PORCN_DROME
ID PORCN_DROME Reviewed; 525 AA.
AC Q9VWV9; Q94549;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
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:0000312|FlyBase:FBgn0004957};
GN Synonyms=porc {ECO:0000303|PubMed:11821428}; ORFNames=CG6205;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8985181; DOI=10.1101/gad.10.24.3116;
RA Kadowaki T., Wilder E., Klingensmith J., Zachary K., Perrimon N.;
RT "The segment polarity gene porcupine encodes a putative multitransmembrane
RT protein involved in Wingless processing.";
RL Genes Dev. 10:3116-3128(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39723.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, GLYCOSYLATION OF WG AND WNT5, INTERACTION WITH WG AND WNT5, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11821428; DOI=10.1074/jbc.m200187200;
RA Tanaka K., Kitagawa Y., Kadowaki T.;
RT "Drosophila segment polarity gene product porcupine stimulates the
RT posttranslational N-glycosylation of wingless in the endoplasmic
RT reticulum.";
RL J. Biol. Chem. 277:12816-12823(2002).
RN [6]
RP FUNCTION.
RX PubMed=15166250; DOI=10.1074/jbc.m403407200;
RA Zhai L., Chaturvedi D., Cumberledge S.;
RT "Drosophila wnt-1 undergoes a hydrophobic modification and is targeted to
RT lipid rafts, a process that requires porcupine.";
RL J. Biol. Chem. 279:33220-33227(2004).
RN [7]
RP FUNCTION.
RX PubMed=22108505; DOI=10.1016/j.ydbio.2011.11.003;
RA Herr P., Basler K.;
RT "Porcupine-mediated lipidation is required for Wnt recognition by Wls.";
RL Dev. Biol. 361:392-402(2012).
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 (By similarity). Also
CC facilitates the glycosylation of Wnt family members, including wg and
CC Wnt5. The cotranslational disulfide bond formation of wg competes with
CC the N-glycosylation. Porc stimulates the post-translational N-
CC glycosylation by anchoring wg at the ER membrane, probably through
CC acylation (PubMed:11821428, PubMed:15166250, PubMed:22108505,
CC PubMed:8985181). {ECO:0000250|UniProtKB:Q9JJJ7,
CC ECO:0000269|PubMed:11821428, ECO:0000269|PubMed:15166250,
CC ECO:0000269|PubMed:22108505, ECO:0000269|PubMed:8985181}.
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 -!- SUBUNIT: Interacts with wg and Wnt5. {ECO:0000269|PubMed:11821428}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11821428, ECO:0000269|PubMed:8985181}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11821428,
CC ECO:0000269|PubMed:8985181}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:8985181}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Porcupine subfamily. {ECO:0000305}.
CC -!- CAUTION: Was initially thought to mediate palmitoylation of Wnt
CC proteins. It was later shown that it instead acts as a serine O-
CC palmitoleoyltransferase that mediates the attachment of palmitoleate, a
CC 16-carbon monounsaturated fatty acid (C16:1), to Wnt proteins.
CC {ECO:0000305}.
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DR EMBL; U77310; AAB18992.1; -; mRNA.
DR EMBL; AE014298; AAF48828.1; -; Genomic_DNA.
DR EMBL; AY069578; AAL39723.1; -; mRNA.
DR RefSeq; NP_001259679.1; NM_001272750.1.
DR RefSeq; NP_001259680.1; NM_001272751.1.
DR RefSeq; NP_476890.1; NM_057542.3.
DR AlphaFoldDB; Q9VWV9; -.
DR BioGRID; 59135; 11.
DR IntAct; Q9VWV9; 3.
DR STRING; 7227.FBpp0305446; -.
DR TCDB; 2.A.50.3.2; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR PaxDb; Q9VWV9; -.
DR DNASU; 32818; -.
DR EnsemblMetazoa; FBtr0074577; FBpp0074349; FBgn0004957.
DR EnsemblMetazoa; FBtr0310487; FBpp0302628; FBgn0004957.
DR EnsemblMetazoa; FBtr0333247; FBpp0305446; FBgn0004957.
DR GeneID; 32818; -.
DR KEGG; dme:Dmel_CG6205; -.
DR UCSC; CG6205-RA; d. melanogaster.
DR CTD; 5447; -.
DR FlyBase; FBgn0004957; por.
DR VEuPathDB; VectorBase:FBgn0004957; -.
DR eggNOG; KOG4312; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_048745_0_0_1; -.
DR InParanoid; Q9VWV9; -.
DR OMA; YIYSPAT; -.
DR OrthoDB; 975725at2759; -.
DR PhylomeDB; Q9VWV9; -.
DR BRENDA; 2.3.1.250; 1994.
DR SignaLink; Q9VWV9; -.
DR BioGRID-ORCS; 32818; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32818; -.
DR PRO; PR:Q9VWV9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0004957; Expressed in embryonic/larval hemocyte (Drosophila) and 24 other tissues.
DR ExpressionAtlas; Q9VWV9; baseline and differential.
DR Genevisible; Q9VWV9; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:UniProtKB.
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:0016409; F:palmitoyltransferase activity; IMP:FlyBase.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0006497; P:protein lipidation; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IMP:UniProtKB.
DR GO; GO:0045234; P:protein palmitoleylation; ISS:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IMP:UniProtKB.
DR GO; GO:0009306; P:protein secretion; IMP:UniProtKB.
DR GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0061355; P:Wnt protein secretion; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT CHAIN 1..525
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /id="PRO_0000213140"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 505..525
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 398
FT /evidence="ECO:0000250|UniProtKB:Q9H237"
FT CONFLICT 463
FT /note="A -> V (in Ref. 1; AAB18992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 59195 MW; D9C402A5F49423F9 CRC64;
MDYQYFEEES DYIDLDEEEE DDDVVTAGSL DHRFGQPNGE EDYYFGGDDV EEELVVDGHG
VLELAGRLLE SLQSCVQPSV LQVMQYVAPM LLLCLLCRLL CLLYSQRRRL TSLAPLHLFH
FACGLIILQI TVGYRLLLLL LLAAVGYLLL QLLRLGRRGA QVLAVLTVGS QFLYELLIWR
RRSDWPQLRG IQMVVNMKLI SLGFDLTASG QLQARIPGPF AYLGYIYSPA TCALGPWVSF
GCYMDCLVPR NSWLVSLRRL LPNVVICVLA VTVSNCVAPA LSDFFGDSSH FLVMYWDALS
VRSSHYFVGM MAQALLVASD QRLDGATKES DMLGPLISQP WRIEWPRSIS SLVRSWNIPM
HEWLKRYIYA PCKPTASTSR GRILVVVLST YLVSSLLHGM DLRIYLVLIS LAFLAEGESL
LRRQLASLLN ACITANLCPG KERCRYSHCP SKRRLNSLSY WLARLTNLAF TALAIFHLAY
LGVVLLGDDL EVGEDGDSFL WHWQQAGYLS HYIGLGTFVL YLFIS
