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Protein-serine O-palmitoleoyltransferase porcupine (EC 2.3.1.-) (Protein MG61)

 PORCN_HUMAN             Reviewed;         461 AA.
Q9H237; B2RBN8; B7ZAR3; Q14829; Q9H234; Q9H235; Q9H236; Q9UJU7;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
27-SEP-2017, entry version 126.
RecName: Full=Protein-serine O-palmitoleoyltransferase porcupine {ECO:0000250|UniProtKB:Q9JJJ7};
EC=2.3.1.- {ECO:0000250|UniProtKB:Q9JJJ7};
AltName: Full=Protein MG61 {ECO:0000303|PubMed:12034504};
Name=PORCN {ECO:0000312|HGNC:HGNC:17652};
Synonyms=MG61 {ECO:0000303|PubMed:12034504}, PORC, PPN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION IN WNT
PROTEINS PROCESSING, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
TISSUE=Hippocampus;
PubMed=12034504; DOI=10.1016/S0378-1119(02)00467-5;
Caricasole A., Ferraro T., Rimland J.M., Terstappen G.C.;
"Molecular cloning and initial characterization of the MG61/PORC gene,
the human homologue of the Drosophila segment polarity gene
Porcupine.";
Gene 288:147-157(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 63-461 (ISOFORM 1).
TISSUE=Retina;
Geraghty M.T.;
Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
[7]
INVOLVEMENT IN FODH.
PubMed=17546031; DOI=10.1038/ng2052;
Grzeschik K.-H., Bornholdt D., Oeffner F., Koenig A.,
del Carmen Boente M., Enders H., Fritz B., Hertl M., Grasshoff U.,
Hoefling K., Oji V., Paradisi M., Schuchardt C., Szalai Z., Tadini G.,
Traupe H., Happle R.;
"Deficiency of PORCN, a regulator of Wnt signaling, is associated with
focal dermal hypoplasia.";
Nat. Genet. 39:833-835(2007).
[8]
FUNCTION.
PubMed=20826466; DOI=10.1242/jcs.072132;
Coombs G.S., Yu J., Canning C.A., Veltri C.A., Covey T.M.,
Cheong J.K., Utomo V., Banerjee N., Zhang Z.H., Jadulco R.C.,
Concepcion G.P., Bugni T.S., Harper M.K., Mihalek I., Jones C.M.,
Ireland C.M., Virshup D.M.;
"WLS-dependent secretion of WNT3A requires Ser209 acylation and
vacuolar acidification.";
J. Cell Sci. 123:3357-3367(2010).
[9]
FUNCTION, PALMITOYLATION AT CYS-187, ACTIVE SITE, AND MUTAGENESIS OF
CYS-187 AND HIS-341.
PubMed=24292069; DOI=10.1038/nchembio.1392;
Gao X., Hannoush R.N.;
"Single-cell imaging of Wnt palmitoylation by the acyltransferase
porcupine.";
Nat. Chem. Biol. 10:61-68(2014).
[10]
VARIANTS FODH ARG-60 AND GLY-365.
PubMed=17546030; DOI=10.1038/ng2057;
Wang X., Reid Sutton V., Omar Peraza-Llanes J., Yu Z., Rosetta R.,
Kou Y.-C., Eble T.N., Patel A., Thaller C., Fang P.,
Van den Veyver I.B.;
"Mutations in X-linked PORCN, a putative regulator of Wnt signaling,
cause focal dermal hypoplasia.";
Nat. Genet. 39:836-838(2007).
[11]
VARIANT FODH GLN-365, AND VARIANT CYS-228.
PubMed=18325042; DOI=10.1111/j.1399-0004.2008.00975.x;
Leoyklang P., Suphapeetiporn K., Wananukul S., Shotelersuk V.;
"Three novel mutations in the PORCN gene underlying focal dermal
hypoplasia.";
Clin. Genet. 73:373-379(2008).
[12]
VARIANTS FODH ARG-331 AND GLN-365.
PubMed=19863546; DOI=10.1111/j.1399-0004.2009.01248.x;
Froyen G., Govaerts K., Van Esch H., Verbeeck J., Tuomi M.L.,
Heikkila H., Torniainen S., Devriendt K., Fryns J.P., Marynen P.,
Jarvela I., Ala-Mello S.;
"Novel PORCN mutations in focal dermal hypoplasia.";
Clin. Genet. 76:535-543(2009).
