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Protein

Protein-serine O-palmitoleoyltransferase porcupine

Gene

PORCN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

Catalytic activityi

(9Z)-hexadecenoyl-CoA + [Wnt]-L-serine = CoA + [Wnt]-O-(9Z)-hexadecenoyl-L-serine.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei341 – 34111 Publication

GO - Molecular functioni

  1. transferase activity, transferring acyl groups Source: UniProtKB-KW

GO - Biological processi

  1. glycoprotein metabolic process Source: Ensembl
  2. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.
REACT_263933. WNT ligand secretion is abrogated by the PORCN inhibitor LGK974.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein-serine O-palmitoleoyltransferase porcupineBy similarity (EC:2.3.1.-By similarity)
Alternative name(s):
Protein MG611 Publication
Gene namesi
Name:PORCNImported
Synonyms:MG611 Publication, PORC, PPN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:17652. PORCN.

Subcellular locationi

  1. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1717CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei18 – 3821HelicalSequence AnalysisAdd
BLAST
Topological domaini39 – 6628ExtracellularSequence AnalysisAdd
BLAST
Transmembranei67 – 8721HelicalSequence AnalysisAdd
BLAST
Topological domaini88 – 958CytoplasmicSequence Analysis
Transmembranei96 – 11621HelicalSequence AnalysisAdd
BLAST
Topological domaini117 – 15236ExtracellularSequence AnalysisAdd
BLAST
Transmembranei153 – 17321HelicalSequence AnalysisAdd
BLAST
Topological domaini174 – 19825CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei199 – 21921HelicalSequence AnalysisAdd
BLAST
Topological domaini220 – 25233ExtracellularSequence AnalysisAdd
BLAST
Transmembranei253 – 27321HelicalSequence AnalysisAdd
BLAST
Topological domaini274 – 33764CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei338 – 35821HelicalSequence AnalysisAdd
BLAST
Topological domaini359 – 39638ExtracellularSequence AnalysisAdd
BLAST
Transmembranei397 – 41721HelicalSequence AnalysisAdd
BLAST
Topological domaini418 – 46144CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex Source: Ensembl
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of endoplasmic reticulum membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Focal dermal hypoplasia (FODH)8 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:305600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601G → R in FODH. 1 Publication
VAR_035089
Natural varianti136 – 1361S → F in FODH. 1 Publication
VAR_058899
Natural varianti168 – 1681G → R in FODH. 2 Publications
VAR_058900
Natural varianti252 – 2521H → Y in FODH. 1 Publication
VAR_065189
Natural varianti258 – 2581V → E in FODH. 1 Publication
VAR_058902
Natural varianti297 – 2971S → L in FODH. 1 Publication
VAR_065190
Natural varianti331 – 3311L → R in FODH. 1 Publication
VAR_065191
Natural varianti341 – 3411H → L in FODH. 1 Publication
VAR_058903
Natural varianti361 – 3611E → V in FODH. 1 Publication
VAR_065192
Natural varianti365 – 3651R → G in FODH. 2 Publications
VAR_035090
Natural varianti365 – 3651R → Q in FODH. 5 Publications
VAR_058904
Natural varianti374 – 3741A → P in FODH. 1 Publication
VAR_066061
Natural varianti385 – 3851C → R in FODH. 1 Publication
VAR_058905
Natural varianti385 – 3851C → Y in FODH. 1 Publication
VAR_065193
Natural varianti439 – 4391W → R in FODH. 1 Publication
VAR_058906

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871C → A: Drastic loss of palmitoylation. 1 Publication
Mutagenesisi341 – 3411H → A: Loss of function. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi305600. phenotype.
Orphaneti2092. Focal dermal hypoplasia.
PharmGKBiPA134906089.

Polymorphism and mutation databases

BioMutaiPORCN.
DMDMi116242723.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Protein-serine O-palmitoleoyltransferase porcupinePRO_0000213137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi187 – 1871S-palmitoyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Palmitate

Proteomic databases

MaxQBiQ9H237.
PaxDbiQ9H237.
PRIDEiQ9H237.

PTM databases

PhosphoSiteiQ9H237.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9H237.
CleanExiHS_PORCN.
ExpressionAtlasiQ9H237. baseline and differential.
GenevestigatoriQ9H237.

Organism-specific databases

HPAiHPA049215.

Interactioni

Subunit structurei

Interacts with WNT1, WNT3, WNT3A, WNT4, WNT5A, WNT5B, WNT6, WNT7A and WNT7B.By similarity

Protein-protein interaction databases

STRINGi9606.ENSP00000322304.

