ERFD_YEAST
ID ERFD_YEAST Reviewed; 237 AA.
AC P41912; D6W1V7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ras modification protein ERF4;
DE AltName: Full=Hyperactive Ras suppressor protein 5;
GN Name=SHR5; Synonyms=ERF4; OrderedLocusNames=YOL110W; ORFNames=HRC237;
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 [GENOMIC DNA], AND FUNCTION.
RC STRAIN=SP1;
RX PubMed=7532279; DOI=10.1128/mcb.15.3.1333;
RA Jung V., Chen L., Hofmann S.L., Wigler M., Powers S.;
RT "Mutations in the SHR5 gene of Saccharomyces cerevisiae suppress Ras
RT function and block membrane attachment and palmitoylation of Ras
RT proteins.";
RL Mol. Cell. Biol. 15:1333-1342(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH ERF2.
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 FUNCTION, MUTAGENESIS OF SER-128; VAL-148 AND LEU-204, INTERACTION WITH
RP ERF2, 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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: The ERF2-SHR5 complex is a palmitoyltransferase specific for
CC Ras proteins (PubMed:12193598, PubMed:12379641, PubMed:7532279).
CC Palmitoylates RAS2, which is required for its proper plasma membrane
CC localization (PubMed:12193598, PubMed:12379641, PubMed:7532279).
CC {ECO:0000269|PubMed:12193598, ECO:0000269|PubMed:12379641,
CC ECO:0000269|PubMed:7532279}.
CC -!- SUBUNIT: Interacts with ERF2. {ECO:0000269|PubMed:12193598,
CC ECO:0000269|PubMed:12379641}.
CC -!- INTERACTION:
CC P41912; Q06551: ERF2; NbExp=2; IntAct=EBI-2087870, EBI-37230;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12379641}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12379641}.
CC -!- MISCELLANEOUS: Present with 937 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ERF4 family. {ECO:0000305}.
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DR EMBL; U18313; AAA67935.1; -; Genomic_DNA.
DR EMBL; Z48149; CAA88152.1; -; Genomic_DNA.
DR EMBL; Z74852; CAA99129.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10673.1; -; Genomic_DNA.
DR PIR; S51889; S51889.
DR RefSeq; NP_014531.1; NM_001183364.1.
DR AlphaFoldDB; P41912; -.
DR BioGRID; 34290; 96.
DR ComplexPortal; CPX-813; Palmitoyltransferase ERF2/SHR5 complex.
DR DIP; DIP-7228N; -.
DR IntAct; P41912; 2.
DR MINT; P41912; -.
DR STRING; 4932.YOL110W; -.
DR PaxDb; P41912; -.
DR PRIDE; P41912; -.
DR EnsemblFungi; YOL110W_mRNA; YOL110W; YOL110W.
DR GeneID; 854039; -.
DR KEGG; sce:YOL110W; -.
DR SGD; S000005470; SHR5.
DR VEuPathDB; FungiDB:YOL110W; -.
DR eggNOG; ENOG502S30T; Eukaryota.
DR HOGENOM; CLU_087349_0_0_1; -.
DR InParanoid; P41912; -.
DR OMA; CITHFPN; -.
DR BioCyc; YEAST:G3O-33507-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR ChiTaRS; SHR5; yeast.
DR PRO; PR:P41912; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P41912; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ComplexPortal.
DR GO; GO:0031211; C:endoplasmic reticulum palmitoyltransferase complex; IPI:SGD.
DR GO; GO:0042406; C:extrinsic component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0002178; C:palmitoyltransferase complex; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IDA:ComplexPortal.
DR GO; GO:0018345; P:protein palmitoylation; IDA:SGD.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR InterPro; IPR019383; Golgin_A_7/ERF4.
DR Pfam; PF10256; Erf4; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Membrane; Reference proteome.
FT CHAIN 1..237
FT /note="Ras modification protein ERF4"
FT /id="PRO_0000213988"
FT MUTAGEN 128
FT /note="S->P: In ERF4-1; loss of function."
FT /evidence="ECO:0000269|PubMed:12379641"
FT MUTAGEN 148
FT /note="V->K: In ERF4-2; loss of function."
FT /evidence="ECO:0000269|PubMed:12379641"
FT MUTAGEN 204
FT /note="L->P: In ERF4-3; loss of function."
FT /evidence="ECO:0000269|PubMed:12379641"
SQ SEQUENCE 237 AA; 26542 MW; 28F66E12B491ADAD CRC64;
MCDSHQKEED NANTSERALF FNYHEFSYSF YEDLGSEDAK PTEHDEDHKL CITHFPNVYA
ARGSAEFQVT RVVRVPRRFD ESRSSLETPQ FSTQLPGSEP AAIVGDDGTS FVRCGRYDIG
DHVFGCSSVS PLSEYLSAAE LAEVVHRVNG FLLREEGEVF GWRNLSGLLL DMLTGGLWSW
VLGPLLSRPV FQESLALEQY VAQLNSPGGL LHERGVRLVL PRRSGCLSLD FVVPRPK
