AKR1_CRYNJ
ID AKR1_CRYNJ Reviewed; 776 AA.
AC P0CS66; Q55ZT8; Q5KP49;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 54.
DE RecName: Full=Palmitoyltransferase AKR1;
DE EC=2.3.1.225;
DE AltName: Full=Ankyrin repeat-containing protein AKR1;
GN Name=AKR1; OrderedLocusNames=CNA04190;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AE017341; AAW40964.1; -; Genomic_DNA.
DR RefSeq; XP_566783.1; XM_566783.1.
DR AlphaFoldDB; P0CS66; -.
DR SMR; P0CS66; -.
DR STRING; 5207.AAW40964; -.
DR PaxDb; P0CS66; -.
DR EnsemblFungi; AAW40964; AAW40964; CNA04190.
DR GeneID; 3253361; -.
DR KEGG; cne:CNA04190; -.
DR VEuPathDB; FungiDB:CNA04190; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_012510_1_0_1; -.
DR InParanoid; P0CS66; -.
DR OMA; DVPDCNG; -.
DR OrthoDB; 445686at2759; -.
DR Proteomes; UP000002149; 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; -; 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; 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..776
FT /note="Palmitoyltransferase AKR1"
FT /id="PRO_0000212921"
FT TOPO_DOM 1..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..336
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..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..553
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..574
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 575..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 68..97
FT /note="ANK 1"
FT REPEAT 103..132
FT /note="ANK 2"
FT REPEAT 137..166
FT /note="ANK 3"
FT REPEAT 170..199
FT /note="ANK 4"
FT REPEAT 203..232
FT /note="ANK 5"
FT REPEAT 236..265
FT /note="ANK 6"
FT DOMAIN 454..504
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 38..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 484
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 776 AA; 84643 MW; 4F82A233DC8F2CBE CRC64;
MDQEMTTVAS PDIRVKATSP DSNRAVLEQS IVLSDSGRLD EGSSIRGGEL ERDSQEVGRE
TVREPLMCHD LDIHALAQRG DTAAIAAMLQ ENPSLNLSAR DAQDVTPLHW AAINAHMGTC
RLLIDSGADI DAIGGELKAT PLQWAARNGH LYVVHLLISR GADPNIHDSQ GFNTLHLITH
SSAVMPLLYM LHQPVAIDEK DTDGHTALMW AAYQGDALSV DLLIRHGASV NSTDNAGMTP
LHWAAVKGNK VSIMHLVEAG ASLDAKEEAG KTPRDMAEEL RGLVPFQKGL EEAGWSIDGV
KMEGKLGPRN TILAIFLLPI AVLWLIFSTF KWLPVYVGVP FAIAEFMGMQ YTVVLVLLGH
IKAQDKVSTS NYFASIITAS LIWVGYCWIS RFAVNTPGYA FSNLGFIIMF VGCCWTFWTA
IVTDPGFVPK GQQDAEIKEV LEDLVDAGRL NGTNFCIVCM ARKPLRSKHC RTCNRCVARF
DHHCPWIWNC VGAKNHRSFL LFVLFLIGGI ILFIRLTIAY IQQNAPEYIP TPNPGLTTCD
ISTTLCQAGD FDPFLLCMAL WSTLQLTWTS VLAISHLWQV SRQMTTFEVS NLGRYGFMGG
RGGQSLRDQS GAMLKQAAAV GAGIGMSGAG EEAAGPPGAE AGPEGNALLP PPGGHVHGPQ
CRHGDHARGH SHGVLHICGA LWKTLTGPLM TILGLDRFTK GKALGGMKRA GRDQNPFDMG
MVKNCIDFWL PDNDVDYMTV YEIPPGGWRA YRRKLAMDKR VPGGKGRYEV VSEQEV
