SWF1_SCHPO
ID SWF1_SCHPO Reviewed; 356 AA.
AC O60069;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Palmitoyltransferase swf1;
DE EC=2.3.1.225;
GN Name=swf1; ORFNames=SPBC13G1.07;
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).
CC -!- FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs.
CC Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic
CC end of their transmembrane domain. May have a role in the cellular
CC quality control of transmembrane domain-containing proteins (By
CC similarity). {ECO:0000250}.
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;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. SWF1
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; CAA18660.1; -; Genomic_DNA.
DR PIR; T39408; T39408.
DR RefSeq; NP_596556.1; NM_001022477.2.
DR AlphaFoldDB; O60069; -.
DR SMR; O60069; -.
DR STRING; 4896.SPBC13G1.07.1; -.
DR PaxDb; O60069; -.
DR EnsemblFungi; SPBC13G1.07.1; SPBC13G1.07.1:pep; SPBC13G1.07.
DR GeneID; 2539719; -.
DR KEGG; spo:SPBC13G1.07; -.
DR PomBase; SPBC13G1.07; swf1.
DR VEuPathDB; FungiDB:SPBC13G1.07; -.
DR eggNOG; KOG1312; Eukaryota.
DR HOGENOM; CLU_042181_0_0_1; -.
DR InParanoid; O60069; -.
DR OMA; CEYCHLE; -.
DR PhylomeDB; O60069; -.
DR PRO; PR:O60069; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:PomBase.
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 InterPro; IPR001594; Palmitoyltrfase_DHHC.
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..356
FT /note="Palmitoyltransferase swf1"
FT /id="PRO_0000212992"
FT TOPO_DOM 1..2
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..107
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..253
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..356
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 158..208
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 356 AA; 41466 MW; F7C7468E90B899A3 CRC64;
MDFFYKYLAL VAIASLMVFI LLFGQIPKLK YTVIGKLNRF FMVTIPYHLH VLDSRYADGR
CSAAMRSLSN YVLYKNNPLV VFLYLALITI GIASFFIYGS SLTQKFSIID WISVLTSVLL
PYISLYIAAK SNPGKIDLKN WNEASRRFPY DYKIFFPNKC STCKFEKPAR SKHCRLCNIC
VEKFDHHCIW INNCVGLNNA RYFFLFLLCT IQLLFHSILR LGYHFNALRD MRQYPSFLRS
WWFAIKSEGE LGSVFLISLI CSVLVLCLLG YEFFLVYAGY TTNESEKWSD LAHLVKNRKV
YMYYENGSQL LALDKDASND AILVTSMSQI DNIYDNGFYN NFFSLVFPYR HLYSTT
