ZDHC7_DICDI
ID ZDHC7_DICDI Reviewed; 438 AA.
AC Q552M6; Q86JC6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Putative ZDHHC-type palmitoyltransferase 7;
DE EC=2.3.1.225;
DE AltName: Full=Zinc finger DHHC domain-containing protein 7;
GN ORFNames=DDB_G0276017;
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:EAL69465.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69465.1};
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 1-60 AND 298-438.
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}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000013; EAL69465.1; -; Genomic_DNA.
DR EMBL; AU074197; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; C91183; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_643386.1; XM_638294.1.
DR AlphaFoldDB; Q552M6; -.
DR PaxDb; Q552M6; -.
DR EnsemblProtists; EAL69465; EAL69465; DDB_G0276017.
DR GeneID; 8620271; -.
DR KEGG; ddi:DDB_G0276017; -.
DR dictyBase; DDB_G0276017; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_626174_0_0_1; -.
DR InParanoid; Q552M6; -.
DR OMA; NNKYYSC; -.
DR PRO; PR:Q552M6; -.
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..438
FT /note="Putative ZDHHC-type palmitoyltransferase 7"
FT /id="PRO_0000262946"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 249..299
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 183..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 12
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 352
FT /note="F -> Y (in Ref. 3; C91183)"
FT /evidence="ECO:0000305"
FT CONFLICT 434..438
FT /note="Missing (in Ref. 3; C91183)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 50297 MW; 832C08B0D3ABBC0A CRC64;
MKLNSNINNN INNSSNSNNN FDAKNIIVDT ITPPDPSVEF ERKLAKSIFC LVHFIVYCVI
IFRKGTILDQ AFKDKDYFYL IWTHCVFFFA IGTYFLISSK RPGFVSLSNQ NLNNNNNNNG
SSNKFILEDS MGCIPQLNIN PTPNYSKISN IKRKLKNSSG DITKNQENED LVPLMEISKN
IDEDSINDDT ITTTTTTTTT TSTSTIPEIS NDDDDNNNEN NNDNVNNRNN NNSNGEKEDN
DIDKLKNHYF CKKCLVDIPL RTKHCVKCNR CVLKYDHHCV FIGGCVGLNN HKNFLLFLLA
ESLLLLLGLR IIVTGFVREN SIKEWIFSNI AIIPPTLLIF GGLCMPFALF CFHSFLILTN
QSSWEFNKYQ RITYLKPFSK RGINPFNKGP WNNLKKFLKG DENPSDWILL SKYEVDQMKK
KEENTFNIWN NKYYSCCG
