ID A0A016WWQ0_9BILA Unreviewed; 278 AA.
AC A0A016WWQ0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Protein-serine O-palmitoleoyltransferase porcupine {ECO:0000256|ARBA:ARBA00040371};
DE EC=2.3.1.250 {ECO:0000256|ARBA:ARBA00038867};
GN Name=Acey_s0493.g2432 {ECO:0000313|EMBL:EYC43453.1};
GN Synonyms=Acey-mom-1 {ECO:0000313|EMBL:EYC43453.1};
GN ORFNames=Y032_0493g2432 {ECO:0000313|EMBL:EYC43453.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC43453.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:0000256|ARBA:ARBA00035752};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Porcupine subfamily. {ECO:0000256|ARBA:ARBA00038269}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC43453.1}.
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DR EMBL; JARK01000093; EYC43453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016WWQ0; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13906; PORCUPINE; 1.
DR PANTHER; PTHR13906:SF12; PROTEIN-SERINE O-PALMITOLEOYLTRANSFERASE PORCUPINE; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..278
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001494984"
FT TRANSMEM 35..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..236
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 278 AA; 30711 MW; E327ABA28D0E4A0D CRC64;
MLAILAGALC LVFLVAVSAS QYKGFTITCA CIASILLLQY FTSASEFVAV RGIVMVLAMK
ISSLAFDQRN SARLADLIPF LAYLANPATL IFGPFHTFQE FETTLNRKEW LLSCIAGIVL
VVIAICLLIY SSCMTIVVPE GSIFSDYFTA QSFRTSHYFV SFLSQGLLTL SGLRLAVCSP
LSVEFPRSLV EVVVAWNIPM HRYLHSCEFY HNVYVNVIPF GAAAAIFASF AISSLLHRYE
IESQTVFPYA CVLVTAENVS IKEDGYVIYE SCLLYLIA
//