PFA3_SCHPO
ID PFA3_SCHPO Reviewed; 329 AA.
AC O14345;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Palmitoyltransferase pfa3;
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:P42836};
DE AltName: Full=Protein fatty acyltransferase 3;
GN Name=pfa3; ORFNames=SPBC2F12.15c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at
CC one or more of its N-terminal cysteine residues, which is required for
CC its proper membrane localization. {ECO:0000250|UniProtKB:P42836}.
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:P42836};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372};
CC Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane
CC protein {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250|UniProtKB:P42836}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:P42836}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3
CC subfamily. {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; CU329671; CAB10162.1; -; Genomic_DNA.
DR PIR; T40126; T40126.
DR RefSeq; NP_595701.1; NM_001021598.2.
DR AlphaFoldDB; O14345; -.
DR SMR; O14345; -.
DR BioGRID; 276991; 39.
DR STRING; 4896.SPBC2F12.15c.1; -.
DR iPTMnet; O14345; -.
DR PaxDb; O14345; -.
DR PRIDE; O14345; -.
DR EnsemblFungi; SPBC2F12.15c.1; SPBC2F12.15c.1:pep; SPBC2F12.15c.
DR GeneID; 2540463; -.
DR KEGG; spo:SPBC2F12.15c; -.
DR PomBase; SPBC2F12.15c; pfa3.
DR VEuPathDB; FungiDB:SPBC2F12.15c; -.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_845091_0_0_1; -.
DR InParanoid; O14345; -.
DR OMA; YAMILII; -.
DR PhylomeDB; O14345; -.
DR PRO; PR:O14345; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISO:PomBase.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IC:PomBase.
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 GO; GO:0042144; P:vacuole fusion, non-autophagic; ISO:PomBase.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Golgi apparatus; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Vacuole.
FT CHAIN 1..329
FT /note="Palmitoyltransferase pfa3"
FT /id="PRO_0000116499"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 97..147
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 329 AA; 38091 MW; 20DE9BFAE33E8E2C CRC64;
MNLIHKVSTI CQCVLVILAK YCMQIIALSL MSGVQWLAWG IYKINKNRVG IIILFLYIMI
VTCYVLTNLT PPGSPSETSF DPNSTRQYMT LQNGKSRFCE KCQEYKCDRS HHCSQCNKCI
LRMDHHCMWF KNCVGFRNHK FFFLECFYLN LYSICVLYST FVAITKTFTA EGANISAIYL
VFWGFLFAFA VGMSIVMTAF TFYHTSLLIH NLSTLESMSS SWSRYTHSTQ PFNVGWYENW
CQIMGKSPFL WLLPFPNSIG EGVEYPLNAN ALPYLPQTEE KNDKLYKSSV PASIAGAEGW
SSDEEQYAMK NRRWNPHMGQ YEWIEDFLV
