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ERFB_NEUCR
ID   ERFB_NEUCR              Reviewed;         680 AA.
AC   Q7SFL7; Q6MVU6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=Palmitoyltransferase 2;
DE   AltName: Full=Ras protein acyltransferase;
GN   Name=ptr-2; Synonyms=erf2; ORFNames=B15B3.180, NCU02015;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: Palmitoyltransferase specific for Ras proteins.
CC       {ECO:0000250|UniProtKB:Q06551}.
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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q06551}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q06551}.
CC   -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE76200.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX842622; CAE76200.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002236; EAA35644.3; -; Genomic_DNA.
DR   RefSeq; XP_964880.3; XM_959787.3.
DR   AlphaFoldDB; Q7SFL7; -.
DR   SMR; Q7SFL7; -.
DR   STRING; 367110.Q7SFL7; -.
DR   EnsemblFungi; EAA35644; EAA35644; NCU02015.
DR   GeneID; 3881029; -.
DR   KEGG; ncr:NCU02015; -.
DR   VEuPathDB; FungiDB:NCU02015; -.
DR   HOGENOM; CLU_021757_0_0_1; -.
DR   InParanoid; Q7SFL7; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..680
FT                   /note="Palmitoyltransferase erf2"
FT                   /id="PRO_0000212945"
FT   TOPO_DOM        1..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..384
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..501
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        502..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        523..543
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..680
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          457..507
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          1..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          656..680
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        487
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDZ4"
FT   CONFLICT        413
FT                   /note="G -> GVCYSLLPF (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   680 AA;  75414 MW;  18C89264D1FD64DC CRC64;
     MASEEGPSRS ASPTNVDNTF PQYPPRAELT VAGPPSLISS RMTDIGTEDG QGSDTTPRGG
     GPSSANPNRR SGFYSDTQSR PETSGTGLSS RGPWAQSVPL RQQLTGKRGS IAGSIGSAGG
     RPISAASRSH VPSLTSHGFF RPMSSQKLQA QRGAGRPPTM NRPYVITGEA GARNSVISTG
     SGRIGAQIAE DAELRMPSRG TEMTEQETME RMTANTSPIN GFFPTSSVTD SVRPLQSPVD
     ARNINVEMNK DYREESPTTP PRSPTRTSRS FRSSFLMPRM NESGITGSNR EIEGGEKLQS
     AASSPNIPPQ SYERQRARFK RRAKRQNRAN LGKNYEYFEG NTVFCLGGRF QNTKQRPINI
     ATGSLIVLPC ILFFIFSAPW IWHNISPAIP VTFAYLAYIC VSSFLHASAS DPGILPRNLH
     KFPPPEMEDS PTGPPTTDWV LVHSAEASTA AMEVPIKYCK TCQLWRPPRA HHCRLCDNCV
     ETQDHHCVWL NNCVGRRNYR YFFTFVSSAT VLALYLIGAC LAQILVYKNQ HHISFGHAVN
     HFRVPFAMVF FGFLTFLYPA ALTGYHIFLM ARGETTREYL NSHKFPKSDR YRAFTQANWL
     KNWFVVLCRP RPPTYYGFKV KYNQGDQRLG SHRRWQQPAV SDSKEGMEMQ NVSPQLPQTG
     FMGPTALRNS NNGSTAEVRA
 
 
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