(data stored in ACNUC6288 zone)

SWISSPROT: PFA4_DEBHA

ID   PFA4_DEBHA              Reviewed;         402 AA.
AC   Q6BLY8; B5RUD0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   10-APR-2019, entry version 85.
DE   RecName: Full=Palmitoyltransferase PFA4 {ECO:0000255|HAMAP-Rule:MF_03199};
DE            EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199};
DE   AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199};
DE            Short=PAT {ECO:0000255|HAMAP-Rule:MF_03199};
DE   AltName: Full=Protein fatty acyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN   Name=PFA4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN   OrderedLocusNames=DEHA2F09702g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC       proteins, thereby regulating their membrane association and
CC       biological function. {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683,
CC         Rhea:RHEA-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; Evidence={ECO:0000255|HAMAP-Rule:MF_03199};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity. {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAR66308.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CR382138; CAR66308.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_002770783.1; XM_002770737.1.
DR   STRING; 4959.XP_002770783.1; -.
DR   PRIDE; Q6BLY8; -.
DR   EnsemblFungi; CAR66308; CAR66308; DEHA2F09702g.
DR   GeneID; 8998928; -.
DR   KEGG; dha:DEHA2F09702g; -.
DR   HOGENOM; HOG000248636; -.
DR   InParanoid; Q6BLY8; -.
DR   KO; K18932; -.
DR   OrthoDB; 1491968at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0005789; C:endoplasmic reticulum 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-UniRule.
DR   GO; GO:0018345; P:protein palmitoylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR033682; PFA4.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BLY8.
DR   SWISS-2DPAGE; Q6BLY8.
KW   Acyltransferase; Complete proteome; Endoplasmic reticulum;
KW   Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    402       Palmitoyltransferase PFA4.
FT                                /FTId=PRO_0000212965.
FT   TOPO_DOM      1      8       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM      9     29       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM     30     39       Lumenal. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM     40     60       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM     61    125       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM    126    146       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM    147    165       Lumenal. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM    166    186       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM    187    402       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   DOMAIN       78    128       DHHC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00067}.
FT   ACT_SITE    108    108       S-palmitoyl cysteine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_03199}.
SQ   SEQUENCE   402 AA;  47335 MW;  CB5B38444AFB7265 CRC64;
     MAVQLKWPII GVVIPCVLIA MVAYGSHYFV FRTNLSRTEQ ILYEVYVCIV WLSYYLAIVV
     DPGSPPKNFT PKAGEWRRWC KKCQNYKPER SHHCKTCNKC VLKMDHHCPW TYNCVGHNNL
     PHFLRFVFFL IVGMTYVLFQ LGKQVLHYYD SSKLPSYLID KKEMCAVIFL LPVTFFVFVS
     IIILFVRCMI NLLFRGMTQI EVWEMERIGS QFHTERLWLQ IRKNYFKLHG KEMPHLVSWN
     RTTRYYEVDE NSNNDNSNEN NIVPKDFTSD DIVFPYDLGV SSNMINACDY PWMWLLPWGG
     PRENGYHFQK NEFMEDDQLG LPWPPDGGHQ EPMAPVDDDF DISDSELQDM PSLRRRLDPR
     NNMTRSEWMN DLGETLDDFG VDLDAEDIEH DDLVSKDEIS NN
//

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