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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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