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AKR1_ASHGO
ID   AKR1_ASHGO              Reviewed;         724 AA.
AC   Q755Y0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Palmitoyltransferase AKR1;
DE            EC=2.3.1.225;
DE   AltName: Full=Ankyrin repeat-containing protein AKR1;
GN   Name=AKR1; OrderedLocusNames=AER388C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016818; AAS53067.1; -; Genomic_DNA.
DR   RefSeq; NP_985243.1; NM_210597.1.
DR   AlphaFoldDB; Q755Y0; -.
DR   SMR; Q755Y0; -.
DR   STRING; 33169.AAS53067; -.
DR   EnsemblFungi; AAS53067; AAS53067; AGOS_AER388C.
DR   GeneID; 4621459; -.
DR   KEGG; ago:AGOS_AER388C; -.
DR   eggNOG; KOG0509; Eukaryota.
DR   HOGENOM; CLU_012510_1_1_1; -.
DR   InParanoid; Q755Y0; -.
DR   OMA; PWMAGIF; -.
DR   Proteomes; UP000000591; Chromosome V.
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:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:EnsemblFungi.
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:0090029; P:negative regulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR   GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
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; -; 3.
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; 5.
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..724
FT                   /note="Palmitoyltransferase AKR1"
FT                   /id="PRO_0000212916"
FT   TOPO_DOM        1..308
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        330..331
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        353..360
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        382..392
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        393..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        414..489
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        490..510
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        511..543
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..724
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          54..84
FT                   /note="ANK 1"
FT   REPEAT          90..119
FT                   /note="ANK 2"
FT   REPEAT          124..153
FT                   /note="ANK 3"
FT   REPEAT          157..187
FT                   /note="ANK 4"
FT   REPEAT          191..220
FT                   /note="ANK 5"
FT   REPEAT          224..253
FT                   /note="ANK 6"
FT   DOMAIN          446..496
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        476
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   724 AA;  81922 MW;  C5C5BBB4D272A99C CRC64;
     MSGQLNVAED SVLLDDISIS SIQPIVSDVP AAEDVGDEDH ISGASIAENR PKDPTLVKYH
     AACQRGDLKT VKDMIEAGVI DVKADWDEEE QVSGLHWASA NNRLNLVRYL IAQGADVNIK
     GGDLEATPLH WASKSGYVYI VHCLLEHGAD PLITDRQGYN LLHTSTFSSE VMLITYVLFT
     GQIPVDSPDP TGKTALHWAA YQGDPNTVEA LLKFDADVRV VDTGGFTPLH WATVKGHPHV
     LKALIEHGSD VFLKNNDGKN ALMIAQEMNT QKALQNALYE CGFNKDGFAI RKYFKNPMHA
     KMVTFFTPWL ILGLILSFFA YFSILLAILG CLLTVLAAGY GLYNFVFPSF ILMKRIVIFK
     TPLLAGILSG TIFWLLYVWL FKMLPATFDD EPILNLTVFA LFAGVVFLLT KLLQSDPGYI
     VPATDHNQIR ATIIELLRVG KYDSKHFCIH SWIRLPLRAK YKRFVHSVIL RYDHYCPWIY
     NYIGFRNHKI FIYFILLLDL GILALAKLCL EYFDELKDHA KNKDALKCSI LSKDLCAGFT
     YDPFTLFLLE WVCVQGMWIL ALSFVQFFEC LKGVTEHEFA HWQRRNRGVV GREHVFNTAP
     EELMEEDPEE ERNKLRSLGA AGQRHCCSTL TTATGFDRFL SVIGSSLGRQ PRTTHNPINY
     PIETDYGWKQ NLKDFWLTSD ISAPMWRRIL LPPVGTRGLL NGQEVDYQKL YNLPERVISI
     EEIV
 
 
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