ID   PFA4_USTMA              Reviewed;         481 AA.
AC   Q4PE27; A0A0D1E7T6;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 2.
DT   25-MAY-2022, entry version 86.
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=PFA4 {ECO:0000255|HAMAP-Rule:MF_03199}; ORFNames=UMAG_11136;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003142; KIS70460.1; -; Genomic_DNA.
DR   RefSeq; XP_011388014.1; XM_011389712.1.
DR   AlphaFoldDB; Q4PE27; -.
DR   SMR; Q4PE27; -.
DR   STRING; 237631.Q4PE27; -.
DR   PRIDE; Q4PE27; -.
DR   EnsemblFungi; KIS70460; KIS70460; UMAG_11136.
DR   GeneID; 23567056; -.
DR   KEGG; uma:UMAG_11136; -.
DR   VEuPathDB; FungiDB:UMAG_11136; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_027721_9_0_1; -.
DR   InParanoid; Q4PE27; -.
DR   OrthoDB; 1491968at2759; -.
DR   Proteomes; UP000000561; Chromosome 3.
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..481
FT                   /note="Palmitoyltransferase PFA4"
FT                   /id="PRO_0000212970"
FT   TOPO_DOM        1..66
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        88..108
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        130..223
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        224..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        245..265
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TRANSMEM        266..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   TOPO_DOM        287..481
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT   DOMAIN          181..231
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        211
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
SQ   SEQUENCE   481 AA;  54443 MW;  45FA5AE72D81D6F0 CRC64;
     MTNQDPDDGA YPSSQSDDDG IEALAINRQS RPLLAYEDQA AGQSDAFTDR DIPASTAPLT
     GRRRTPLSWT EVIWVSLTLL LIAVLGYSSQ LYVMLPYYEK TPSFSPQALA AVLVPFNLGL
     LAIYYNYWLC VTTDAGSVPA GWQPEWSALE PVASLAELEH LHLVAEEEPS LELKQAIYRP
     RYCKTCSAFK PPRSHHCKTC QRCVLRMDHH CPWLANCVGH FNHAHFIRFL FYVDVTCLYH
     LIMISCRVLD SFNSYTYWRE PCARELVWLV VNYALCIPVI LLVGIFSLYH FYCLAVNQTT
     IESWEKDRTA TMIRRGRVRK VKYPYDLGLW RNVRQVLGAS PLVWCLPGAG ARMAGDGLKY
     PVANGLDSGS QYRWPPKDPS RPHPSRRTWA SSSSPFTYPE RSNPILDPTL STRFPHNSSP
     SSSDSHSSLH LPHPPSLLDP LPHHFDPPHD PDTQPVNCPK RVSVRRGSEG YEVRPHTPWS
     V