PORCN_HUMAN
ID PORCN_HUMAN Reviewed; 461 AA.
AC Q9H237; B2RBN8; B7ZAR3; Q14829; Q9H234; Q9H235; Q9H236; Q9UJU7;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
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=Protein MG61 {ECO:0000303|PubMed:12034504};
GN Name=PORCN {ECO:0000312|HGNC:HGNC:17652};
GN Synonyms=MG61 {ECO:0000303|PubMed:12034504}, PORC, PPN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION IN WNT
RP PROTEINS PROCESSING, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=12034504; DOI=10.1016/s0378-1119(02)00467-5;
RA Caricasole A., Ferraro T., Rimland J.M., Terstappen G.C.;
RT "Molecular cloning and initial characterization of the MG61/PORC gene, the
RT human homologue of the Drosophila segment polarity gene Porcupine.";
RL Gene 288:147-157(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 63-461 (ISOFORM 1).
RC TISSUE=Retina;
RA Geraghty M.T.;
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INVOLVEMENT IN FODH.
RX PubMed=17546031; DOI=10.1038/ng2052;
RA Grzeschik K.-H., Bornholdt D., Oeffner F., Koenig A., del Carmen Boente M.,
RA Enders H., Fritz B., Hertl M., Grasshoff U., Hoefling K., Oji V.,
RA Paradisi M., Schuchardt C., Szalai Z., Tadini G., Traupe H., Happle R.;
RT "Deficiency of PORCN, a regulator of Wnt signaling, is associated with
RT focal dermal hypoplasia.";
RL Nat. Genet. 39:833-835(2007).
RN [8]
RP FUNCTION.
RX PubMed=20826466; DOI=10.1242/jcs.072132;
RA Coombs G.S., Yu J., Canning C.A., Veltri C.A., Covey T.M., Cheong J.K.,
RA Utomo V., Banerjee N., Zhang Z.H., Jadulco R.C., Concepcion G.P.,
RA Bugni T.S., Harper M.K., Mihalek I., Jones C.M., Ireland C.M.,
RA Virshup D.M.;
RT "WLS-dependent secretion of WNT3A requires Ser209 acylation and vacuolar
RT acidification.";
RL J. Cell Sci. 123:3357-3367(2010).
RN [9]
RP FUNCTION, PALMITOYLATION AT CYS-187, ACTIVE SITE, AND MUTAGENESIS OF
RP CYS-187 AND HIS-341.
RX PubMed=24292069; DOI=10.1038/nchembio.1392;
RA Gao X., Hannoush R.N.;
RT "Single-cell imaging of Wnt palmitoylation by the acyltransferase
RT porcupine.";
RL Nat. Chem. Biol. 10:61-68(2014).
RN [10]
RP VARIANTS FODH ARG-60 AND GLY-365.
RX PubMed=17546030; DOI=10.1038/ng2057;
RA Wang X., Reid Sutton V., Omar Peraza-Llanes J., Yu Z., Rosetta R.,
RA Kou Y.-C., Eble T.N., Patel A., Thaller C., Fang P., Van den Veyver I.B.;
RT "Mutations in X-linked PORCN, a putative regulator of Wnt signaling, cause
RT focal dermal hypoplasia.";
RL Nat. Genet. 39:836-838(2007).
RN [11]
RP VARIANT FODH GLN-365, AND VARIANT CYS-228.
RX PubMed=18325042; DOI=10.1111/j.1399-0004.2008.00975.x;
RA Leoyklang P., Suphapeetiporn K., Wananukul S., Shotelersuk V.;
RT "Three novel mutations in the PORCN gene underlying focal dermal
RT hypoplasia.";
RL Clin. Genet. 73:373-379(2008).
RN [12]
RP VARIANTS FODH ARG-331 AND GLN-365.
RX PubMed=19863546; DOI=10.1111/j.1399-0004.2009.01248.x;
RA Froyen G., Govaerts K., Van Esch H., Verbeeck J., Tuomi M.L., Heikkila H.,
RA Torniainen S., Devriendt K., Fryns J.P., Marynen P., Jarvela I.,
RA Ala-Mello S.;
RT "Novel PORCN mutations in focal dermal hypoplasia.";
RL Clin. Genet. 76:535-543(2009).
