AKR1_YARLI
ID AKR1_YARLI Reviewed; 702 AA.
AC Q6C520;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=YALI0E21780g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382131; CAG79837.1; -; Genomic_DNA.
DR RefSeq; XP_504242.1; XM_504242.1.
DR AlphaFoldDB; Q6C520; -.
DR SMR; Q6C520; -.
DR STRING; 4952.CAG79837; -.
DR EnsemblFungi; CAG79837; CAG79837; YALI0_E21780g.
DR GeneID; 2911956; -.
DR KEGG; yli:YALI0E21780g; -.
DR VEuPathDB; FungiDB:YALI0_E21780g; -.
DR HOGENOM; CLU_012510_1_0_1; -.
DR InParanoid; Q6C520; -.
DR OMA; PWMAGIF; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
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; PF13637; Ank_4; 1.
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; 5.
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..702
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212933"
FT TOPO_DOM 1..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..320
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..379
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..518
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 49..80
FT /note="ANK 1"
FT REPEAT 83..112
FT /note="ANK 2"
FT REPEAT 117..147
FT /note="ANK 3"
FT REPEAT 150..179
FT /note="ANK 4"
FT REPEAT 183..212
FT /note="ANK 5"
FT REPEAT 216..245
FT /note="ANK 6"
FT DOMAIN 436..486
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 702 AA; 77430 MW; D8591EE783B9529B CRC64;
MSTDAELQTI SGLSVASKSA PSTQTEGVTA SGKVESTTNA EEATSDVEEE ENPLVVAARD
GNTAEVKRLC ESGSYSVLDT AEDGVTALHW AAVNNRISTC QYLVEQGAVV DAKGGQLNGT
PLHWACRRGL VYIVHYLIQN GADPLRSDVQ GYNALHLATH SSNVMLLVYL LHQGLPVDCQ
DPNGRTALHW AAYQGDALSV DVLLRWGSDV KITDTQGFLP LHWGIVNGSR NSLARLIEEG
SDMYAKSSDG KTPHVMAAEM NTTAQLEGAL DDCGRFPDGS QKTKYFDART TNLLCFFTPF
ILILLGLVLC TFCGPIFGII LTVATLFGSI KLLKTLVLPS LYNGHAALLK SPFQAGIFTG
SAFWVTVKYL TSVLPATFAS HPILNFFFAS IFGLAMYCFF RCMSMDPGYI PKLSGITEQK
EVIETLIERG EFDTRHFCFV TYVRKPLRSK FCRQSKRVVA RFDHFCPWVW NAIGVRNHRM
FVLYVLFLQI GIPLWLALNS AYFGELLEIK RWDPLEFYLV IWISLQLIWI TFLSFVQIFQ
ICRSLTTSEA VNLQKYGYMG ADDYSSVPLD HSAATASAKS VMNAHGHAAK SPCFSSVLKL
LGVDQFVATA GEAIKHRDNR SWKEKNPTDS GAGTNCFDFW FPNGKFDLLA VFEAGKGGGA
IGGHAVDYYK LWDFPDVSPN QQQTNNRSTR EDGEALLAES QV