[13]
VARIANTS FODH VAL-361 AND TYR-385.
PubMed=19277062; DOI=10.1038/ejhg.2009.40;
Harmsen M.B., Azzarello-Burri S., Garcia Gonzalez M.M.,
Gillessen-Kaesbach G., Meinecke P., Muller D., Rauch A., Rossier E.,
Seemanova E., Spaich C., Steiner B., Wieczorek D., Zenker M.,
Kutsche K.;
"Goltz-Gorlin (focal dermal hypoplasia) and the microphthalmia with
linear skin defects (MLS) syndrome: no evidence of genetic overlap.";
Eur. J. Hum. Genet. 17:1207-1215(2009).
[14]
VARIANTS FODH PHE-136; ARG-168; GLU-258; LEU-341; GLN-365; GLY-365;
ARG-385 AND ARG-439.
PubMed=19309688; DOI=10.1002/humu.20992;
Bornholdt D., Oeffner F., Koenig A., Happle R., Alanay Y.,
Ascherman J., Benke P.J., Boente M.C., van der Burgt I., Chassaing N.,
Ellis I., Francisco C.R.I., Della Giovanna P., Hamel B., Has C.,
Heinelt K., Janecke A., Kastrup W., Loeys B., Lohrisch I.,
Marcelis C., Mehraein Y., Nicolas M.E.O., Pagliarini D., Paradisi M.,
Patrizi A., Piccione M., Piza-Katzer H., Prager B., Prescott K.,
Strien J., Utine G.E., Zeller M.S., Grzeschik K.-H.;
"PORCN mutations in focal dermal hypoplasia: coping with lethality.";
Hum. Mutat. 30:E618-E628(2009).
[15]
VARIANTS FODH ARG-168; LEU-297; GLN-365 AND PRO-374.
PubMed=19586929; DOI=10.1136/jmg.2009.068403;
Maas S.M., Lombardi M.P., van Essen A.J., Wakeling E.L., Castle B.,
Temple I.K., Kumar V.K., Writzl K., Hennekam R.C.;
"Phenotype and genotype in 17 patients with Goltz-Gorlin syndrome.";
J. Med. Genet. 46:716-720(2009).
[16]
VARIANTS FODH TYR-252 AND GLN-365.
PubMed=21472892; DOI=10.1002/humu.21505;
Lombardi M.P., Bulk S., Celli J., Lampe A., Gabbett M.T.,
Ousager L.B., van der Smagt J.J., Soller M., Stattin E.L.,
Mannens M.A., Smigiel R., Hennekam R.C.;
"Mutation update for the PORCN gene.";
Hum. Mutat. 32:723-728(2011).
-!- FUNCTION: Protein-serine O-palmitoleoyltransferase that acts as a
key regulator of the Wnt signaling pathway by mediating the
attachment of palmitoleate, a 16-carbon monounsaturated fatty acid
(C16:1), to Wnt proteins. Serine palmitoleylation of WNT proteins
is required for efficient binding to frizzled receptors.
{ECO:0000250|UniProtKB:Q9JJJ7, ECO:0000269|PubMed:12034504,
ECO:0000269|PubMed:20826466, ECO:0000269|PubMed:24292069}.
-!- CATALYTIC ACTIVITY: (9Z)-hexadecenoyl-CoA + [Wnt]-L-serine = CoA +
[Wnt]-O-(9Z)-hexadecenoyl-L-serine.
{ECO:0000250|UniProtKB:Q9JJJ7}.
-!- SUBUNIT: Interacts with WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B,
WNT6, WNT7A and WNT7B. {ECO:0000250|UniProtKB:Q9JJJ7}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q9JJJ7}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q9JJJ7}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=D;
IsoId=Q9H237-1; Sequence=Displayed;
Name=2; Synonyms=B;
IsoId=Q9H237-2; Sequence=VSP_015888;
Name=3; Synonyms=C;
IsoId=Q9H237-3; Sequence=VSP_015887;
Name=4; Synonyms=A;
IsoId=Q9H237-4; Sequence=VSP_015886;
Name=5;
IsoId=Q9H237-5; Sequence=VSP_055419, VSP_015886;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 is expressed in fetal brain, brain,
amygdala, caudate nucleus, cerebellum, hippocampus, pituitary,
thalamus, heart, skeletal muscle and testis. Isoform 4 is
expressed in amygdala, corpus callosum, hippocampus, spinal cord,
kidney, liver, lung, spleen, uterus, testis. Isoform 2 and isoform
3 are expressed in substantia negra, spinal cord, heart and lung.