RN [13]
RP VARIANTS FODH VAL-361 AND TYR-385.
RX PubMed=19277062; DOI=10.1038/ejhg.2009.40;
RA Harmsen M.B., Azzarello-Burri S., Garcia Gonzalez M.M.,
RA Gillessen-Kaesbach G., Meinecke P., Muller D., Rauch A., Rossier E.,
RA Seemanova E., Spaich C., Steiner B., Wieczorek D., Zenker M., Kutsche K.;
RT "Goltz-Gorlin (focal dermal hypoplasia) and the microphthalmia with linear
RT skin defects (MLS) syndrome: no evidence of genetic overlap.";
RL Eur. J. Hum. Genet. 17:1207-1215(2009).
RN [14]
RP VARIANTS FODH PHE-136; ARG-168; GLU-258; LEU-341; GLN-365; GLY-365; ARG-385
RP AND ARG-439.
RX PubMed=19309688; DOI=10.1002/humu.20992;
RA Bornholdt D., Oeffner F., Koenig A., Happle R., Alanay Y., Ascherman J.,
RA Benke P.J., Boente M.C., van der Burgt I., Chassaing N., Ellis I.,
RA Francisco C.R.I., Della Giovanna P., Hamel B., Has C., Heinelt K.,
RA Janecke A., Kastrup W., Loeys B., Lohrisch I., Marcelis C., Mehraein Y.,
RA Nicolas M.E.O., Pagliarini D., Paradisi M., Patrizi A., Piccione M.,
RA Piza-Katzer H., Prager B., Prescott K., Strien J., Utine G.E., Zeller M.S.,
RA Grzeschik K.-H.;
RT "PORCN mutations in focal dermal hypoplasia: coping with lethality.";
RL Hum. Mutat. 30:E618-E628(2009).
RN [15]
RP VARIANTS FODH ARG-168; LEU-297; GLN-365 AND PRO-374.
RX PubMed=19586929; DOI=10.1136/jmg.2009.068403;
RA Maas S.M., Lombardi M.P., van Essen A.J., Wakeling E.L., Castle B.,
RA Temple I.K., Kumar V.K., Writzl K., Hennekam R.C.;
RT "Phenotype and genotype in 17 patients with Goltz-Gorlin syndrome.";
RL J. Med. Genet. 46:716-720(2009).
RN [16]
RP VARIANTS FODH TYR-252 AND GLN-365.
RX PubMed=21472892; DOI=10.1002/humu.21505;
RA Lombardi M.P., Bulk S., Celli J., Lampe A., Gabbett M.T., Ousager L.B.,
RA van der Smagt J.J., Soller M., Stattin E.L., Mannens M.A., Smigiel R.,
RA Hennekam R.C.;
RT "Mutation update for the PORCN gene.";
RL Hum. Mutat. 32:723-728(2011).
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. {ECO:0000250|UniProtKB:Q9JJJ7,
CC ECO:0000269|PubMed:12034504, ECO:0000269|PubMed:20826466,
CC ECO:0000269|PubMed:24292069}.
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 WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B, WNT6,
CC WNT7A and WNT7B. {ECO:0000250|UniProtKB:Q9JJJ7}.
CC -!- INTERACTION:
CC Q9H237-2; P55056: APOC4; NbExp=3; IntAct=EBI-18254170, EBI-18302142;
CC Q9H237-2; Q8N350-4: CBARP; NbExp=3; IntAct=EBI-18254170, EBI-19051169;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9JJJ7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9JJJ7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=D;
CC IsoId=Q9H237-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q9H237-2; Sequence=VSP_015888;
CC Name=3; Synonyms=C;
CC IsoId=Q9H237-3; Sequence=VSP_015887;
CC Name=4; Synonyms=A;
CC IsoId=Q9H237-4; Sequence=VSP_015886;
CC Name=5;
CC IsoId=Q9H237-5; Sequence=VSP_055419, VSP_015886;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in fetal brain, brain,
CC amygdala, caudate nucleus, cerebellum, hippocampus, pituitary,
CC thalamus, heart, skeletal muscle and testis. Isoform 4 is expressed in
CC amygdala, corpus callosum, hippocampus, spinal cord, kidney, liver,
CC lung, spleen, uterus, testis. Isoform 2 and isoform 3 are expressed in
CC substantia negra, spinal cord, heart and lung.
