ID F5HLQ3_ANOGA Unreviewed; 809 AA.
AC F5HLQ3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN Name=1274788 {ECO:0000313|EnsemblMetazoa:AGAP005111-PB};
GN ORFNames=AgaP_AGAP005111 {ECO:0000313|EMBL:EGK97214.1};
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165 {ECO:0000313|EMBL:EGK97214.1};
RN [1] {ECO:0000313|EMBL:EGK97214.1, ECO:0000313|Proteomes:UP000007062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97214.1,
RC ECO:0000313|Proteomes:UP000007062};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000313|EMBL:EGK97214.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97214.1};
RG The Anopheles Genome Sequencing Consortium;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EGK97214.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97214.1};
RX PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT "The Anopheles gambiae genome: an update.";
RL Trends Parasitol. 20:49-52(2004).
RN [4] {ECO:0000313|EMBL:EGK97214.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97214.1};
RX PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT "Update of the Anopheles gambiae PEST genome assembly.";
RL Genome Biol. 8:R5.1-R5.13(2007).
RN [5] {ECO:0000313|EMBL:EGK97214.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PEST {ECO:0000313|EMBL:EGK97214.1};
RG VectorBase;
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblMetazoa:AGAP005111-PB}
RP IDENTIFICATION.
RC STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP005111-PB};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
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:0000256|RuleBase:RU079119};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000256|RuleBase:RU079119}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000256|RuleBase:RU079119}.
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DR EMBL; AAAB01008900; EGK97214.1; -; Genomic_DNA.
DR RefSeq; XP_003435719.1; XM_003435671.1.
DR AlphaFoldDB; F5HLQ3; -.
DR EnsemblMetazoa; AGAP005111-RB; AGAP005111-PB; AGAP005111.
DR GeneID; 1274788; -.
DR KEGG; aga:AgaP_AGAP005111; -.
DR VEuPathDB; VectorBase:AGAP005111; -.
DR eggNOG; ENOG502T8NX; Eukaryota.
DR HOGENOM; CLU_018741_6_0_1; -.
DR OrthoDB; 5480099at2759; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR22883:SF43; PALMITOYLTRANSFERASE APP; 1.
DR PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU079119}; Membrane {ECO:0000256|RuleBase:RU079119};
KW Reference proteome {ECO:0000313|Proteomes:UP000007062};
KW Transferase {ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 64..85
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 180..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 224..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 134..259
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 446..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 809 AA; 86775 MW; 3BBA2D2D552D0C7B CRC64;
MAPSQKVTKK WEIFAGRNKF FCDGYLMTAP NSGVFYFTVI LITATSGLFF VFDCPFLAQR
ITPAIPIIGG ILFVFTLSSL FRTAFSDPGI IPRASQDEAA YIEKQIEVPN SLNSPTYRPP
PRTKEVFVKG QTVKLKYCFT CKIFRPPRAS HCSLCDNCVD RFDHHCPWVG NCVGKRNYRF
FYMFIVSLAF LAVFIFSCTT THIVMLLKED NQFIDVVKRT PSSVIIAIIC FCSVWSVIGL
AGFHTYLTTS DQTTNEDIKG SFSSKGGQQA INPYSQGNIC LNCFHILCGP ITPSLIDRRG
VVTDEYRTQM QATEKYNSAT VPPLVVMQPG MDTLNKHYSM EHELQNASNG GGVGGTGVYR
QRSYDNLQND KSNSVAHLVE NEAPLSTTGN VSILSGGAGG GLEDTTTTTV LLDEDGMELE
TRGMGGGPSM DDSSNQLTGS YTNLFRDSMS NGVANGPSGG GQPGKPNNSY HHHSSMMMSE
CDKIQSADEI INVSELMMVC SVSGHENVYS NVPPAQISPS GSAVGLLASP KRASVGSSNV
SGVVDVSSST VGPGGYQHVY SNVTSPCGPA AAEQLPTGVS TGTGGISGSQ QQQQHIHPAL
GNGKHHQQQQ HHQHHHHPHH QLALDDPSQL LSSTFISNDL DLDDPVLSSS FATATKSTAN
TMTKLHPPPA PSSAAGGPMV AAQQQHLKQP QAMITTIEMK NVIKTLDPNV IIQQQASSNG
ASGTTAAVSS SANVIDSNGG IASMHNNTTT TNNNNNNSHT ESPMFISPSA SRMRLLQEST
MIDTALDLDS LDGSIGNHSQ SCLVKTAIV
//
