PFA4_EMENI
ID PFA4_EMENI Reviewed; 435 AA.
AC Q5BD15; C8VN05;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, 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=pfa4 {ECO:0000255|HAMAP-Rule:MF_03199}; ORFNames=AN1565;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000025; EAA64272.1; -; Genomic_DNA.
DR EMBL; BN001307; CBF85122.1; -; Genomic_DNA.
DR RefSeq; XP_659169.1; XM_654077.1.
DR AlphaFoldDB; Q5BD15; -.
DR STRING; 162425.CADANIAP00008195; -.
DR PRIDE; Q5BD15; -.
DR EnsemblFungi; CBF85122; CBF85122; ANIA_01565.
DR EnsemblFungi; EAA64272; EAA64272; AN1565.2.
DR GeneID; 2875674; -.
DR KEGG; ani:AN1565.2; -.
DR VEuPathDB; FungiDB:AN1565; -.
DR eggNOG; KOG1314; Eukaryota.
DR HOGENOM; CLU_027721_8_1_1; -.
DR InParanoid; Q5BD15; -.
DR OMA; CQRCIPK; -.
DR OrthoDB; 1491968at2759; -.
DR Proteomes; UP000000560; Chromosome VII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..435
FT /note="Palmitoyltransferase pfa4"
FT /id="PRO_0000212966"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 32..48
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 70..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 151..179
FT /note="Lumenal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT TOPO_DOM 201..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
FT DOMAIN 91..141
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 359..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03199"
SQ SEQUENCE 435 AA; 50007 MW; 567AB44B60D3CCA6 CRC64;
MLCSSFSVSR LAIPAVCILI AFLAYTSQIF FLYFEDAPLK EDEVWRINIL AICIWICYYR
ACTVDPGHVP KGWMPSDRER LKADRASGRQ RWCRRCEAYK PPRAHHCKTC ERCVPKMDHH
CPWTSNCVSH FTFPHFARFL FYAVVGIAYL ETRLWQRVSK VWGSRHLPSY LGPSMGQIGH
LFVLFVTNSL TLFALSLLLL RTLWSLGSNT TTIESWEIER HETLLRRARR LGGSLPGPGG
ISVHITKQEF PYDIGIWSNI RAGMGGSANV LSWFWPLART PDRSTGLEFE ENGFEDPTVS
WPPPDPDRIP LPPMDQRDSF MYDITDTSGT SGQIDIEAFN RRKEADLRRR RAPTEIERRK
PFHVRLEEYS NGSSDAEADT GSDDDSDHGE EGWKNSEGER LRDFGVDEEA EFYDEEDIPL
ALLIQQRAKR QHLSQ