CC {ECO:0000269|PubMed:12034504}.
CC -!- DISEASE: Focal dermal hypoplasia (FODH) [MIM:305600]: A rare congenital
CC ectomesodermal disorder characterized by a combination of skin defects,
CC skeletal abnormalities, and ocular anomalies. Affected individuals have
CC patchy dermal hypoplasia, often in a distribution pattern following the
CC Blaschko lines, and areas of subcutaneous fat herniation or deposition
CC of fat into the dermis. In addition, sparse and brittle hair,
CC hypoplastic nails and papillomas have been described. Skeletal
CC abnormalities usually comprise syndactyly, ectrodactyly, and
CC brachydactyly, and in some cases osteopathia striata has been seen.
CC Patients frequently have ocular anomalies, including microphthalmia/
CC anophthalmia, coloboma, pigmentary and vascularization defects of the
CC retina. Dental abnormalities are often present.
CC {ECO:0000269|PubMed:17546030, ECO:0000269|PubMed:17546031,
CC ECO:0000269|PubMed:18325042, ECO:0000269|PubMed:19277062,
CC ECO:0000269|PubMed:19309688, ECO:0000269|PubMed:19586929,
CC ECO:0000269|PubMed:19863546, ECO:0000269|PubMed:21472892}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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 (PubMed:24292069). It was later shown that it instead acts as
CC a serine O-palmitoleoyltransferase that mediates the attachment of
CC palmitoleate, a 16-carbon monounsaturated fatty acid (C16:1), to Wnt
CC proteins. {ECO:0000269|PubMed:24292069}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74510.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown upstream of position 63 for unknown reasons.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Leiden Open Variation Database; Note=Porcupine
CC homolog (Drosophila) (PORCN);
CC URL="https://databases.lovd.nl/shared/genes/PORCN";
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DR EMBL; AF317058; AAG39628.1; -; mRNA.
DR EMBL; AF317059; AAG39629.1; -; mRNA.
DR EMBL; AF317060; AAG39630.1; -; mRNA.
DR EMBL; AF317061; AAG39631.1; -; mRNA.
DR EMBL; AK314745; BAG37285.1; -; mRNA.
DR EMBL; AK316378; BAH14749.1; -; mRNA.
DR EMBL; AF196972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50780.1; -; Genomic_DNA.
DR EMBL; BC019080; AAH19080.1; -; mRNA.
DR EMBL; L08239; AAA74510.1; ALT_SEQ; mRNA.
DR CCDS; CCDS14296.1; -. [Q9H237-4]
DR CCDS; CCDS14297.1; -. [Q9H237-2]
DR CCDS; CCDS14298.1; -. [Q9H237-3]
DR CCDS; CCDS14299.1; -. [Q9H237-1]
DR RefSeq; NP_001269096.1; NM_001282167.1. [Q9H237-5]
DR RefSeq; NP_073736.2; NM_022825.3. [Q9H237-4]
DR RefSeq; NP_982299.1; NM_203473.2. [Q9H237-2]
DR RefSeq; NP_982300.1; NM_203474.1. [Q9H237-3]
DR RefSeq; NP_982301.1; NM_203475.2. [Q9H237-1]
DR RefSeq; XP_006724609.1; XM_006724546.3.
DR RefSeq; XP_011542250.1; XM_011543948.2.
DR RefSeq; XP_016885225.1; XM_017029736.1.
DR AlphaFoldDB; Q9H237; -.
DR BioGRID; 122316; 7.
DR IntAct; Q9H237; 2.
DR STRING; 9606.ENSP00000322304; -.
DR BindingDB; Q9H237; -.
DR ChEMBL; CHEMBL1255163; -.
DR GuidetoPHARMACOLOGY; 3145; -.
DR TCDB; 2.A.50.3.1; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR iPTMnet; Q9H237; -.
