PORCN_ANOGA
ID PORCN_ANOGA Reviewed; 495 AA.
AC Q7Q3N5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein-serine O-palmitoleoyltransferase porcupine {ECO:0000250|UniProtKB:Q9JJJ7};
DE EC=2.3.1.250 {ECO:0000250|UniProtKB:Q9JJJ7};
GN Name=por {ECO:0000250|UniProtKB:Q9VWV9}; ORFNames=AGAP007962;
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:EAA12856.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|EMBL:EAA12856.1};
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).
CC -!- FUNCTION: Protein-serine O-palmitoleoyltransferase that acts as a key
CC regulator of the Wnt signaling pathway by mediating the attachment of
CC palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1), to Wnt
CC proteins. Serine palmitoleylation of WNT proteins is required for
CC efficient binding to frizzled receptors.
CC {ECO:0000250|UniProtKB:Q9JJJ7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + [Wnt protein]-L-serine = [Wnt
CC protein]-O-(9Z)-hexadecenoyl-L-serine + CoA; Xref=Rhea:RHEA:45336,
CC Rhea:RHEA-COMP:11170, Rhea:RHEA-COMP:11171, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:85189;
CC EC=2.3.1.250; Evidence={ECO:0000250|UniProtKB:Q9JJJ7};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9VWV9}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9VWV9}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Porcupine subfamily. {ECO:0000305}.
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DR EMBL; AAAB01008964; EAA12856.1; -; Genomic_DNA.
DR RefSeq; XP_317509.1; XM_317509.1.
DR AlphaFoldDB; Q7Q3N5; -.
DR STRING; 7165.AGAP007962-PA; -.
DR PaxDb; Q7Q3N5; -.
DR GeneID; 1277989; -.
DR KEGG; aga:AgaP_AGAP007962; -.
DR CTD; 1277989; -.
DR VEuPathDB; VectorBase:AGAP007962; -.
DR eggNOG; KOG4312; Eukaryota.
DR HOGENOM; CLU_048745_0_0_1; -.
DR InParanoid; Q7Q3N5; -.
DR OMA; GMDFRIY; -.
DR OrthoDB; 975725at2759; -.
DR PhylomeDB; Q7Q3N5; -.
DR Proteomes; UP000007062; Chromosome 3R.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:1990698; F:palmitoleoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0006497; P:protein lipidation; ISS:UniProtKB.
DR GO; GO:0045234; P:protein palmitoleylation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IBA:GO_Central.
DR GO; GO:0061355; P:Wnt protein secretion; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT CHAIN 1..495
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /id="PRO_0000213139"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 376
FT /evidence="ECO:0000250|UniProtKB:Q9H237"
SQ SEQUENCE 495 AA; 56957 MW; 490DEDBAF719616E CRC64;
MDYYYDDYYD EYYDHPDQAA ARLFHRDLSI EETIKNCVHP SLRFATQYIT NFIAINLLFS
VLVLIVRKLF PTAQRSLHLL SCVCGAALVY RVIDHGFYHF LQLAVSLYAV QWTLHRWLTG
TGRYIKTPFI VIAYGIGNLL VSELLEPSPE TWNRIRGTQM ILLMKALSLA FDTDDNHSLR
SQLTVLSYSG YILCPANIVL GPWISFNDYL TIWKPPAGIE PKQCRSSSGR RMLIHVFRIV
TSALMAVGFL LTSNCMIDYL LAPINSWKWV RAYGRALSFR TSHYFIGYLS QCSMMAAAAD
WHRAEDERSI MLPVSSLYRI TSPMAVEFPR SLVQVVTAWN IPMHLWLKRY IFRTTKRPFG
TGTAIALTYI ISSLLHGLHY RLWITLLTIG SWTFVEHEVR KKLATIYSAC VLVGKCPSSC
TVHQHKSNSV FCTVINMLFF ALNIFNLIYL GCIFESSEGP PDEVQQDKSM FGPWTELNYA
SHWLLVFAYL FYFVI
