ID F2Q174_TRIEC Unreviewed; 437 AA.
AC F2Q174;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Palmitoyltransferase PFA4 {ECO:0000256|HAMAP-Rule:MF_03199};
DE EC=2.3.1.225 {ECO:0000256|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein S-acyltransferase {ECO:0000256|HAMAP-Rule:MF_03199};
DE Short=PAT {ECO:0000256|HAMAP-Rule:MF_03199};
DE AltName: Full=Protein fatty acyltransferase 4 {ECO:0000256|HAMAP-Rule:MF_03199};
GN Name=PFA4 {ECO:0000256|HAMAP-Rule:MF_03199};
GN ORFNames=TEQG_06924 {ECO:0000313|EMBL:EGE07892.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC proteins, thereby regulating their membrane association and biological
CC function. {ECO:0000256|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:0000256|ARBA:ARBA00001870,
CC ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC {ECO:0000256|HAMAP-Rule:MF_03199}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03199}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03199}.
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DR EMBL; DS995768; EGE07892.1; -; Genomic_DNA.
DR AlphaFoldDB; F2Q174; -.
DR VEuPathDB; FungiDB:TEQG_06924; -.
DR eggNOG; KOG1314; Eukaryota.
DR HOGENOM; CLU_027721_8_1_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR InterPro; IPR033682; PFA4.
DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF19; S-ACYLTRANSFERASE; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03199, ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|HAMAP-Rule:MF_03199};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03199};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03199,
KW ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199,
FT ECO:0000256|RuleBase:RU079119"
FT DOMAIN 95..224
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 357..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 128
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03199"
SQ SEQUENCE 437 AA; 50826 MW; 3E99DD4206924D40 CRC64;
MADFSIYQLA VPFVVLLIAF LSYGSQYLFL YIEPAPLNTS ELVKFNLLVA CIWICYARAC
LTDPGRIPKD WNPPAAAGGL LEKHSSVEEG GDPSYRQRWC RRCEAYKPPR SHHCKTCQRC
IPKMDHHCPW TYNCVSHFTF PHFIRFLFYA VISMMYLERF LYIRIAVIWN NRNLPSYYGP
SLAQLGLLFT LTVVNTIVLL ALLILFLRNI WMLGANETTI EGWEIERHKT LCRRARALGG
YLEGPNGIKV YIKRQEFPYD IGIWNNIRDG MGGSNNIFGW FWPFSRTPDR RTGLEFEVNG
FEDESLTWPP PDPDRMARSM PPGEHDTTLL GEGQNFTYDE VEAFRLRQEA DYLRQRGGKN
VRRRKPFHKR YTKKGDDAHL SSVSDLDDEE SSKSGEEGWR NSEGERLKDF GVDEEVEFYD
EDDIPLAELI RRRRLQS
//