DR PhosphoSitePlus; Q9H237; -.
DR BioMuta; PORCN; -.
DR DMDM; 116242723; -.
DR EPD; Q9H237; -.
DR jPOST; Q9H237; -.
DR MassIVE; Q9H237; -.
DR MaxQB; Q9H237; -.
DR PaxDb; Q9H237; -.
DR PeptideAtlas; Q9H237; -.
DR PRIDE; Q9H237; -.
DR ProteomicsDB; 7081; -.
DR ProteomicsDB; 80481; -. [Q9H237-1]
DR ProteomicsDB; 80482; -. [Q9H237-2]
DR ProteomicsDB; 80483; -. [Q9H237-3]
DR ProteomicsDB; 80484; -. [Q9H237-4]
DR Antibodypedia; 25667; 111 antibodies from 21 providers.
DR DNASU; 64840; -.
DR Ensembl; ENST00000326194.11; ENSP00000322304.6; ENSG00000102312.24. [Q9H237-1]
DR Ensembl; ENST00000355961.8; ENSP00000348233.4; ENSG00000102312.24. [Q9H237-2]
DR Ensembl; ENST00000359882.8; ENSP00000352946.4; ENSG00000102312.24. [Q9H237-3]
DR Ensembl; ENST00000361988.7; ENSP00000354978.3; ENSG00000102312.24. [Q9H237-4]
DR Ensembl; ENST00000367574.9; ENSP00000356546.6; ENSG00000102312.24. [Q9H237-4]
DR Ensembl; ENST00000537758.6; ENSP00000446401.3; ENSG00000102312.24. [Q9H237-4]
DR Ensembl; ENST00000683923.1; ENSP00000506737.1; ENSG00000102312.24. [Q9H237-4]
DR GeneID; 64840; -.
DR KEGG; hsa:64840; -.
DR MANE-Select; ENST00000326194.11; ENSP00000322304.6; NM_203475.3; NP_982301.1.
DR UCSC; uc004djr.3; human. [Q9H237-1]
DR CTD; 64840; -.
DR DisGeNET; 64840; -.
DR GeneCards; PORCN; -.
DR GeneReviews; PORCN; -.
DR HGNC; HGNC:17652; PORCN.
DR HPA; ENSG00000102312; Tissue enhanced (adrenal).
DR MalaCards; PORCN; -.
DR MIM; 300651; gene.
DR MIM; 305600; phenotype.
DR neXtProt; NX_Q9H237; -.
DR OpenTargets; ENSG00000102312; -.
DR Orphanet; 98938; Colobomatous microphthalmia.
DR Orphanet; 2092; Focal dermal hypoplasia.
DR PharmGKB; PA134906089; -.
DR VEuPathDB; HostDB:ENSG00000102312; -.
DR eggNOG; KOG4312; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR InParanoid; Q9H237; -.
DR OMA; YIYSPAT; -.
DR OrthoDB; 975725at2759; -.
DR PhylomeDB; Q9H237; -.
DR TreeFam; TF313724; -.
DR BRENDA; 2.3.1.250; 2681.
DR PathwayCommons; Q9H237; -.
DR Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
DR Reactome; R-HSA-5340573; LGK974 inhibits PORCN.
DR SignaLink; Q9H237; -.
DR SIGNOR; Q9H237; -.
DR BioGRID-ORCS; 64840; 19 hits in 705 CRISPR screens.
DR ChiTaRS; PORCN; human.
DR GenomeRNAi; 64840; -.
DR Pharos; Q9H237; Tchem.
DR PRO; PR:Q9H237; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9H237; protein.
DR Bgee; ENSG00000102312; Expressed in lower esophagus mucosa and 109 other tissues.
DR ExpressionAtlas; Q9H237; baseline and differential.
DR Genevisible; Q9H237; HS.
DR GO; GO:0032281; C:AMPA glutamate receptor complex; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:Ensembl.
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:0009100; P:glycoprotein metabolic process; IEA:Ensembl.
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:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; IEA:Ensembl.
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 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Disease variant;
KW Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Wnt signaling pathway.
