(data stored in ACNUC7421 zone)

SWISSPROT: ERFB_ASHGO

ID   ERFB_ASHGO              Reviewed;         367 AA.
AC   Q750R7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Palmitoyltransferase ERF2;
DE            EC=2.3.1.225;
DE   AltName: Full=DHHC cysteine-rich domain-containing protein ERF2;
DE   AltName: Full=Ras protein acyltransferase;
GN   Name=ERF2; OrderedLocusNames=AGL125C;
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.
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: The ERF2-ERF4 complex is a palmitoyltransferase specific for
CC       Ras proteins. {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   -!- SUBUNIT: Interacts with ERF4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250}.
CC   -!- PTM: Autopalmitoylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily. {ECO:0000305}.
DR   EMBL; AE016820; AAS54366.1; -; Genomic_DNA.
DR   RefSeq; NP_986542.1; NM_211604.1.
DR   STRING; 33169.AAS54366; -.
DR   PRIDE; Q750R7; -.
DR   EnsemblFungi; AAS54366; AAS54366; AGOS_AGL125C.
DR   GeneID; 4622841; -.
DR   KEGG; ago:AGOS_AGL125C; -.
DR   HOGENOM; HOG000248576; -.
DR   InParanoid; Q750R7; -.
DR   KO; K16675; -.
DR   OMA; TFNIVYV; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:EnsemblFungi.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0031211; C:endoplasmic reticulum palmitoyltransferase complex; IEA:EnsemblFungi.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; IEA:EnsemblFungi.
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   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q750R7.
DR   SWISS-2DPAGE; Q750R7.
KW   Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..367
FT                   /note="Palmitoyltransferase ERF2"
FT                   /id="PRO_0000212937"
FT   TOPO_DOM        1..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..121
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..229
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        251..262
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          185..235
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ   SEQUENCE   367 AA;  42039 MW;  37C069EC7219FD6A CRC64;
     MRLHSRQASN PHRQYSAAQS LHSSSDDSEH KEIPSTMGWA KRLMRWMVTV DQPHTFETSL
     KNYQSLAHVT NYIFFCGGRL RTVAKTKYLS VLVLVMLIAP IVLFSVFETG YLWKHVAGAK
     PCVVLCYYFW TLCFASFIST GATDPGTLPR NIHLAQLQDD YKLPLEYYSI ITLPSPVANA
     PVRLKYCTTC RIWRPPRASH CAVCDSCILS FDHHCDWLNN CIGQRNHRYF LAFLFSSVLS
     SIWLLTCCAL KLRHAGSPSA APVSLLLICY CAVSIWYPLL LAIYHLFLTG TQQTTHEYLK
     AVDSRNPIFH KVTHPERNPF VTGSCARNML LLMCQPRGYD FLHTRSEHQA GDWRFFRLPI
     PHSFEKV
//

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