{ECO:0000269|PubMed:12034504}.
-!- DISEASE: Focal dermal hypoplasia (FODH) [MIM:305600]: A rare
congenital ectomesodermal disorder characterized by a combination
of skin defects, skeletal abnormalities, and ocular anomalies.
Affected individuals have patchy dermal hypoplasia, often in a
distribution pattern following the Blaschko lines, and areas of
subcutaneous fat herniation or deposition of fat into the dermis.
In addition, sparse and brittle hair, hypoplastic nails and
papillomas have been described. Skeletal abnormalities usually
comprise syndactyly, ectrodactyly, and brachydactyly, and in some
cases osteopathia striata has been seen. Patients frequently have
ocular anomalies, including microphthalmia/ anophthalmia,
coloboma, pigmentary and vascularization defects of the retina.
Dental abnormalities are often present.
{ECO:0000269|PubMed:17546030, ECO:0000269|PubMed:17546031,
ECO:0000269|PubMed:18325042, ECO:0000269|PubMed:19277062,
ECO:0000269|PubMed:19309688, ECO:0000269|PubMed:19586929,
ECO:0000269|PubMed:19863546, ECO:0000269|PubMed:21472892}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
Porcupine subfamily. {ECO:0000305}.
-!- CAUTION: Was initially thought to mediate palmitoylation of Wnt
proteins (PubMed:24292069). It was later shown that it instead
acts as a serine O-palmitoleoyltransferase that mediates the
attachment of palmitoleate, a 16-carbon monounsaturated fatty acid
(C16:1), to Wnt proteins. {ECO:0000269|PubMed:24292069}.
-!- SEQUENCE CAUTION:
Sequence=AAA74510.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown upstream of position 63 for unknown reasons.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Leiden Open Variation Database; Note=Porcupine
homolog (Drosophila) (PORCN);
URL="http://grenada.lumc.nl/LOVD2/amc/home.php";
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EMBL; AF317058; AAG39628.1; -; mRNA.
EMBL; AF317059; AAG39629.1; -; mRNA.
EMBL; AF317060; AAG39630.1; -; mRNA.
EMBL; AF317061; AAG39631.1; -; mRNA.
EMBL; AK314745; BAG37285.1; -; mRNA.
EMBL; AK316378; BAH14749.1; -; mRNA.
EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471224; EAW50780.1; -; Genomic_DNA.
EMBL; BC019080; AAH19080.1; -; mRNA.
EMBL; L08239; AAA74510.1; ALT_SEQ; mRNA.
CCDS; CCDS14296.1; -. [Q9H237-4]
CCDS; CCDS14297.1; -. [Q9H237-2]
CCDS; CCDS14298.1; -. [Q9H237-3]
CCDS; CCDS14299.1; -. [Q9H237-1]
RefSeq; NP_001269096.1; NM_001282167.1. [Q9H237-5]
RefSeq; NP_073736.2; NM_022825.3. [Q9H237-4]
RefSeq; NP_982299.1; NM_203473.2. [Q9H237-2]
RefSeq; NP_982300.1; NM_203474.1. [Q9H237-3]
RefSeq; NP_982301.1; NM_203475.2. [Q9H237-1]
RefSeq; XP_006724609.1; XM_006724546.3. [Q9H237-1]
RefSeq; XP_011542250.1; XM_011543948.2. [Q9H237-5]
RefSeq; XP_016885225.1; XM_017029736.1. [Q9H237-5]
UniGene; Hs.386453; -.
ProteinModelPortal; Q9H237; -.
STRING; 9606.ENSP00000322304; -.
BindingDB; Q9H237; -.
ChEMBL; CHEMBL1255163; -.
iPTMnet; Q9H237; -.
PhosphoSitePlus; Q9H237; -.
BioMuta; PORCN; -.
DMDM; 116242723; -.
MaxQB; Q9H237; -.
PaxDb; Q9H237; -.
PeptideAtlas; Q9H237; -.
PRIDE; Q9H237; -.
DNASU; 64840; -.
