AKR1_CANAL
ID AKR1_CANAL Reviewed; 813 AA.
AC Q5AL27; A0A1D8PFK8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=CAALFM_C113220CA;
GN ORFNames=CaO19.12414, CaO19.4950;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017623; AOW26929.1; -; Genomic_DNA.
DR RefSeq; XP_722161.1; XM_717068.2.
DR AlphaFoldDB; Q5AL27; -.
DR SMR; Q5AL27; -.
DR STRING; 237561.Q5AL27; -.
DR PRIDE; Q5AL27; -.
DR GeneID; 3636166; -.
DR KEGG; cal:CAALFM_C113220CA; -.
DR CGD; CAL0000187472; AKR1.
DR VEuPathDB; FungiDB:C1_13220C_A; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_1_1; -.
DR InParanoid; Q5AL27; -.
DR OMA; PWMAGIF; -.
DR OrthoDB; 445686at2759; -.
DR PRO; PR:Q5AL27; -.
DR Proteomes; UP000000559; Chromosome 1.
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:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
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; 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..813
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212919"
FT TOPO_DOM 1..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..412
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..485
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..579
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 601..642
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..813
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 133..162
FT /note="ANK 1"
FT REPEAT 167..196
FT /note="ANK 2"
FT REPEAT 201..231
FT /note="ANK 3"
FT REPEAT 235..264
FT /note="ANK 4"
FT REPEAT 276..305
FT /note="ANK 5"
FT REPEAT 309..338
FT /note="ANK 6"
FT DOMAIN 536..586
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 566
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 813 AA; 91741 MW; 6A27A94506E7AA90 CRC64;
MAKKKSKSKS SSPKPKVSST AAKPVEIDNQ QNIENVQDSP SALQQQSATA EESENTATTA
TPSEGTTATT ESSPVTTSNE TDPIELSVLD NADHAIDSNS IKSTEAVLET LDSELNTIAD
TKTEPPTEQE LNPTLAKYMR SCQEGNLTIV KELISSGQVL VNDTFSDEIT GLHWACINNR
LSLVKFLIAN GANPNQLGGE LKASPLHWAC RNGLVYIVDY LMRNSDADPN LRDAQTYNAL
HLAVHSSNIM LVIYLLLSCC STDSVKKVYI DEPDGSNRTA LHWASYQNDI FTINALLRFG
ADVSKVDNSL FIPLHWAFMK GYKSVLKALV EAGSDIYFKN DQNKNSFDIA KDMNCSNTWE
KVLIETGRDP KNNWAPLKPW VSAKLGKIIT FLTPYFLLPL SFNVLSMGGD QGGFIIPKLI
LAIGILGGGI YLLNKLIISQ YIFDDKKLAK SPILAGVFSA TAFWSVLVWL YNILPTTFIH
NFFANVIMAI LIAIFTWSFF KAMFINPGFV PTPADNNVIL SQVAQLIELG KFDTDHFCVN
SFVRKPLRSR YSKHNKRLIA RFDHSCPWVY NDIGVRNHKI FITFVYSLNM AIFVFLYLSL
QYFDKVKDQY DSDDEGEGEG FVCSILGDDM CYGYKNHHFH FNVFMWDLFQ CVWVSFLCIV
QTFQILKGLT TWEFSSLNKQ LQTNRFNHST VPRDFEAGEG ISLDQTQPSD GQHRHNHNEF
QTCMNLLGID QFILTLKMSL KSLFSNTRHG NNNTNYDPLT SLHIPTDHGI KQNWLDFWII
GEEKWRNVFY LPIDGENNLN GKVVDYYTLY SYH
