AKR1_NAUCC
ID AKR1_NAUCC Reviewed; 757 AA.
AC Q876A6; G0VDF6; Q876A7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=NCAS_0C05280;
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-156 AND 172-757.
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
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).
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; HE576754; CCC69518.1; -; Genomic_DNA.
DR EMBL; AY144909; AAO32473.1; -; Genomic_DNA.
DR EMBL; AY144908; AAO32472.1; -; Genomic_DNA.
DR RefSeq; XP_003675882.1; XM_003675834.1.
DR AlphaFoldDB; Q876A6; -.
DR SMR; Q876A6; -.
DR STRING; 1064592.Q876A6; -.
DR EnsemblFungi; CCC69518; CCC69518; NCAS_0C05280.
DR GeneID; 11527817; -.
DR KEGG; ncs:NCAS_0C05280; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; Q876A6; -.
DR OMA; PWMAGIF; -.
DR OrthoDB; 445686at2759; -.
DR Proteomes; UP000001640; Chromosome 3.
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; 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..757
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212929"
FT TOPO_DOM 1..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..331
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..375
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..402
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..550
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 58..88
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 DOMAIN 455..505
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 485
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT CONFLICT 172..185
FT /note="NVMLVAYVLFFVVA -> EVHVVEFLLPVLFF (in Ref. 1;
FT AAO32472)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 85371 MW; 2E864259817B0C41 CRC64;
MSDINTESGE STSLPNSTDP PLSDVNIDVE DDDTAESISS LQPIVSNTTN PPEEPINPVL
GQYHQACQKG DLATVKQLLD SGVLDLNTDL TGDITGLHWA SINNRLSVVK YLISQGIDVN
AKAGDLEATP LHWAARYGYV HIVDCLLNKG ADPTMCDMQG FNLLHLAVNS SNVMLVAYVL
FFVVAKGIID IDCQDPKGRT PLLWAAYQGD SLSVMLLLKF GASTKIVDEG GFTPLHWATV
KGQPYVLTHL IRDGADFFLK TNDGKDCFTI AQEMNTSHSF KDALSICGFN QDGYPKRKLF
KKSDHAKVIT FFVPLVALSI IFILFTHLHP LFALLISLIF GLAVNKALKE LILPSYSNYG
LHSTSLLKSP FLSGTFFGSL LLLTIVWIFK IAPFTIFKSR LLTNFFMFLI LMQIYYLFIK
LIFSDPGCVP IETDHENVRG TIKELLDTGK FDIKNFCLET WIRKPLRSHF STLNTHNVAR
FDHFCPWIYN DIGLKNHKNF MWFILLTEVG IWFFISLTMK YFDILEDTNE DVACFLLGDD
ELCAGFVYDR FTFLIALWAL IQSVWVGFLI VVQVFQTFTG VTNKEFNKYV KEKKNQHAFD
PIFFNDTFNT TPEELRNDDD DTAASRTGNN PNHSNGTTIP SEGSRINTRK PRTCFNLCFA
ITGLDQVRTI VRETLGIGGA NEMSRMQLLS SIPTNYGWKR NLADFWLTSD VMAPIWRRLF
YSPVESRALL NGVEVDYFKL YDFPEKTYPE PTGPESV
