ID   F1PMM2_CANLF            Unreviewed;       622 AA.
AC   F1PMM2;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 2.
DT   16-MAR-2016, entry version 38.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   Name=ZDHHC13 {ECO:0000313|Ensembl:ENSCAFP00000013856};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000013856, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000013856, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000013856,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C.,
RA   Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A.,
RA   Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F.,
RA   Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A.,
RA   Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M.,
RA   Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L.,
RA   Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J.,
RA   Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L.,
RA   Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A.,
RA   Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N.,
RA   Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A.,
RA   Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N.,
RA   Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N.,
RA   Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K.,
RA   Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G.,
RA   Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E.,
RA   Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C.,
RA   Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L.,
RA   Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C.,
RA   Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T.,
RA   Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J.,
RA   Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J.,
RA   Marabella R., Maru K., Matthews C., McDonough S., Mehta T.,
RA   Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K.,
RA   Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J.,
RA   Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K.,
RA   Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F.,
RA   Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C.,
RA   Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S.,
RA   Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J.,
RA   Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S.,
RA   Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S.,
RA   Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T.,
RA   Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X.,
RA   Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000013856}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000013856};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + [protein]-L-cysteine =
CC       [protein]-S-palmitoyl-L-cysteine + CoA.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity. {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Contains 1 DHHC-type zinc finger.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Contains 6 ANK repeats.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSCAFP00000013856}.
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DR   EMBL; AAEX03012973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX03012974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005633806.1; XM_005633749.2.
DR   STRING; 9615.ENSCAFP00000013856; -.
DR   PaxDb; F1PMM2; -.
DR   Ensembl; ENSCAFT00000014970; ENSCAFP00000013856; ENSCAFG00000009410.
DR   GeneID; 613004; -.
DR   KEGG; cfa:613004; -.
DR   CTD; 54503; -.
DR   eggNOG; KOG0509; Eukaryota.
DR   eggNOG; COG0666; LUCA.
DR   eggNOG; COG5273; LUCA.
DR   GeneTree; ENSGT00530000063074; -.
DR   InParanoid; F1PMM2; -.
DR   KO; K18932; -.
DR   OMA; HCATTFR; -.
DR   TreeFam; TF317342; -.
DR   Proteomes; UP000002254; Chromosome 21.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:Ensembl.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR030290; ZDHHC13.
DR   InterPro; IPR001594; Znf_DHHC_palmitoyltrfase.
DR   PANTHER; PTHR24161:SF16; PTHR24161:SF16; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01529; zf-DHHC; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50216; ZF_DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW   ANK repeat {ECO:0000256|RuleBase:RU079119};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002254};
KW   Membrane {ECO:0000256|RuleBase:RU079119};
KW   Metal-binding {ECO:0000256|RuleBase:RU079119,
KW   ECO:0000256|SAAS:SAAS00517379};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254};
KW   Repeat {ECO:0000256|RuleBase:RU079119};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119};
KW   Zinc {ECO:0000256|RuleBase:RU079119, ECO:0000256|SAAS:SAAS00517407};
KW   Zinc-finger {ECO:0000256|RuleBase:RU079119,
KW   ECO:0000256|SAAS:SAAS00517361}.
FT   TRANSMEM    292    310       Helical. {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM    316    338       Helical. {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM    345    368       Helical. {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM    374    392       Helical. {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM    470    487       Helical. {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM    519    539       Helical. {ECO:0000256|RuleBase:RU079119}.
FT   DOMAIN       48    269       ANK_REP_REGION. {ECO:0000259|PROSITE:
FT                                PS50297}.
FT   DOMAIN      426    476       DHHC-type. {ECO:0000259|PROSITE:PS50216}.
SQ   SEQUENCE   622 AA;  71267 MW;  ADDDE15DE579552D CRC64;
     MEGPGLGSQC RNHSHGPHPP GFGRHGICAY ESKELAKARE ALPLIEDSSN CDIVKATQYG
     IFERCKELVE AGYDVRQPDK ENVSLLHWAA INNRLDLVKY YISKGAVVDQ LGGDLNSTPL
     HWAIRQGHLP MVILLLQYGA DPTLIDGEGF SSIHLAVLFQ HMPIIAYLIS KGQSVNMTDL
     NGQTPLMLSA HKVLGPEPTG FLLKFNPSLN VVDKTHQNTP LHWAVAAGNV NAVDKLLEAG
     SRLDIRNVKG ETPLDMALQN KNRLIIHMLK TEAKMRANEK FRLWRWLQKC ELFLLLMLSV
     ITMWAVGYIL DFNSDSWLLK GCLLLTLFFL TSLLPRFLVG YKSLIYLPTV FLLSSIFWIF
     VTWFILFFPH LAGTPFYFAF LLSIIGFLYF FYKTWATDPG FTKASEEERK TNIITLAETG
     CLDFRTFCTS CLIRKPLRSL HCHVCNSCVA RYDQHCLWTG RCIGFGNHRY YIFFLFFLSI
     VCDWIMYESF IYWSNHCTTT FREDGLWTYL NQIVACSPWV LYIFMLAAFH FSWSTFLLLN
     QLFQIAFLGL TSHERTSLLK QSRHMKQTLS LRRTPYNLGF TQNLADFFQC GCFGLVKPCA
     VDWTSQYTMV FHPAKEKVLR SV
//