Structurei

3D structure databases

ProteinModelPortaliQ9H237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG325605.
GeneTreeiENSGT00440000033687.
HOGENOMiHOG000231245.
HOVERGENiHBG061243.
InParanoidiQ9H237.
KOiK00181.
OMAiLYHFFQL.
OrthoDBiEOG7XWPNC.
PhylomeDBiQ9H237.
TreeFamiTF313724.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H237-1) [UniParc]FASTAAdd to basket

Also known as: D

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATFSRQEFF QQLLQGCLLP TAQQGLDQIW LLLAICLACR LLWRLGLPSY
60 70 80 90 100
LKHASTVAGG FFSLYHFFQL HMVWVVLLSL LCYLVLFLCR HSSHRGVFLS
110 120 130 140 150
VTILIYLLMG EMHMVDTVTW HKMRGAQMIV AMKAVSLGFD LDRGEVGTVP
160 170 180 190 200
SPVEFMGYLY FVGTIVFGPW ISFHSYLQAV QGRPLSCRWL QKVARSLALA
210 220 230 240 250
LLCLVLSTCV GPYLFPYFIP LNGDRLLRNK KRKARGTMVR WLRAYESAVS
260 270 280 290 300
FHFSNYFVGF LSEATATLAG AGFTEEKDHL EWDLTVSKPL NVELPRSMVE
310 320 330 340 350
VVTSWNLPMS YWLNNYVFKN ALRLGTFSAV LVTYAASALL HGFSFHLAAV
360 370 380 390 400
LLSLAFITYV EHVLRKRLAR ILSACVLSKR CPPDCSHQHR LGLGVRALNL
410 420 430 440 450
LFGALAIFHL AYLGSLFDVD VDDTTEEQGY GMAYTVHKWS ELSWASHWVT
460
FGCWIFYRLI G
Length:461
Mass (Da):52,318
Last modified:October 17, 2006 - v2
Checksum:i000624825E507385
GO
Isoform 2 (identifier: Q9H237-2) [UniParc]FASTAAdd to basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     235-239: Missing.

Show »
Length:456
Mass (Da):51,773
Checksum:iBF22FF1836BC9397
GO
Isoform 3 (identifier: Q9H237-3) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     229-235: NKKRKAR → K

Show »
Length:455
Mass (Da):51,564
Checksum:i21532BA9B4D19F4A
GO
Isoform 4 (identifier: Q9H237-4) [UniParc]FASTAAdd to basket

Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     229-240: NKKRKARGTMVR → K

Show »
Length:450
Mass (Da):51,019
Checksum:i7ECE3021794835EB
GO
Isoform 5 (identifier: Q9H237-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.
     229-240: NKKRKARGTMVR → K

Note: No experimental confirmation available.

Show »
Length:379
Mass (Da):42,878
Checksum:i562081CACFEDA645
GO

Sequence cautioni

The sequence AAA74510.1 differs from that shown.The sequence differs from that shown upstream of position 63 for unknown reasons.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421L → P in AAG39631 (PubMed:12034504).Curated
Sequence conflicti179 – 1791A → T in AAG39628 (PubMed:12034504).Curated
Sequence conflicti179 – 1791A → T in AAG39630 (PubMed:12034504).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601G → R in FODH. 1 Publication
VAR_035089
Natural varianti136 – 1361S → F in FODH. 1 Publication
VAR_058899
Natural varianti168 – 1681G → R in FODH. 2 Publications
VAR_058900
Natural varianti228 – 2281R → C in a patient with focal dermal hypoplasia also carrying a frameshift mutation; uncertain pathological significance. 1 Publication
VAR_058901
Natural varianti252 – 2521H → Y in FODH. 1 Publication
VAR_065189
Natural varianti258 – 2581V → E in FODH. 1 Publication
VAR_058902
Natural varianti297 – 2971S → L in FODH. 1 Publication
VAR_065190
Natural varianti331 – 3311L → R in FODH. 1 Publication
VAR_065191
Natural varianti341 – 3411H → L in FODH. 1 Publication
VAR_058903
Natural varianti361 – 3611E → V in FODH. 1 Publication
VAR_065192
Natural varianti365 – 3651R → G in FODH. 2 Publications
VAR_035090
Natural varianti365 – 3651R → Q in FODH. 5 Publications
VAR_058904
Natural varianti374 – 3741A → P in FODH. 1 Publication
VAR_066061
Natural varianti385 – 3851C → R in FODH. 1 Publication
VAR_058905
Natural varianti385 – 3851C → Y in FODH. 1 Publication
VAR_065193
Natural varianti439 – 4391W → R in FODH. 1 Publication
VAR_058906

