ZDHC6_DICDI
ID ZDHC6_DICDI Reviewed; 698 AA.
AC Q8T2Q0; Q554I2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Putative ZDHHC-type palmitoyltransferase 6;
DE EC=2.3.1.225;
DE AltName: Full=Zinc finger DHHC domain-containing protein 6;
GN ORFNames=DDB_G0275149;
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:EAL69855.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4 {ECO:0000312|EMBL:EAL69855.1};
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 184-256 AND 623-698.
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:Q8IUH5}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000255}.
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; AAFI02000013; EAL69855.1; -; Genomic_DNA.
DR EMBL; AU053808; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AU060436; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_643729.1; XM_638637.1.
DR AlphaFoldDB; Q8T2Q0; -.
DR SMR; Q8T2Q0; -.
DR STRING; 44689.DDB0167498; -.
DR PaxDb; Q8T2Q0; -.
DR EnsemblProtists; EAL69855; EAL69855; DDB_G0275149.
DR GeneID; 8619769; -.
DR KEGG; ddi:DDB_G0275149; -.
DR dictyBase; DDB_G0275149; -.
DR eggNOG; KOG0509; Eukaryota.
DR HOGENOM; CLU_395076_0_0_1; -.
DR InParanoid; Q8T2Q0; -.
DR OMA; WACIGGD; -.
DR PhylomeDB; Q8T2Q0; -.
DR PRO; PR:Q8T2Q0; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; ANK repeat; Glycoprotein; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..698
FT /note="Putative ZDHHC-type palmitoyltransferase 6"
FT /id="PRO_0000259995"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 58..87
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 92..121
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 125..155
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 159..188
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 192..221
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT DOMAIN 395..445
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT REGION 532..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..653
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 425
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 555
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 698 AA; 79314 MW; 876469CF336CC973 CRC64;
MIDHNNIIIG NSINSKTFSL IESVKNGKLK ECIGYLEKIR LQNPSLDLGE IINSGDDCGN
TALHWACYKK WYDIVKYLLS MGADPNIANT DELQTPFQWA CIGGDLHIVK YVLNNGGDPH
LQDKRGYNSL IHATQYNEIS VVRYLLDKGG VNVDSPDFLQ KTSLHWAAYQ GHTQLLLFLV
NKGADINALD SLGRSPLHWA AFKGNSDPIK ALCDFGSKTM EKDSNNQSPS DICSSQNHNY
LAHFIKTFNY HPFRKVGPLL YNIFWIIFAI LLQLYFGFIF YHFTLIPALI LFGASLTCCK
LFIEPITLSN SPNPLLPTWM ITSFTVSFVY YVRYVVPAFP NIILTHTITL FVYSSYYYCA
FKLFFSDPGT VSSSTTSQDS KDFINAVEKE LEIPEVCSTC LINKPIRAKH CRTCKRCVAR
FDHHCAWINN CVGVNNNLLF IILLCLFSLA YIISVTFNFK LMSIDENSPL YSEGKMEWWT
YHYSTYKGLI LFTIYKSFIM AWLARLLYVQ ITGVINNVTM FELMKPPKGS KKKCCNHAPQ
DQNNNNNNNN TTTNNSSSSS SSNNNSTGTN NDNNNNNNLG TSSNESGQSN CNIDQHNDHD
GQSSEPLLNE VSIQIRSENG VEEDDDDENN KNPSNKSFNK NSRDLDPTQT NFRDSILIPK
RTNNNENPYD KGSRENIREF LYDTSKWFRT TTFSNKNF