Ensembl; ENST00000326194; ENSP00000322304; ENSG00000102312. [Q9H237-1]
Ensembl; ENST00000355961; ENSP00000348233; ENSG00000102312. [Q9H237-2]
Ensembl; ENST00000359882; ENSP00000352946; ENSG00000102312. [Q9H237-3]
Ensembl; ENST00000361988; ENSP00000354978; ENSG00000102312. [Q9H237-4]
Ensembl; ENST00000367574; ENSP00000356546; ENSG00000102312. [Q9H237-3]
Ensembl; ENST00000537758; ENSP00000446401; ENSG00000102312. [Q9H237-2]
GeneID; 64840; -.
KEGG; hsa:64840; -.
UCSC; uc004djr.3; human. [Q9H237-1]
CTD; 64840; -.
DisGeNET; 64840; -.
EuPathDB; HostDB:ENSG00000102312.20; -.
GeneCards; PORCN; -.
GeneReviews; PORCN; -.
HGNC; HGNC:17652; PORCN.
HPA; HPA049215; -.
HPA; HPA058413; -.
MalaCards; PORCN; -.
MIM; 300651; gene.
MIM; 305600; phenotype.
neXtProt; NX_Q9H237; -.
OpenTargets; ENSG00000102312; -.
Orphanet; 2092; Focal dermal hypoplasia.
PharmGKB; PA134906089; -.
eggNOG; KOG4312; Eukaryota.
eggNOG; ENOG410YDZ6; LUCA.
GeneTree; ENSGT00440000033687; -.
HOGENOM; HOG000231245; -.
HOVERGEN; HBG061243; -.
InParanoid; Q9H237; -.
KO; K00181; -.
OMA; LYHFFQL; -.
OrthoDB; EOG091G0DRB; -.
PhylomeDB; Q9H237; -.
TreeFam; TF313724; -.
Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
Reactome; R-HSA-5340573; WNT ligand secretion is abrogated by the PORCN inhibitor LGK974.
ChiTaRS; PORCN; human.
GenomeRNAi; 64840; -.
PRO; PR:Q9H237; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102312; -.
CleanEx; HS_PORCN; -.
ExpressionAtlas; Q9H237; baseline and differential.
Genevisible; Q9H237; HS.
GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:1990698; F:palmitoleoyltransferase activity; ISS:UniProtKB.
GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0009100; P:glycoprotein metabolic process; IEA:Ensembl.
GO; GO:0006497; P:protein lipidation; ISS:UniProtKB.
GO; GO:0045234; P:protein palmitoleylation; ISS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; ISS:UniProtKB.
InterPro; IPR004299; MBOAT_fam.
Pfam; PF03062; MBOAT; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Disease mutation; Endoplasmic reticulum; Lipoprotein; Membrane;
Palmitate; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Wnt signaling pathway.
CHAIN 1 461 Protein-serine O-palmitoleoyltransferase
porcupine.
/FTId=PRO_0000213137.
TOPO_DOM 1 17 Cytoplasmic. {ECO:0000255}.
TRANSMEM 18 38 Helical. {ECO:0000255}.
TOPO_DOM 39 66 Extracellular. {ECO:0000255}.
TRANSMEM 67 87 Helical. {ECO:0000255}.
TOPO_DOM 88 95 Cytoplasmic. {ECO:0000255}.
TRANSMEM 96 116 Helical. {ECO:0000255}.
TOPO_DOM 117 152 Extracellular. {ECO:0000255}.
TRANSMEM 153 173 Helical. {ECO:0000255}.
TOPO_DOM 174 198 Cytoplasmic. {ECO:0000255}.
TRANSMEM 199 219 Helical. {ECO:0000255}.
TOPO_DOM 220 252 Extracellular. {ECO:0000255}.
TRANSMEM 253 273 Helical. {ECO:0000255}.
TOPO_DOM 274 337 Cytoplasmic. {ECO:0000255}.
TRANSMEM 338 358 Helical. {ECO:0000255}.
TOPO_DOM 359 396 Extracellular. {ECO:0000255}.
TRANSMEM 397 417 Helical. {ECO:0000255}.
TOPO_DOM 418 461 Cytoplasmic. {ECO:0000255}.
ACT_SITE 341 341 {ECO:0000269|PubMed:24292069}.
LIPID 187 187 S-palmitoyl cysteine.
{ECO:0000269|PubMed:24292069}.
VAR_SEQ 1 71 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055419.
