AKR1_LACK1
ID AKR1_LACK1 Reviewed; 737 AA.
AC Q875S9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1;
OS Lachancea kluyveri (strain ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 /
OS JCM 7257 / NCYC 543 / NRRL Y-12651) (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=226302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 58438 / CBS 3082 / BCRC 21498 / NBRC 1685 / JCM 7257 / NCYC 543
RC / NRRL Y-12651;
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; AY144990; AAO32553.1; -; Genomic_DNA.
DR AlphaFoldDB; Q875S9; -.
DR SMR; Q875S9; -.
DR PRIDE; Q875S9; -.
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; -; 2.
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; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..737
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212930"
FT TOPO_DOM 1..304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..396
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..493
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..547
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..737
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..190
FT /note="ANK 4"
FT REPEAT 194..223
FT /note="ANK 5"
FT REPEAT 227..256
FT /note="ANK 6"
FT DOMAIN 450..500
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 480
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 737 AA; 84025 MW; 7F0840F1819445F5 CRC64;
MKQIDSEDSI TVPNDTPEDN SASSMQPVMS NLSIEEHQSE NEPIEQEQAD AKDPLLSKYH
LACQQGDLAT VKEIIENGVI DLKHDYDDVE RVSGLHWASI NNRLSVVRYL ISKDVDVNFQ
GGELNATPLH WAARYGYVYI VDYLLEHGAD PSVTDAQGFN LLHLSINSSN IMLVIYVLFF
VIDDKLDIDC VDPNGRTALL WAAYQGDSLS VETLLKFRAS VKATDKGGFT PLHWGTVKGQ
AQVLKHLIEN GADFFQKTAD GKNCFAIAHD MNTTGSLVGA LYQCGFNKEG FAIPVYFKKS
LHTKLVTFFA PWIFIGVLFK CFASIHPIFS LIFSILLGLG MRYTLKKYVI PAYAQRNTRQ
SFLKTPFLAG VFSGSVFWAS YTWLTRIMPL TLIEEPITNL LFFAGVVLLA SLFVKLVRSD
PGLIPEETDH SKVKETIKEL LNVGKFDAKH FCISTWVRKP IRSKFSNFSR ALVTRFDHFC
PWIYNDIGLR NHKTFLFFIL CLETCIFVFL KLCMEYFDVL EDTFEDDYDL NCGIFGEDLC
AGFFFDTFTF LVLAWTCFQG IWVGFLTFVQ LFQTAKGVTN YEFSTLSKRR HNHDSSVNEY
FTTTPLELID EEEADPLNPV IPGNNPRDPL MQKSRTCFGI CWTLTGLDQF VMVIKETFGV
AQREEPRNNI LSFKISTDYG WRTNLKDFWL TSDITAPTWQ RFLYSPSCSK ALLNGEEVDY
FKLYKLPERH YLAEEIV
