(data stored in ACNUC8465 zone)

SWISSPROT: AKR1_CANGA

ID   AKR1_CANGA              Reviewed;         763 AA.
AC   Q6FJ70;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 114.
DE   RecName: Full=Palmitoyltransferase AKR1;
DE            EC=2.3.1.225;
DE   AltName: Full=Ankyrin repeat-containing protein AKR1;
GN   Name=AKR1; OrderedLocusNames=CAGL0M08712g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Palmitoyltransferase specific for casein kinase 1.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Multi-pass membrane
CC       protein. Golgi apparatus membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       AKR/ZDHHC17 subfamily. {ECO:0000305}.
DR   EMBL; CR380959; CAG62700.1; -; Genomic_DNA.
DR   RefSeq; XP_449724.1; XM_449724.1.
DR   SMR; Q6FJ70; -.
DR   STRING; 5478.XP_449724.1; -.
DR   EnsemblFungi; CAG62700; CAG62700; CAGL0M08712g.
DR   GeneID; 2891285; -.
DR   KEGG; cgr:CAGL0M08712g; -.
DR   CGD; CAL0137231; CAGL0M08712g.
DR   EuPathDB; FungiDB:CAGL0M08712g; -.
DR   eggNOG; KOG0509; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   eggNOG; COG5273; LUCA.
DR   HOGENOM; HOG000033883; -.
DR   InParanoid; Q6FJ70; -.
DR   KO; K20032; -.
DR   OMA; QCRNHSH; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:EnsemblFungi.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0018345; P:protein palmitoylation; IEA:EnsemblFungi.
DR   GO; GO:0006612; P:protein targeting to membrane; IEA:EnsemblFungi.
DR   GO; GO:0030100; P:regulation of endocytosis; IEA:EnsemblFungi.
DR   CDD; cd00204; ANK; 2.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF01529; DHHC; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6FJ70.
DR   SWISS-2DPAGE; Q6FJ70.
KW   Acyltransferase; ANK repeat; Complete proteome; Endosome;
KW   Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Repeat; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    763       Palmitoyltransferase AKR1.
FT                                /FTId=PRO_0000212920.
FT   TOPO_DOM      1    307       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    308    325       Helical. {ECO:0000255}.
FT   TOPO_DOM    326    330       Lumenal. {ECO:0000255}.
FT   TRANSMEM    331    348       Helical. {ECO:0000255}.
FT   TOPO_DOM    349    368       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    369    389       Helical. {ECO:0000255}.
FT   TOPO_DOM    390    401       Lumenal. {ECO:0000255}.
FT   TRANSMEM    402    422       Helical. {ECO:0000255}.
FT   TOPO_DOM    423    497       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    498    518       Helical. {ECO:0000255}.
FT   TOPO_DOM    519    546       Lumenal. {ECO:0000255}.
FT   TRANSMEM    547    567       Helical. {ECO:0000255}.
FT   TOPO_DOM    568    763       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       57     87       ANK 1.
FT   REPEAT       92    121       ANK 2.
FT   REPEAT      126    155       ANK 3.
FT   REPEAT      159    188       ANK 4.
FT   REPEAT      197    226       ANK 5.
FT   REPEAT      230    259       ANK 6.
FT   REPEAT      292    322       ANK 7.
FT   DOMAIN      454    504       DHHC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00067}.
FT   ACT_SITE    484    484       S-palmitoyl cysteine intermediate.
FT                                {ECO:0000250}.
SQ   SEQUENCE   763 AA;  85540 MW;  E5A42F43026BEA59 CRC64;
     MEDNSEQASV SSQASMRPLV SDNGDREAGA GVEVNIANDN DTSVGVDGEN GNEDDDPILS
     KYHNACQRGD LEVVREMIHG GQVNVSSDAD REGVTGLHWA AINNRLNVVD FLVREGANVE
     SKAGALEATP LHWAARYGFV YVVDYLLQHG ASATTTDKQG FNLLHLSVNS SNIMLVVYVL
     FFVVSKGIID IDYVDPKGRT ALLWAAYQGD SLTVAALIKF NASVKIADEG GFTPLHWGTV
     KGQPHVLKYL IQDGADFFQK TNDNKDCFVI AEEMSNTHSF QEALRHNNFD KNGYPINKLV
     KRDDHAKIIT FLIPLLVLGF AFFGFSHLHI LFALPVIILL LLASNKFIKS FLLPSYETKG
     TNSASLLKSP LIAGILFGSI FWLAFVWILR ILPYTFTKRP LGNLTFCAIL CFVCYSLFLL
     AFSDPGHIGS ENDHEKIRET ISNLLKEGKF DTRSFCLETW VRKPLRSKYS YLNDALILRF
     DHYCPWIYND VGLKNHKLFI FFILALELGI FSFVKVCLKY FDELDMDGDC FILGDDDLCS
     GLIGDRFTFL IMTWACIQAV WIFSLVIVQL FQITKGLTNS ELNALIREGR RVDIDSQTHN
     EFFNTVPEGF INNKDTEEEA APPVRNNTNE RISTTFSGNL PKPRTCMGMI CAVTGLHQCV
     AIIKDTFGIA RHGSSRSTNT RSLLSSISTD YGWRRNWCDF WLLSDTNTPL WKRIFFSPPS
     TKALLNGKEA DYATLYEVPN KNHGSVSQLQ ELQDPLSEID DMV
//

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