. 6 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS50216. ZF_DHHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio976032.

Entry information

Entry nameAKR2_YEAST
AccessionPrimary (citable) accession number: Q12013
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents