PORCN_CAEBR
ID PORCN_CAEBR Reviewed; 444 AA.
AC A8WZ09;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein-serine O-palmitoleoyltransferase porcupine {ECO:0000250|UniProtKB:Q9JJJ7};
DE EC=2.3.1.250 {ECO:0000250|UniProtKB:Q9JJJ7};
DE AltName: Full=More of ms protein 1 {ECO:0000250|UniProtKB:Q22329};
GN Name=mom-1 {ECO:0000250|UniProtKB:Q22329}; ORFNames=CBG05032;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- FUNCTION: Key regulator of the Wnt signaling pathway that mediates
CC lipid modification of Wnt proteins. Acts as a protein-serine O-
CC palmitoleoyltransferase that catalyzes the attachment of palmitoleate,
CC a 16-carbon monounsaturated fatty acid (C16:1), to Wnt proteins. Serine
CC palmitoleylation of WNT proteins is required for efficient binding to
CC frizzled receptors. Has a role in cell specification, specifically in
CC blastomere signaling. Involved in cytosketetal polarity. Required for
CC the orientation of mitotic spindle axis. {ECO:0000250|UniProtKB:Q22329,
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: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Porcupine subfamily. {ECO:0000305}.
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DR EMBL; HE600917; CAP25618.1; -; Genomic_DNA.
DR RefSeq; XP_002644859.1; XM_002644813.1.
DR AlphaFoldDB; A8WZ09; -.
DR STRING; 6238.CBG05032; -.
DR GeneID; 8586855; -.
DR KEGG; cbr:CBG_05032; -.
DR CTD; 8586855; -.
DR WormBase; CBG05032; CBP39278; WBGene00027587; Cbr-mom-1.
DR eggNOG; KOG4312; Eukaryota.
DR HOGENOM; CLU_619997_0_0_1; -.
DR InParanoid; A8WZ09; -.
DR OMA; GMDFRIY; -.
DR OrthoDB; 975725at2759; -.
DR Proteomes; UP000008549; Chromosome X.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0007367; P:segment polarity determination; IEA:UniProtKB-KW.
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; Developmental protein; Membrane; Reference proteome;
KW Segmentation polarity protein; Transferase; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT CHAIN 1..444
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /id="PRO_0000397907"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..440
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 323
FT /evidence="ECO:0000250|UniProtKB:Q9H237"
SQ SEQUENCE 444 AA; 51361 MW; B94A16C370492C95 CRC64;
MDHHLDPNLD NLFEMYGESV EECATQVANG TLLTLLQMLV LVWMFFLVWR LSLPPRIQTF
LHIAMTTLTV AWFSPKKLES VMIFHTFSLI SLFCAVQKLN GYRILGLNIM LLIALQNICS
RANADDYFLT LRGVLMMHIM RLSTASFAIV DSNVRSISFD QLTLYLEYIY FPPFIIFGPY
VTFDQFVKMR EKKWTRFEEQ LGVFVQGSVL IFIGITLAII SSCYVDFFEP GSQFVEDALT
AMSFRCSHYF ICLSTQAFAM FLGSKIVVAN PVNIEFSRST LQTVSEWNRP FHTYLHENIF
KRRFFQSTAL NVLLTFAVSA LLHARDYQMW LTLLALGFIA YSETVFRKRI ADRFSMCVAA
KPCSVRANRR ICKHKHASFS KRVLIINLFF MILSMYHLVF TGMTFTDDYA AIGYPFSHTW
TIWGTHYYSS FIVSFAFLAL SKII
