AKR1_DEBHA
ID AKR1_DEBHA Reviewed; 821 AA.
AC Q6BP80;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=DEHA2E15796g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88243.2; -; Genomic_DNA.
DR RefSeq; XP_459990.2; XM_459990.1.
DR AlphaFoldDB; Q6BP80; -.
DR SMR; Q6BP80; -.
DR STRING; 4959.XP_459990.2; -.
DR PRIDE; Q6BP80; -.
DR EnsemblFungi; CAG88243; CAG88243; DEHA2E15796g.
DR GeneID; 2902136; -.
DR KEGG; dha:DEHA2E15796g; -.
DR VEuPathDB; FungiDB:DEHA2E15796g; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; Q6BP80; -.
DR OMA; WFIAYLL; -.
DR OrthoDB; 445686at2759; -.
DR Proteomes; UP000000599; Chromosome E.
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:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
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; PF00023; Ank; 1.
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; 3.
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..821
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212922"
FT TOPO_DOM 1..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..494
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 611..650
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..671
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 142..172
FT /note="ANK 1"
FT REPEAT 176..205
FT /note="ANK 2"
FT REPEAT 213..243
FT /note="ANK 3"
FT REPEAT 247..277
FT /note="ANK 4"
FT REPEAT 289..318
FT /note="ANK 5"
FT REPEAT 322..351
FT /note="ANK 6"
FT DOMAIN 546..596
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 576
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 821 AA; 93243 MW; 3F61697BE02D56DB CRC64;
MVDKDANNEL DSIPLVSEQV TNGENGELNI KASESTVGSN GAVADHEESE TNNQTAVDNT
ENDTLDKDKL DAQPNHNEQQ READLSDAFS VKIQDESVND KTSEPDENKD TASRKSMDGI
LNLSENNLDA TKPEASEQEL NPSLHNLMSA CQQGDLTKVS ELISNGEVKA NDTFSDGITA
LHWAAINNRL TIVKYLIEND HSKADPNLLG GELKASPLHW ACRNGLVYIV DYFIVHTDAD
PTLRDSQSYN ALHLAVHSSN ITLIIYLLLS CCGSTSTSKQ LYVDESDNCD RTSLHWAAYQ
GDLLTINALL KFGADVSKID KNLFIPLHWA FMKGYKTVLK VLAGAGSNIF AKNDQGKDSF
EVAKDMNCYD TWIKVLKECG RNPKNHWEMK TIYLNPKIGK LVTFFTPYII LPIMFQVCSF
YNGFVIPKLF FSVVLFAGSI YILQKLVIPT YLAEEKAIPK SPLLAGIFSG TAFWCIVTWA
FNIIPTLLFK KFISNLVLSA FIYLFVWSFF KAMFINPGYV PVPSDNSVTL DQVKDLIKIG
RFDTDNFCVN TFVRKPLRSK YSRFNKKLIA RFDHYCPWVY NDIGVRNHKL FVVFVYSLNL
AVLLFTHLSI KLFKNTEKMS GYDSDDESQK CWLLSDELCV GYKSHHFQFN LMLWCLIQYI
WIAFLCLVQT FQILKGLTTW EFSSLNNRLQ THNGYNHSTL PKDFDLTSSN TNRYNSPKQS
NGLSICLKLI GLDQVVLAIK LGIKSIFSHT SSVETYDPLN EFEIPTDYGF RTNWLDFWFI
GDIEWRNIFY LPIEGENNLN RTVVDYYKLY EYPPKLADVD A
