AKR1_KLULA
ID AKR1_KLULA Reviewed; 752 AA.
AC Q875M2; Q6CMY6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=KLLA0E16764g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76492 / CBS 2359/152 / CLIB 210;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; AY145047; AAO32609.1; -; Genomic_DNA.
DR EMBL; CR382125; CAG99790.1; -; Genomic_DNA.
DR RefSeq; XP_454703.1; XM_454703.1.
DR AlphaFoldDB; Q875M2; -.
DR SMR; Q875M2; -.
DR STRING; 28985.XP_454703.1; -.
DR EnsemblFungi; CAG99790; CAG99790; KLLA0_E16721g.
DR GeneID; 2893937; -.
DR KEGG; kla:KLLA0_E16721g; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; Q875M2; -.
DR OMA; PWMAGIF; -.
DR Proteomes; UP000000598; 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; PF12796; Ank_2; 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; 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..752
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212925"
FT TOPO_DOM 1..318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 340..341
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..380
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 402..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..567
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 568..588
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 589..752
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 72..102
FT /note="ANK 1"
FT REPEAT 108..137
FT /note="ANK 2"
FT REPEAT 142..171
FT /note="ANK 3"
FT REPEAT 175..208
FT /note="ANK 4"
FT REPEAT 212..241
FT /note="ANK 5"
FT REPEAT 245..274
FT /note="ANK 6"
FT DOMAIN 466..516
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 496
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 752 AA; 84940 MW; 168A92D30C723DDD CRC64;
MTAEEVDKES DPAIEDVKSD YDAIELGNEN ENENEVVSLD SMKAVISRAS SELKHENDQG
EERDLGSVEK DPILERYHAA CKQGDMKTLR EMVESKVIDL SNDYDPKERV SGLHWACINN
RLSAVKYLAG AGAEVNFKGG ELDATPLHWA SKSGLVYIVD ELLKAGADPN ITDSQGYNLL
HTSVFSSNIM LVIYVLFFVV DGKEDVDQPD PHQRTALQWA TYQADALTVE NLLKFNADVK
NADDAGFTAL HWGTVKGSIP VMDLLIKHGS DFFQTTNDGK NCFTIGKELY SIGSLEASLY
KNGFDKNGFP LPQYFSASTG KMLTFFLPWV LIPLVFYIFS KITFFIALLI NTIVLVISGL
VLSRLVVPSY LLSKRHPILN SPLLAGILSG TIAIAFFIWF TKISILTFTE KPVGNIIMLG
FFIGLITLFI GLMKSDPGYI PGTVDHDKVR ETIKELLSLG KFDAKHFCVH TWIRIPLRSK
YDRDSACLIS AFDHFCPWVY NQIGLLNHKL FYMFVVLLEI SVWWFLPLMM EYFDELEDYL
ENRKGKHFGD CHFLGDEDLC FGLHHDTFNF LLLCWVIFQA FWVLCLIAVQ TVQMLKGVTD
YEFVQINKKL KSNGTTTEDI FSSTPPELMS EELIAELDAP ALDPRQVPQR TCFTVCCTLL
GLDKLVTMIK SVLRLKSDEP SSRSSHLSAL ARIPTDYGWK QNLKDFWLLP DTSSPLWRRI
LLPPKDSHAL LNGMEVDYYT LYTLPNATEE LV
