ERFB_SCHPO
ID ERFB_SCHPO Reviewed; 350 AA.
AC O74384;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Palmitoyltransferase erf2;
DE EC=2.3.1.225 {ECO:0000305|PubMed:23843742};
DE AltName: Full=DHHC cysteine-rich domain-containing protein erf2;
DE AltName: Full=Meiotically up-regulated gene 142 protein;
DE AltName: Full=Ras protein acyltransferase;
GN Name=erf2 {ECO:0000303|PubMed:23843742}; Synonyms=mug142;
GN ORFNames=SPBC3H7.09 {ECO:0000312|PomBase:SPBC3H7.09};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION IN SPORULATION.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF CYS-212.
RX PubMed=23843742; DOI=10.1371/journal.pbio.1001597;
RA Zhang M.M., Wu P.Y., Kelly F.D., Nurse P., Hang H.C.;
RT "Quantitative control of protein S-palmitoylation regulates meiotic entry
RT in fission yeast.";
RL PLoS Biol. 11:e1001597-e1001597(2013).
CC -!- FUNCTION: The erf2-erf4 complex is a palmitoyltransferase with a major
CC role in driving sexual development (PubMed:23843742, PubMed:16303567).
CC Palmitoylates ras1 (PubMed:23843742). Palmitoylates isp3
CC (PubMed:23843742). Palmitoylates rho3 (PubMed:23843742).
CC {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:23843742}.
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:0000305|PubMed:23843742};
CC -!- SUBUNIT: Interacts with erf4. {ECO:0000250|UniProtKB:Q06551}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q06551}. Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during meiosis and sporulation
CC (at protein level). {ECO:0000269|PubMed:23843742}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:Q06551}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC -!- DISRUPTION PHENOTYPE: Abolishes palmitoylation of ras1 during
CC vegetative growth (PubMed:23843742). Delays mitotic entry
CC (PubMed:23843742). {ECO:0000269|PubMed:23843742}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC ERF2/ZDHHC9 subfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAA20305.1; -; Genomic_DNA.
DR PIR; T40406; T40406.
DR RefSeq; NP_595766.1; NM_001021667.2.
DR AlphaFoldDB; O74384; -.
DR SMR; O74384; -.
DR BioGRID; 277573; 46.
DR STRING; 4896.SPBC3H7.09.1; -.
DR PaxDb; O74384; -.
DR EnsemblFungi; SPBC3H7.09.1; SPBC3H7.09.1:pep; SPBC3H7.09.
DR GeneID; 2541058; -.
DR KEGG; spo:SPBC3H7.09; -.
DR PomBase; SPBC3H7.09; erf2.
DR VEuPathDB; FungiDB:SPBC3H7.09; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_792633_0_0_1; -.
DR InParanoid; O74384; -.
DR OMA; PLVYQRW; -.
DR PhylomeDB; O74384; -.
DR Reactome; R-SPO-203615; eNOS activation.
DR PRO; PR:O74384; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0031211; C:endoplasmic reticulum palmitoyltransferase complex; ISO:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IMP:PomBase.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IC:PomBase.
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 GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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; Golgi apparatus; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Sporulation; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..350
FT /note="Palmitoyltransferase erf2"
FT /id="PRO_0000212946"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..112
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..270
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 292..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 182..232
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 212
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT MUTAGEN 212
FT /note="C->A: Abolishes palmitoylation of ras1 during
FT sporulation."
FT /evidence="ECO:0000269|PubMed:23843742"
SQ SEQUENCE 350 AA; 40294 MW; A9F97E1780DE4445 CRC64;
MSYEKHSDAK ASRYAWNQPW NPFEVTLSDP TYPMNLEEKN QIPYRFQSVP DDVPEVPHIE
SRYKNLPGNN IYLCCGRLQM SSQYKAFLIS LFALILPGVL FFIFSAFWLW HHVSPAVPIT
FAYLYALAVV SMFKCSTADP GILPRNAYSL TYNPAHPWSV IPEDRKVLVG STRSDSVFVN
TVYCHTCHLY RPPRASHCHL CDNCVEYLDH HCIWLNTCIG RRNYRYYFIF LLSVVLSALY
LTGLGFYTSI GSFHESTDTN FAAHLRRPWA GVSFFLGIYG ALGAILPGIL FCYQCYLISV
GQNVHEYLRA KSTETEDVHP FHDSIWLNFL VVLCRPKNVS YVRPTRKSYV
