ZDH24_MOUSE
ID ZDH24_MOUSE Reviewed; 284 AA.
AC Q6IR37; Q3TAY4; Q3TDF1; Q3TF09; Q9CS66;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable palmitoyltransferase ZDHHC24 {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000305};
DE AltName: Full=Zinc finger DHHC domain-containing protein 24 {ECO:0000312|MGI:MGI:1917855};
GN Name=Zdhhc24 {ECO:0000312|MGI:MGI:1917855};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probable palmitoyltransferase that could catalyze the
CC addition of palmitate onto various protein substrates. {ECO:0000305}.
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; Evidence={ECO:0000305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36684;
CC Evidence={ECO:0000305};
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:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30905.2; Type=Frameshift; Evidence={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; AK017737; BAB30905.2; ALT_FRAME; mRNA.
DR EMBL; AK169337; BAE41089.1; -; mRNA.
DR EMBL; AK170233; BAE41651.1; -; mRNA.
DR EMBL; AK170706; BAE41967.1; -; mRNA.
DR EMBL; AK171568; BAE42530.1; -; mRNA.
DR EMBL; BC071194; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS50353.1; -.
DR RefSeq; NP_081752.2; NM_027476.3.
DR AlphaFoldDB; Q6IR37; -.
DR SMR; Q6IR37; -.
DR STRING; 10090.ENSMUSP00000006632; -.
DR PhosphoSitePlus; Q6IR37; -.
DR PaxDb; Q6IR37; -.
DR PRIDE; Q6IR37; -.
DR ProteomicsDB; 275342; -.
DR Antibodypedia; 16343; 99 antibodies from 16 providers.
DR DNASU; 70605; -.
DR Ensembl; ENSMUST00000006632; ENSMUSP00000006632; ENSMUSG00000006463.
DR GeneID; 70605; -.
DR KEGG; mmu:70605; -.
DR UCSC; uc008gbh.2; mouse.
DR CTD; 254359; -.
DR MGI; MGI:1917855; Zdhhc24.
DR VEuPathDB; HostDB:ENSMUSG00000006463; -.
DR eggNOG; KOG1311; Eukaryota.
DR GeneTree; ENSGT00940000162361; -.
DR HOGENOM; CLU_027721_5_2_1; -.
DR InParanoid; Q6IR37; -.
DR OMA; RMHLTWL; -.
DR OrthoDB; 863846at2759; -.
DR PhylomeDB; Q6IR37; -.
DR TreeFam; TF319523; -.
DR BioGRID-ORCS; 70605; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Zdhhc24; mouse.
DR PRO; PR:Q6IR37; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6IR37; protein.
DR Bgee; ENSMUSG00000006463; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; Q6IR37; baseline and differential.
DR Genevisible; Q6IR37; MM.
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; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..284
FT /note="Probable palmitoyltransferase ZDHHC24"
FT /id="PRO_0000233711"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..52
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..166
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..284
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 94..144
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 124
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT CONFLICT 4
FT /note="S -> P (in Ref. 1; BAE41089)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="E -> G (in Ref. 1; BAE41651)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> D (in Ref. 2; BC071194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 30430 MW; 5DEE2138A442364C CRC64;
MGESWAARGA EGAPARMPLV LTALWAAVVV LELAYVMVLG PGPPPLGPLA RALQLALAAY
QLLNLLGNVV LFLRSDPSIR GVMLAGRGLG QGWAYCYQCQ SQVPPRSGHC SACRVCILRR
DHHCRLLGCC VGFHNYRPFL CLLLHSAGVL LHISVLLGPA LSALLQAHSA LYTVALLLLP
WLMLLTGKVS LAQFALAFVV DTCVAGALLC GAGLLFHGML LLRGQTTWEW ARGHHCYDLG
TCHNLQAALG PRWALVWFWP FLASPLPGDG ISFQTPGDVG LVTS