VAR_SEQ 229 240 NKKRKARGTMVR -> K (in isoform 4 and
isoform 5). {ECO:0000303|PubMed:12034504,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_015886.
VAR_SEQ 229 235 NKKRKAR -> K (in isoform 3).
{ECO:0000303|PubMed:12034504}.
/FTId=VSP_015887.
VAR_SEQ 235 239 Missing (in isoform 2).
{ECO:0000303|PubMed:12034504,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015888.
VARIANT 60 60 G -> R (in FODH; dbSNP:rs267606973).
{ECO:0000269|PubMed:17546030}.
/FTId=VAR_035089.
VARIANT 136 136 S -> F (in FODH).
{ECO:0000269|PubMed:19309688}.
/FTId=VAR_058899.
VARIANT 168 168 G -> R (in FODH).
{ECO:0000269|PubMed:19309688,
ECO:0000269|PubMed:19586929}.
/FTId=VAR_058900.
VARIANT 228 228 R -> C (in a patient with focal dermal
hypoplasia also carrying a frameshift
mutation; uncertain pathological
significance).
{ECO:0000269|PubMed:18325042}.
/FTId=VAR_058901.
VARIANT 252 252 H -> Y (in FODH).
{ECO:0000269|PubMed:21472892}.
/FTId=VAR_065189.
VARIANT 258 258 V -> E (in FODH).
{ECO:0000269|PubMed:19309688}.
/FTId=VAR_058902.
VARIANT 297 297 S -> L (in FODH).
{ECO:0000269|PubMed:19586929}.
/FTId=VAR_065190.
VARIANT 331 331 L -> R (in FODH).
{ECO:0000269|PubMed:19863546}.
/FTId=VAR_065191.
VARIANT 341 341 H -> L (in FODH).
{ECO:0000269|PubMed:19309688}.
/FTId=VAR_058903.
VARIANT 361 361 E -> V (in FODH).
{ECO:0000269|PubMed:19277062}.
/FTId=VAR_065192.
VARIANT 365 365 R -> G (in FODH).
{ECO:0000269|PubMed:17546030,
ECO:0000269|PubMed:19309688}.
/FTId=VAR_035090.
VARIANT 365 365 R -> Q (in FODH).
{ECO:0000269|PubMed:18325042,
ECO:0000269|PubMed:19309688,
ECO:0000269|PubMed:19586929,
ECO:0000269|PubMed:19863546,
ECO:0000269|PubMed:21472892}.
/FTId=VAR_058904.
VARIANT 374 374 A -> P (in FODH).
{ECO:0000269|PubMed:19586929}.
/FTId=VAR_066061.
VARIANT 385 385 C -> R (in FODH).
{ECO:0000269|PubMed:19309688}.
/FTId=VAR_058905.
VARIANT 385 385 C -> Y (in FODH).
{ECO:0000269|PubMed:19277062}.
/FTId=VAR_065193.
VARIANT 439 439 W -> R (in FODH).
{ECO:0000269|PubMed:19309688}.
/FTId=VAR_058906.
MUTAGEN 187 187 C->A: Drastic loss of palmitoylation.
{ECO:0000269|PubMed:24292069}.
MUTAGEN 341 341 H->A: Loss of function.
{ECO:0000269|PubMed:24292069}.
CONFLICT 42 42 L -> P (in Ref. 1; AAG39631).
{ECO:0000305}.
CONFLICT 179 179 A -> T (in Ref. 1; AAG39628/AAG39630).
{ECO:0000305}.
SEQUENCE 461 AA; 52318 MW; 000624825E507385 CRC64;
MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY LKHASTVAGG
FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS VTILIYLLMG EMHMVDTVTW
HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV
QGRPLSCRWL QKVARSLALA LLCLVLSTCV GPYLFPYFIP LNGDRLLRNK KRKARGTMVR
WLRAYESAVS FHFSNYFVGF LSEATATLAG AGFTEEKDHL EWDLTVSKPL NVELPRSMVE
VVTSWNLPMS YWLNNYVFKN ALRLGTFSAV LVTYAASALL HGFSFHLAAV LLSLAFITYV
EHVLRKRLAR ILSACVLSKR CPPDCSHQHR LGLGVRALNL LFGALAIFHL AYLGSLFDVD
VDDTTEEQGY GMAYTVHKWS ELSWASHWVT FGCWIFYRLI G


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