PORCN_CAEEL
ID PORCN_CAEEL Reviewed; 442 AA.
AC Q22329; O16142;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein-serine O-palmitoleoyltransferase porcupine {ECO:0000250|UniProtKB:Q9JJJ7};
DE Short=Porc {ECO:0000303|PubMed:15020416};
DE EC=2.3.1.250 {ECO:0000250|UniProtKB:Q9JJJ7};
DE AltName: Full=More of ms protein 1 {ECO:0000303|PubMed:15020416};
GN Name=mom-1 {ECO:0000312|WormBase:T07H6.2}; ORFNames=T07H6.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9288750; DOI=10.1016/s0092-8674(00)80531-0;
RA Rocheleau C.E., Downs W.D., Lin R., Wittmann C., Bei Y., Cha Y.-H., Ali M.,
RA Priess J.R., Mello C.C.;
RT "Wnt signaling and an APC-related gene specify endoderm in early C. elegans
RT embryos.";
RL Cell 90:707-716(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9288749; DOI=10.1016/s0092-8674(00)80530-9;
RA Thorpe C.J., Schlesinger A., Carter J.C., Bowerman B.;
RT "Wnt signaling polarizes an early C. elegans blastomere to distinguish
RT endoderm from mesoderm.";
RL Cell 90:695-705(1997).
RN [4]
RP FUNCTION.
RX PubMed=10444600; DOI=10.1101/gad.13.15.2028;
RA Schlesinger A., Shelton C.A., Maloof J.N., Meneghini M.D., Bowerman B.;
RT "Wnt pathway components orient a mitotic spindle in the early
RT Caenorhabditis elegans embryo without requiring gene transcription in the
RT responding cell.";
RL Genes Dev. 13:2028-2038(1999).
RN [5]
RP IDENTIFICATION OF MBOAT FAMILY.
RX PubMed=10694878; DOI=10.1016/s0968-0004(99)01539-x;
RA Hofmann K.;
RT "A superfamily of membrane-bound O-acyltransferases with implications for
RT wnt signaling.";
RL Trends Biochem. Sci. 25:111-112(2000).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15020416; DOI=10.1534/genetics.166.1.171;
RA Siegfried K.R., Kidd A.R. III, Chesney M.A., Kimble J.;
RT "The sys-1 and sys-3 genes cooperate with Wnt signaling to establish the
RT proximal-distal axis of the Caenorhabditis elegans gonad.";
RL Genetics 166:171-186(2004).
CC -!- FUNCTION: Key regulator of the Wnt signaling pathway that mediates
CC lipid modification of Wnt proteins (PubMed:10444600, PubMed:15020416,
CC PubMed:9288750). Acts as a protein-serine O-palmitoleoyltransferase
CC that catalyzes the attachment of palmitoleate, a 16-carbon
CC monounsaturated fatty acid (C16:1), to Wnt proteins (By similarity).
CC Serine palmitoleylation of WNT proteins is required for efficient
CC binding to frizzled receptors (By similarity). Has a role in cell
CC specification, specifically in blastomere signaling (PubMed:10444600,
CC PubMed:15020416, PubMed:9288750). Involved in cytosketetal polarity
CC (PubMed:10444600, PubMed:15020416, PubMed:9288750). Required for the
CC orientation of mitotic spindle axis (PubMed:9288749, PubMed:10444600,
CC PubMed:15020416, PubMed:9288750). {ECO:0000250|UniProtKB:Q9JJJ7,
CC ECO:0000269|PubMed:10444600, ECO:0000269|PubMed:15020416,
CC ECO:0000269|PubMed:9288749, ECO:0000269|PubMed:9288750}.
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 -!- DISRUPTION PHENOTYPE: Embryonic lethal with severely defective
CC embryonic morphogenesis with no endoderm and excess mesoderm. In
CC addition, embryos have defective mitotic spindle orientation in the 8-
CC cell stage ABar blastomere. {ECO:0000269|PubMed:15020416,
CC ECO:0000269|PubMed:9288749, ECO:0000269|PubMed:9288750}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Porcupine subfamily. {ECO:0000305}.
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DR EMBL; AF013489; AAC47728.1; -; mRNA.
DR EMBL; FO081717; CCD74393.1; -; Genomic_DNA.
DR PIR; T16834; T16834.
DR PIR; T42048; T42048.
DR RefSeq; NP_509054.1; NM_076653.3.
DR AlphaFoldDB; Q22329; -.
DR BioGRID; 45834; 3.
DR DIP; DIP-27046N; -.
DR IntAct; Q22329; 1.
DR STRING; 6239.T07H6.2; -.
DR PaxDb; Q22329; -.
DR EnsemblMetazoa; T07H6.2.1; T07H6.2.1; WBGene00003394.
DR GeneID; 180904; -.
DR KEGG; cel:CELE_T07H6.2; -.
DR UCSC; T07H6.2; c. elegans.
DR CTD; 180904; -.
DR WormBase; T07H6.2; CE25982; WBGene00003394; mom-1.
DR eggNOG; KOG4312; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_619997_0_0_1; -.
DR InParanoid; Q22329; -.
DR OMA; GMDFRIY; -.
DR OrthoDB; 975725at2759; -.
DR PhylomeDB; Q22329; -.
DR BRENDA; 2.3.1.250; 1045.
DR SignaLink; Q22329; -.
DR PRO; PR:Q22329; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003394; Expressed in embryo and 4 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:WormBase.
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; ISS:WormBase.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR GO; GO:0070986; P:left/right axis specification; IGI:UniProtKB.
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; ISS:WormBase.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:WormBase.
DR GO; GO:0061359; P:regulation of Wnt signaling pathway by Wnt protein secretion; ISS:WormBase.
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 GO; GO:0060069; P:Wnt signaling pathway, regulating spindle positioning; IMP:WormBase.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Developmental protein; Membrane; Reference proteome;
KW Segmentation polarity protein; Transferase; Transmembrane;
KW Transmembrane helix; Wnt signaling pathway.
FT CHAIN 1..442
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /id="PRO_0000397908"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 321
FT /evidence="ECO:0000250|UniProtKB:Q9H237"
SQ SEQUENCE 442 AA; 50874 MW; EFF205467C29A822 CRC64;
MDNGHGYEEF ELLEDGSLGE CSTQVANATF LTISKLICLV VAFKFIKHIP ISTTVRVYVH
VFASTFTVMW FSRNHLQSAI IYNMFSLISL ALAIKQFSGY IILAGNISLL IALQNFCRHY
RSEDYFLSIR GILMIHIMRL TTVAFNLEKA NSNKFRFVQF SSYVEYIYFP PFIIFGPYLS
FEQFFKMRDK KWTGSENELG FIIQSLLAIF NAITLAIISS CHFEFFEPSS QFMEDALTAM
SFRFSHYFVC LSTQAFVLML GSDVVVANPL NIEFSRSTLQ TVSEWNKPFH TFLHENIFKR
RLFNSTACNV FFTFAVSSLL HGLDFQMTIT LLALGFIAYS ETVFRKRLSA RYSMCVAAKA
CPVRSNSLSC KHRHSNKTGR ALIINLFFLM LSMYHLVFTG MTFTDDYSAI GYPFDHAWKI
WGSHYYSSFM ISFLFLALSK II
