ID   AKR1_MORAP              Reviewed;         559 AA.
AC   Q9UVH3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Palmitoyltransferase AKR1;
DE            EC=2.3.1.225;
DE   AltName: Full=Ankyrin repeat-containing protein AKR1;
DE   Flags: Fragment;
OS   Mortierella alpina (Oleaginous fungus) (Mortierella renispora).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX   NCBI_TaxID=64518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 32222 / CBS 528.72 / M136;
RX   PubMed=12055292; DOI=10.1099/00221287-148-6-1725;
RA   MacKenzie D.A., Carter A.T., Wongwathanarat P., Eagles J., Salt J.,
RA   Archer D.B.;
RT   "A third fatty acid delta9-desaturase from Mortierella alpina with a
RT   different substrate specificity to ole1p and ole2p.";
RL   Microbiology 148:1725-1735(2002).
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; AJ249747; CAB56510.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9UVH3; -.
DR   SMR; Q9UVH3; -.
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; 3.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; ANK repeat; Endosome; Golgi apparatus; Lipoprotein;
KW   Membrane; Palmitate; Repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           <1..559
FT                   /note="Palmitoyltransferase AKR1"
FT                   /id="PRO_0000212926"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          8..38
FT                   /note="ANK 1"
FT   REPEAT          42..71
FT                   /note="ANK 2"
FT   REPEAT          75..104
FT                   /note="ANK 3"
FT   DOMAIN          272..322
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        302
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   559 AA;  62823 MW;  3394522A78C149F2 CRC64;
     DPMLQDSQGF NALHLATHSS NAMLVLYLLM AGEMPVDTAD TLGHTSLMWA AYQGDSLSVQ
     ILLKHGARVD TKDREGFTPL HWAVVKGNRE CLSKILMAGA DIKAGDKSGK TPVDMIKELK
     GTMIWDKALS DAKLSSDGQT RRTPFDKLMV LFPWYIALPL AVAQFLFGHI GAIKFLLRTR
     TPNDMLQTPY YTAVFQSTAF WVGFVWLRYL LGNTSHLLWM NIAFFVGYTS ALYFFYGAVM
     ADPGWTKANS SYESQREAVV QMADRGLLDA RHFCVSCIAQ RPLRSKHCKF CNRCVAKFDH
     HCPWIYNCIG AKNHRAFLIF LALFLSSVPI YAYLSFEYLH VLSPSYVPVS SDPCLLGDTL
     CGYFQYDAFT TTLAFWSLFQ MTWPGLLFLV QLYQVGQAKT TNEAMNFQRH SYLGKSMTIR
     QRILRSLTEI DSEMAGAGHP LQEESINLLE ANGTATNDED EVTLFAQEES KPVGFGDHEG
     HNHGARRAGG GGMWNLLVGT ARRRRQQGED RDVNPFDFGL WQNCVGFWSD GTQGPMRGVN
     WYSFYEAEAR GGAATSRRM