FT CHAIN 1..461
FT /note="Protein-serine O-palmitoleoyltransferase porcupine"
FT /id="PRO_0000213137"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..66
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..252
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..396
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 341
FT /evidence="ECO:0000269|PubMed:24292069"
FT LIPID 187
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:24292069"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055419"
FT VAR_SEQ 229..240
FT /note="NKKRKARGTMVR -> K (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:12034504,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_015886"
FT VAR_SEQ 229..235
FT /note="NKKRKAR -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12034504"
FT /id="VSP_015887"
FT VAR_SEQ 235..239
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12034504,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015888"
FT VARIANT 60
FT /note="G -> R (in FODH; dbSNP:rs267606973)"
FT /evidence="ECO:0000269|PubMed:17546030"
FT /id="VAR_035089"
FT VARIANT 136
FT /note="S -> F (in FODH)"
FT /evidence="ECO:0000269|PubMed:19309688"
FT /id="VAR_058899"
FT VARIANT 168
FT /note="G -> R (in FODH; dbSNP:rs1602072227)"
FT /evidence="ECO:0000269|PubMed:19309688,
FT ECO:0000269|PubMed:19586929"
FT /id="VAR_058900"
FT VARIANT 228
FT /note="R -> C (in a patient with focal dermal hypoplasia
FT also carrying a frameshift mutation; uncertain pathological
FT significance; dbSNP:rs1556974235)"
FT /evidence="ECO:0000269|PubMed:18325042"
FT /id="VAR_058901"
FT VARIANT 252
FT /note="H -> Y (in FODH)"
FT /evidence="ECO:0000269|PubMed:21472892"
FT /id="VAR_065189"
FT VARIANT 258
FT /note="V -> E (in FODH)"
FT /evidence="ECO:0000269|PubMed:19309688"
FT /id="VAR_058902"
FT VARIANT 297
FT /note="S -> L (in FODH)"
FT /evidence="ECO:0000269|PubMed:19586929"
FT /id="VAR_065190"
FT VARIANT 331
FT /note="L -> R (in FODH)"
FT /evidence="ECO:0000269|PubMed:19863546"
FT /id="VAR_065191"
FT VARIANT 341
FT /note="H -> L (in FODH)"
FT /evidence="ECO:0000269|PubMed:19309688"
FT /id="VAR_058903"
FT VARIANT 361
FT /note="E -> V (in FODH)"
FT /evidence="ECO:0000269|PubMed:19277062"
FT /id="VAR_065192"
FT VARIANT 365
FT /note="R -> G (in FODH)"
FT /evidence="ECO:0000269|PubMed:17546030,
FT ECO:0000269|PubMed:19309688"
FT /id="VAR_035090"
FT VARIANT 365
FT /note="R -> Q (in FODH)"
FT /evidence="ECO:0000269|PubMed:18325042,
FT ECO:0000269|PubMed:19309688, ECO:0000269|PubMed:19586929,
FT ECO:0000269|PubMed:19863546, ECO:0000269|PubMed:21472892"
FT /id="VAR_058904"
FT VARIANT 374
FT /note="A -> P (in FODH)"
FT /evidence="ECO:0000269|PubMed:19586929"
FT /id="VAR_066061"
FT VARIANT 385
FT /note="C -> R (in FODH)"
FT /evidence="ECO:0000269|PubMed:19309688"
FT /id="VAR_058905"
FT VARIANT 385
FT /note="C -> Y (in FODH)"
FT /evidence="ECO:0000269|PubMed:19277062"
FT /id="VAR_065193"
FT VARIANT 439
FT /note="W -> R (in FODH)"
FT /evidence="ECO:0000269|PubMed:19309688"
FT /id="VAR_058906"
FT MUTAGEN 187
FT /note="C->A: Drastic loss of palmitoylation."
FT /evidence="ECO:0000269|PubMed:24292069"
FT MUTAGEN 341
FT /note="H->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:24292069"
FT CONFLICT 42
FT /note="L -> P (in Ref. 1; AAG39631)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> T (in Ref. 1; AAG39628/AAG39630)"
FT /evidence="ECO:0000305"
SQ 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
