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ZDHC2_DICDI
ID   ZDHC2_DICDI             Reviewed;         446 AA.
AC   Q86A83; Q555W9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Putative ZDHHC-type palmitoyltransferase 2;
DE            EC=2.3.1.225;
DE   AltName: Full=Zinc finger DHHC domain-containing protein 2;
GN   ORFNames=DDB_G0274739;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:EAL70262.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4 {ECO:0000312|EMBL:EAL70262.1};
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-169 AND 378-446.
RC   STRAIN=AX4;
RX   PubMed=15010511; DOI=10.1093/nar/gkh262;
RA   Urushihara H., Morio T., Saito T., Kohara Y., Koriki E., Ochiai H.,
RA   Maeda M., Williams J.G., Takeuchi I., Tanaka Y.;
RT   "Analyses of cDNAs from growth and slug stages of Dictyostelium
RT   discoideum.";
RL   Nucleic Acids Res. 32:1647-1653(2004).
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: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250|UniProtKB:Q9NYG2}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000255}.
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DR   EMBL; AAFI02000012; EAL70262.1; -; Genomic_DNA.
DR   EMBL; AU053196; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AU053698; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AU060371; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AU062170; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_643941.1; XM_638849.1.
DR   AlphaFoldDB; Q86A83; -.
DR   SMR; Q86A83; -.
DR   STRING; 44689.DDB0203296; -.
DR   PaxDb; Q86A83; -.
DR   EnsemblProtists; EAL70262; EAL70262; DDB_G0274739.
DR   GeneID; 8619369; -.
DR   KEGG; ddi:DDB_G0274739; -.
DR   dictyBase; DDB_G0274739; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_614567_0_0_1; -.
DR   InParanoid; Q86A83; -.
DR   OMA; NCVGLFN; -.
DR   PhylomeDB; Q86A83; -.
DR   PRO; PR:Q86A83; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Glycoprotein; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..446
FT                   /note="Putative ZDHHC-type palmitoyltransferase 2"
FT                   /id="PRO_0000259606"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          261..311
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          56..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        14
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        141
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   446 AA;  51496 MW;  FFAB59277FA1AC5D CRC64;
     MNLYNNSNSS GSSNSSSSSN NKTNIDYNDI NNNDILTPKG YHTSIYIDDN DLNNNQIINK
     NNNNNHNRNN NNNNNNNNNH NNPKKMVINL NPSGIFIPLM NDFDDDDDDE QESLIKNNKI
     TIPTINSQIA IPILNNNDNN NNSNNKTEQT TTTTTIIKNT TIFNNKTISF GRIGFRSIVI
     FLILVPYIYI LNFAIFPWTV NYETERKGKI HSFISMALVI QMLCNYYLCS TTDPGSFKDT
     ISPSYYLLHP ISSTDSNDHK KWCNKCNHQK PERAHHCRYC NRCVLRMDHH CQWLQNCIGL
     FNQKYFVLFL FYTSISIIYF FTLLIKRSIE LVTKYTMEKT LPSFDLLHLF LLGILIIILI
     IAGISIMALL WTQIALISKG LTTIEHEDKK RKYQQPNYLN LYKKYDKGSI ISNFSIVFGN
     LSFLWLLPTI PNNLKITSKK GDIFIV
 
 
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