ERFB_YEAST
ID ERFB_YEAST Reviewed; 359 AA.
AC Q06551; D6VYP4; Q6B217;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Palmitoyltransferase ERF2;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:Q8VDZ4};
DE AltName: Full=DHHC cysteine-rich domain-containing protein ERF2;
DE AltName: Full=Ras protein acyltransferase;
GN Name=ERF2; OrderedLocusNames=YLR246W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP MUTAGENESIS OF LYS-173; ARG-182; CYS-189; ASP-200 AND PHE-218, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10490616; DOI=10.1128/mcb.19.10.6775;
RA Bartels D.J., Mitchell D.A., Dong X., Deschenes R.J.;
RT "Erf2, a novel gene product that affects the localization and
RT palmitoylation of Ras2 in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:6775-6787(1999).
RN [5]
RP FUNCTION, MUTAGENESIS OF CYS-189; HIS-201 AND CYS-203, AND INTERACTION WITH
RP SHR5.
RX PubMed=12193598; DOI=10.1074/jbc.m206573200;
RA Lobo S., Greentree W.K., Linder M.E., Deschenes R.J.;
RT "Identification of a Ras palmitoyltransferase in Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 277:41268-41273(2002).
RN [6]
RP INTERACTION WITH SHR5, AND SUBCELLULAR LOCATION.
RX PubMed=12379641; DOI=10.1074/jbc.m209760200;
RA Zhao L., Lobo S., Dong X., Ault A.D., Deschenes R.J.;
RT "Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved
RT in the plasma membrane localization of yeast Ras proteins.";
RL J. Biol. Chem. 277:49352-49359(2002).
RN [7]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: The ERF2-SHR5 complex is a palmitoyltransferase specific for
CC Ras proteins. Palmitoylates RAS2, which is required for its proper
CC plasma membrane localization. {ECO:0000269|PubMed:12193598}.
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:0000250|UniProtKB:Q8VDZ4};
CC -!- SUBUNIT: Interacts with SHR5. {ECO:0000269|PubMed:12193598,
CC ECO:0000269|PubMed:12379641}.
CC -!- INTERACTION:
CC Q06551; P41912: SHR5; NbExp=2; IntAct=EBI-37230, EBI-2087870;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10490616, ECO:0000269|PubMed:12379641}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10490616,
CC ECO:0000269|PubMed:12379641}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; U20865; AAB67393.1; -; Genomic_DNA.
DR EMBL; AY692913; AAT92932.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09560.1; -; Genomic_DNA.
DR PIR; S59392; S59392.
DR RefSeq; NP_013347.1; NM_001182133.1.
DR AlphaFoldDB; Q06551; -.
DR SMR; Q06551; -.
DR BioGRID; 31513; 79.
DR ComplexPortal; CPX-813; Palmitoyltransferase ERF2/SHR5 complex.
DR DIP; DIP-4783N; -.
DR IntAct; Q06551; 2.
DR MINT; Q06551; -.
DR STRING; 4932.YLR246W; -.
DR SwissPalm; Q06551; -.
DR PaxDb; Q06551; -.
DR PRIDE; Q06551; -.
DR EnsemblFungi; YLR246W_mRNA; YLR246W; YLR246W.
DR GeneID; 850947; -.
DR KEGG; sce:YLR246W; -.
DR SGD; S000004236; ERF2.
DR VEuPathDB; FungiDB:YLR246W; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000174593; -.
DR HOGENOM; CLU_047581_0_0_1; -.
DR InParanoid; Q06551; -.
DR OMA; ISVRIKY; -.
DR BioCyc; YEAST:G3O-32351-MON; -.
DR BRENDA; 2.3.1.225; 984.
DR Reactome; R-SCE-203615; eNOS activation.
DR PRO; PR:Q06551; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06551; protein.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0031211; C:endoplasmic reticulum palmitoyltransferase complex; IPI:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016409; F:palmitoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:ComplexPortal.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Palmitoyltransferase ERF2"
FT /id="PRO_0000212948"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..104
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..250
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 173..223
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 203
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MUTAGEN 173
FT /note="K->E: In ERF2-1; loss of function."
FT /evidence="ECO:0000269|PubMed:10490616"
FT MUTAGEN 182
FT /note="R->Q: In ERF2-7; loss of function."
FT /evidence="ECO:0000269|PubMed:10490616"
FT MUTAGEN 189
FT /note="C->S: Abolishes palmitoyltransferase activity and
FT interaction with SHR5."
FT /evidence="ECO:0000269|PubMed:10490616,
FT ECO:0000269|PubMed:12193598"
FT MUTAGEN 200
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10490616"
FT MUTAGEN 201
FT /note="H->A: Abolishes palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12193598"
FT MUTAGEN 203
FT /note="C->S: Abolishes palmitoyltransferase activity."
FT /evidence="ECO:0000269|PubMed:12193598"
FT MUTAGEN 218
FT /note="F->S: In ERF2-2; loss of function."
FT /evidence="ECO:0000269|PubMed:10490616"
FT CONFLICT 68
FT /note="R -> M (in Ref. 3; AAT92932)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 41099 MW; B1FF42A2370F064B CRC64;
MALVSRRSTR SESTSITKEE HTGEGSLTKL FFRWLVTLEG DQDINDGKGY ISLPNVSNYI
FFLGGRFRTV KGAKPLWLGV LLAIVCPMVL FSIFEAHKLW HTQNGYKVLV IFFYYFWVIT
LASFIRTATS DPGVLPRNIH LSQLRNNYQI PQEYYNLITL PTHSSISKDI TIKYCPSCRI
WRPPRSSHCS TCNVCVMVHD HHCIWVNNCI GKRNYRFFLI FLLGAILSSV ILLTNCAIHI
ARESGGPRDC PVAILLLCYA GLTLWYPAIL FTYHIFMAGN QQTTREFLKG IGSKKNPVFH
RVVKEENIYN KGSFLKNMGH LMLEPRGPSF VSARKPHEAG DWRFMDLSPA HSFEKIQKI