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171Missing in isoform 5. 1 PublicationVSP_055419Add
BLAST
Alternative sequencei229 – 24012NKKRK…GTMVR → K in isoform 4 and isoform 5. 2 PublicationsVSP_015886Add
BLAST
Alternative sequencei229 – 2357NKKRKAR → K in isoform 3. 1 PublicationVSP_015887
Alternative sequencei235 – 2395Missing in isoform 2. 2 PublicationsVSP_015888

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF317058 mRNA. Translation: AAG39628.1.
AF317059 mRNA. Translation: AAG39629.1.
AF317060 mRNA. Translation: AAG39630.1.
AF317061 mRNA. Translation: AAG39631.1.
AK314745 mRNA. Translation: BAG37285.1.
AK316378 mRNA. Translation: BAH14749.1.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50780.1.
BC019080 mRNA. Translation: AAH19080.1.
L08239 mRNA. Translation: AAA74510.1. Sequence problems.
CCDSiCCDS14296.1. [Q9H237-4]
CCDS14297.1. [Q9H237-2]
CCDS14298.1. [Q9H237-3]
CCDS14299.1. [Q9H237-1]
RefSeqiNP_001269096.1. NM_001282167.1. [Q9H237-5]
NP_073736.2. NM_022825.3. [Q9H237-4]
NP_982299.1. NM_203473.2. [Q9H237-2]
NP_982300.1. NM_203474.1. [Q9H237-3]
NP_982301.1. NM_203475.2. [Q9H237-1]
XP_006724609.1. XM_006724546.2. [Q9H237-1]
UniGeneiHs.386453.

Genome annotation databases

EnsembliENST00000326194; ENSP00000322304; ENSG00000102312. [Q9H237-1]
ENST00000355961; ENSP00000348233; ENSG00000102312. [Q9H237-2]
ENST00000359882; ENSP00000352946; ENSG00000102312. [Q9H237-3]
ENST00000361988; ENSP00000354978; ENSG00000102312. [Q9H237-4]
ENST00000367574; ENSP00000356546; ENSG00000102312. [Q9H237-3]
ENST00000537758; ENSP00000446401; ENSG00000102312. [Q9H237-2]
GeneIDi64840.
KEGGihsa:64840.
UCSCiuc004djr.1. human. [Q9H237-2]
uc004djs.1. human. [Q9H237-4]
uc004djv.1. human. [Q9H237-1]
uc004djw.1. human. [Q9H237-3]

Polymorphism and mutation databases

BioMutaiPORCN.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Leiden Open Variation Database

Porcupine homolog (Drosophila) (PORCN)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF317058 mRNA. Translation: AAG39628.1.
AF317059 mRNA. Translation: AAG39629.1.
AF317060 mRNA. Translation: AAG39630.1.
AF317061 mRNA. Translation: AAG39631.1.
AK314745 mRNA. Translation: BAG37285.1.
AK316378 mRNA. Translation: BAH14749.1.
AF196972 Genomic DNA. No translation available.
CH471224 Genomic DNA. Translation: EAW50780.1.
BC019080 mRNA. Translation: AAH19080.1.
L08239 mRNA. Translation: AAA74510.1. Sequence problems.
CCDSiCCDS14296.1. [Q9H237-4]
CCDS14297.1. [Q9H237-2]
CCDS14298.1. [Q9H237-3]
CCDS14299.1. [Q9H237-1]
RefSeqiNP_001269096.1. NM_001282167.1. [Q9H237-5]
NP_073736.2. NM_022825.3. [Q9H237-4]
NP_982299.1. NM_203473.2. [Q9H237-2]
NP_982300.1. NM_203474.1. [Q9H237-3]
NP_982301.1. NM_203475.2. [Q9H237-1]
XP_006724609.1. XM_006724546.2. [Q9H237-1]
UniGeneiHs.386453.

3D structure databases

ProteinModelPortaliQ9H237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000322304.

Chemistry

ChEMBLiCHEMBL1255163.

PTM databases

PhosphoSiteiQ9H237.

Polymorphism and mutation databases

BioMutaiPORCN.
DMDMi116242723.

Proteomic databases

MaxQBiQ9H237.
PaxDbiQ9H237.
PRIDEiQ9H237.

