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PFA4_NEUCR
ID   PFA4_NEUCR              Reviewed;         486 AA.
AC   Q7SCY6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Palmitoyltransferase pfa4 {ECO:0000255|HAMAP-Rule:MF_03199};
DE            EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199};
DE   AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199};
DE            Short=PAT {ECO:0000255|HAMAP-Rule:MF_03199};
DE   AltName: Full=Protein fatty acyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN   Name=ptr-4 {ECO:0000305}; Synonyms=pfa4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN   ORFNames=NCU02118;
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=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: Mediates the reversible addition of palmitate to target
CC       proteins, thereby regulating their membrane association and biological
CC       function. {ECO:0000255|HAMAP-Rule:MF_03199}.
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:0000255|HAMAP-Rule:MF_03199};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
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DR   EMBL; CM002236; EAA34619.1; -; Genomic_DNA.
DR   RefSeq; XP_963855.1; XM_958762.2.
DR   AlphaFoldDB; Q7SCY6; -.
DR   STRING; 5141.EFNCRP00000001158; -.
DR   PRIDE; Q7SCY6; -.
DR   EnsemblFungi; EAA34619; EAA34619; NCU02118.
DR   GeneID; 3880004; -.
DR   KEGG; ncr:NCU02118; -.
DR   VEuPathDB; FungiDB:NCU02118; -.
DR   HOGENOM; CLU_027721_8_1_1; -.
DR   InParanoid; Q7SCY6; -.
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   HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR033682; PFA4.
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..486
FT                   /note="Palmitoyltransferase pfa4"
FT                   /id="PRO_0000212969"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        37..51
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        52..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        73..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        147..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        167..178
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        179..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        202..486
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   DOMAIN          102..152
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          81..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        345..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        132
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
SQ   SEQUENCE   486 AA;  55630 MW;  C2F129A71DDD5D82 CRC64;
     MTNLQTGPTT RGLQRFAIPA VCGLIIFLGY YSQYLFNTSA DLAPGPLTCR ESLIFNILLV
     CLWLTYYQAC TVDPGQYKFP PKEKEDGDNN NKRGGRGPQK AKWCKKCDAP KPPRAHHCRH
     CARCIPRMDH HCPWTGNCVS LQTFPHFLRF LVYTNAALVY FARLLWTRLY YGLWDQRHVP
     AYLGPSVGAL LGCTMLSIAW FATQFALMVL LVTTVRSWML GKTMIEEWEA ERHETLLARS
     YDGDDYWGAD GHGGFVPVKV EFPYDNGFWS NMAQAMGTNN FLRWFLPVGG GGPKISNDTP
     WKGTGWEYEE NGFNDRVGMW PPPDPEKLRR ERAGAGGKWP GARENLNTEK PEVDYYRSSE
     DMKTAFKRRQ QEDLRRRQQR RQHSSEEDEI MAELEEDEGY EQRSRTRSPP QDGRAWMNSE
     GDTLWDYGVD VDEEENYGYP GQGVSESLPL VKTATGYNDG QGDEDEDVPL AELIRRRKVK
     SNGVHE
 
 
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