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 25-MAY-2022, entry version 125.
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 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC 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., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., 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, Rhea:RHEA-
CC 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 membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR EMBL; CR380959; CAG62700.1; -; Genomic_DNA.
DR RefSeq; XP_449724.1; XM_449724.1.
DR AlphaFoldDB; Q6FJ70; -.
DR SMR; Q6FJ70; -.
DR STRING; 5478.XP_449724.1; -.
DR PRIDE; Q6FJ70; -.
DR EnsemblFungi; CAG62700; CAG62700; CAGL0M08712g.
DR GeneID; 2891285; -.
DR KEGG; cgr:CAGL0M08712g; -.
DR CGD; CAL0137231; CAGL0M08712g.
DR VEuPathDB; FungiDB:CAGL0M08712g; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; Q6FJ70; -.
DR OMA; DVPDCNG; -.
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 Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
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;
KW Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Repeat; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..763
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212920"
FT TOPO_DOM 1..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..401
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..546
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 57..87
FT /note="ANK 1"
FT REPEAT 92..121
FT /note="ANK 2"
FT REPEAT 126..155
FT /note="ANK 3"
FT REPEAT 159..188
FT /note="ANK 4"
FT REPEAT 197..226
FT /note="ANK 5"
FT REPEAT 230..259
FT /note="ANK 6"
FT REPEAT 292..322
FT /note="ANK 7"
FT DOMAIN 454..504
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="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