Protocols and materials databases

DNASUi64840.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326194; ENSP00000322304; ENSG00000102312. [Q9H237-1]
ENST00000355961; ENSP00000348233; ENSG00000102312. [Q9H237-2]
ENST00000359882; ENSP00000352946; ENSG00000102312. [Q9H237-3]
ENST00000361988; ENSP00000354978; ENSG00000102312. [Q9H237-4]
ENST00000367574; ENSP00000356546; ENSG00000102312. [Q9H237-3]
ENST00000537758; ENSP00000446401; ENSG00000102312. [Q9H237-2]
GeneIDi64840.
KEGGihsa:64840.
UCSCiuc004djr.1. human. [Q9H237-2]
uc004djs.1. human. [Q9H237-4]
uc004djv.1. human. [Q9H237-1]
uc004djw.1. human. [Q9H237-3]

Organism-specific databases

CTDi64840.
GeneCardsiGC0XP048367.
GeneReviewsiPORCN.
HGNCiHGNC:17652. PORCN.
HPAiHPA049215.
MIMi300651. gene.
305600. phenotype.
neXtProtiNX_Q9H237.
Orphaneti2092. Focal dermal hypoplasia.
PharmGKBiPA134906089.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG325605.
GeneTreeiENSGT00440000033687.
HOGENOMiHOG000231245.
HOVERGENiHBG061243.
InParanoidiQ9H237.
KOiK00181.
OMAiLYHFFQL.
OrthoDBiEOG7XWPNC.
PhylomeDBiQ9H237.
TreeFamiTF313724.

Enzyme and pathway databases

ReactomeiREACT_163710. WNT ligand biogenesis and trafficking.
REACT_263933. WNT ligand secretion is abrogated by the PORCN inhibitor LGK974.

Miscellaneous databases

ChiTaRSiPORCN. human.
GenomeRNAii64840.
NextBioi66934.
PROiQ9H237.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H237.
CleanExiHS_PORCN.
ExpressionAtlasiQ9H237. baseline and differential.
GenevestigatoriQ9H237.

Family and domain databases

InterProiIPR004299. MBOAT_fam.
[Graphical view]
PfamiPF03062. MBOAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and initial characterization of the MG61/PORC gene, the human homologue of the Drosophila segment polarity gene Porcupine."
    Caricasole A., Ferraro T., Rimland J.M., Terstappen G.C.
    Gene 288:147-157(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION IN WNT PROTEINS PROCESSING, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Hippocampus.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
  3. "The DNA sequence of the human X chromosome."
    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.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  6. Geraghty M.T.
    Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-461 (ISOFORM 1).
    Tissue: Retina.
  7. Cited for: INVOLVEMENT IN FODH.
  8. Cited for: FUNCTION.
  9. "Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine."
    Gao X., Hannoush R.N.
    Nat. Chem. Biol. 10:61-68(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PALMITOYLATION AT CYS-187, ACTIVE SITE, MUTAGENESIS OF CYS-187 AND HIS-341.
  10. "Mutations in X-linked PORCN, a putative regulator of Wnt signaling, cause focal dermal hypoplasia."
    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.
    Nat. Genet. 39:836-838(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FODH ARG-60 AND GLY-365.
  11. "Three novel mutations in the PORCN gene underlying focal dermal hypoplasia."
    Leoyklang P., Suphapeetiporn K., Wananukul S., Shotelersuk V.
    Clin. Genet. 73:373-379(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT FODH GLN-365, VARIANT CYS-228.
  12. Cited for: VARIANTS FODH ARG-331 AND GLN-365.
  13. "Goltz-Gorlin (focal dermal hypoplasia) and the microphthalmia with linear skin defects (MLS) syndrome: no evidence of genetic overlap."
    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.
    Eur. J. Hum. Genet. 17:1207-1215(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FODH VAL-361 AND TYR-385.
  14. Cited for: VARIANTS FODH PHE-136; ARG-168; GLU-258; LEU-341; GLN-365; GLY-365; ARG-385 AND ARG-439.
  15. Cited for: VARIANTS FODH ARG-168; LEU-297; GLN-365 AND PRO-374.
  16. Cited for: VARIANTS FODH TYR-252 AND GLN-365.

Entry informationi

Entry nameiPORCN_HUMAN
AccessioniPrimary (citable) accession number: Q9H237
Secondary accession number(s): B2RBN8
, B7ZAR3, Q14829, Q9H234, Q9H235, Q9H236, Q9UJU7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 17, 2006
Last modified: April 29, 2015
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.