(data stored in ACNUC7421 zone)

SWISSPROT: PFA4_ASHGO

ID   PFA4_ASHGO              Reviewed;         375 AA.
AC   Q75CB4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   11-DEC-2019, entry version 94.
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}; OrderedLocusNames=ACL003C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 115-128.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
CC   -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC       proteins, thereby regulating their membrane association and biological
CC       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, 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; 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 activity.
CC       {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
DR   EMBL; AE016816; AAS51225.2; -; Genomic_DNA.
DR   RefSeq; NP_983401.2; NM_208754.2.
DR   STRING; 33169.AAS51225; -.
DR   EnsemblFungi; AAS51225; AAS51225; AGOS_ACL003C.
DR   GeneID; 4619526; -.
DR   KEGG; ago:AGOS_ACL003C; -.
DR   HOGENOM; HOG000248636; -.
DR   InParanoid; Q75CB4; -.
DR   KO; K18932; -.
DR   OMA; YYLAIYT; -.
DR   Proteomes; UP000000591; Chromosome III.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
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; Q75CB4.
DR   SWISS-2DPAGE; Q75CB4.
KW   Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..375
FT                   /note="Palmitoyltransferase PFA4"
FT                   /id="PRO_0000212960"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        31..33
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        55..121
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        143..164
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        186..375
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   DOMAIN          78..128
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        108
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
SQ   SEQUENCE   375 AA;  44021 MW;  D1EE21A6956D9D32 CRC64;
     MAVLVKWPWL GVAIPCFLIS FTGYFAHFFV LTNFLSFKEL LWFQVSLSMI WISYWKAIYK
     NPGRPTKGFR PLRYEWQNYC TKCETYKPER THHCKRCNQC VLVMDHHCPW TMNCVGYKNF
     PHFIRFLFWI IATTGILLHY FVKRIKFTWV NRYATANLVS KQELIFLTIL TPLDAFILLT
     ISLLFVRCVK NQIVNGRTQI EAWEMDRIEN LFYHQRLLPQ LLTNLKEIYP GSLEGQEKEV
     EEFLSSSTCS FDEVINFPYD INPWVNLLNC MGSPLNWLNP FGGPKADGMV FQKNEISDYD
     EATSIQDKLL ALPWPPDDTR HGIAFPSVSH VEKDTQGGEQ VVRRRHVPIA VPPRNEWYND
     WGESLEHFGV DVEVE
//

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