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Phosphatidylinositol N-acetylglucosaminyltransferase subunit P (EC 2.4.1.198) (Down syndrome critical region protein 5) (Down syndrome critical region protein C) (Phosphatidylinositol-glycan biosynthesis class P protein) (PIG-P)

 PIGP_HUMAN              Reviewed;         158 AA.
P57054; A0A0C4DH71; B2RB18; B2RE99; B5BU92; D3DSG7; J3KR75; Q53Y28;
Q96KI1; Q9NZA6;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 4.
10-OCT-2018, entry version 147.
RecName: Full=Phosphatidylinositol N-acetylglucosaminyltransferase subunit P;
EC=2.4.1.198;
AltName: Full=Down syndrome critical region protein 5;
AltName: Full=Down syndrome critical region protein C;
AltName: Full=Phosphatidylinositol-glycan biosynthesis class P protein;
Short=PIG-P;
Name=PIGP; Synonyms=DCRC, DSCR5, DSCRC; ORFNames=NPD010;
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 A; B AND C).
TISSUE=Testis;
PubMed=10814524; DOI=10.1006/bbrc.2000.2685;
Shibuya K., Kudoh J., Minoshima S., Kawasaki K., Asakawa S.,
Shimizu N.;
"Isolation of two novel genes, DSCR5 and DSCR6, from Down syndrome
critical region on human chromosome 21q22.2.";
Biochem. Biophys. Res. Commun. 271:693-698(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
PubMed=10907851; DOI=10.1093/dnares/7.3.207;
Togashi T., Choi D.-K., Taylor T.D., Suzuki Y., Sugano S., Hattori M.,
Sakaki Y.;
"A novel gene, DSCR5, from the distal Down syndrome critical region on
chromosome 21q22.2.";
DNA Res. 7:207-212(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 26-33, AND FUNCTION
(ISOFORM A).
PubMed=10944123; DOI=10.1093/emboj/19.16.4402;
Watanabe R., Murakami Y., Marmor M.D., Inoue N., Maeda Y., Hino J.,
Kangawa K., Julius M., Kinoshita T.;
"Initial enzyme for glycosylphosphatidylinositol biosynthesis requires
PIG-P and is regulated by DPM2.";
EMBO J. 19:4402-4411(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Pituitary;
Song H., Gao G., Peng Y., Ren S., Chen Z., Han Z.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
TISSUE=Kidney, and Umbilical cord blood;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[9]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Brain;
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).
[11]
INVOLVEMENT IN EIEE55, VARIANT EIEE55 THR-25, CHARACTERIZATION OF
VARIANT EIEE55 THR-25, AND FUNCTION.
PubMed=28334793; DOI=10.1093/hmg/ddx077;
Care4Rare Canada Consortium;
Johnstone D.L., Nguyen T.T., Murakami Y., Kernohan K.D., Tetreault M.,
Goldsmith C., Doja A., Wagner J.D., Huang L., Hartley T., St-Denis A.,
le Deist F., Majewski J., Bulman D.E., Kinoshita T., Dyment D.A.,
Boycott K.M., Campeau P.M.;
"Compound heterozygous mutations in the gene PIGP are associated with
early infantile epileptic encephalopathy.";
Hum. Mol. Genet. 26:1706-1715(2017).
-!- FUNCTION: Part of the complex catalyzing the transfer of N-
acetylglucosamine from UDP-N-acetylglucosamine to
phosphatidylinositol, the first step of GPI biosynthesis.
{ECO:0000269|PubMed:10944123, ECO:0000269|PubMed:28334793}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-
1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-
phosphatidyl-1D-myo-inositol.
-!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-
anchor biosynthesis.
-!- SUBUNIT: Associates with PIGA, PIGC, PIGH, PIGQ and DPM2. The
latter is not essential for activity.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=B;
IsoId=P57054-1; Sequence=Displayed;
Name=A;
IsoId=P57054-2; Sequence=VSP_004202;
Name=C; Synonyms=DCRC-S;
IsoId=P57054-3; Sequence=VSP_004203, VSP_004204;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DISEASE: Epileptic encephalopathy, early infantile, 55 (EIEE55)
[MIM:617599]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent. EIEE55 is an
autosomal recessive condition. {ECO:0000269|PubMed:28334793}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the PIGP family. {ECO:0000305}.
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EMBL; AB037162; BAA96871.1; -; mRNA.
EMBL; AB037163; BAA96872.1; -; mRNA.
EMBL; AB037164; BAA96873.1; -; mRNA.
EMBL; AB035742; BAA95633.1; -; mRNA.
EMBL; AB035743; BAA95634.1; -; mRNA.
EMBL; AB035744; BAA95635.1; -; mRNA.
EMBL; AB035745; BAA95636.1; -; mRNA.
EMBL; AF216305; AAF32289.1; -; mRNA.
EMBL; AB039659; BAB12395.1; -; mRNA.
EMBL; AF237812; AAG09757.1; -; mRNA.
EMBL; BT007053; AAP35702.1; -; mRNA.
EMBL; AK314457; BAG37065.1; -; mRNA.
EMBL; AK316609; BAG38196.1; -; mRNA.
EMBL; AB451328; BAG70142.1; -; mRNA.
EMBL; AB451472; BAG70286.1; -; mRNA.
EMBL; AP000704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001727; BAA95512.1; -; Genomic_DNA.
EMBL; KC877872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09724.1; -; Genomic_DNA.
EMBL; CH471079; EAX09725.1; -; Genomic_DNA.
EMBL; CH471079; EAX09727.1; -; Genomic_DNA.
EMBL; CH471079; EAX09726.1; -; Genomic_DNA.
EMBL; CH471079; EAX09728.1; -; Genomic_DNA.
EMBL; BC005180; AAH05180.1; -; mRNA.
EMBL; BC011007; AAH11007.1; -; mRNA.
CCDS; CCDS13649.1; -. [P57054-1]
CCDS; CCDS13650.1; -. [P57054-2]
CCDS; CCDS82670.1; -. [P57054-3]
PIR; JC7301; JC7301.
PIR; JC7302; JC7302.
RefSeq; NP_001307409.1; NM_001320480.1. [P57054-2]
RefSeq; NP_057514.2; NM_016430.3. [P57054-3]
RefSeq; NP_710148.1; NM_153681.2. [P57054-1]
RefSeq; NP_710149.1; NM_153682.2. [P57054-2]
RefSeq; XP_005261047.1; XM_005260990.4.
RefSeq; XP_011527898.1; XM_011529596.2.
RefSeq; XP_016883853.1; XM_017028364.1.
RefSeq; XP_016883854.1; XM_017028365.1. [P57054-3]
UniGene; Hs.656565; -.
UniGene; Hs.716087; -.
ProteinModelPortal; P57054; -.
SMR; P57054; -.
BioGrid; 119391; 6.
IntAct; P57054; 6.
STRING; 9606.ENSP00000420037; -.
iPTMnet; P57054; -.
PhosphoSitePlus; P57054; -.
BioMuta; PIGP; -.
DMDM; 425906062; -.
EPD; P57054; -.
PaxDb; P57054; -.
PeptideAtlas; P57054; -.
PRIDE; P57054; -.
ProteomicsDB; 56970; -.
ProteomicsDB; 56971; -. [P57054-2]
ProteomicsDB; 56972; -. [P57054-3]
TopDownProteomics; P57054-2; -. [P57054-2]
TopDownProteomics; P57054-3; -. [P57054-3]
DNASU; 51227; -.
Ensembl; ENST00000360525; ENSP00000353719; ENSG00000185808. [P57054-2]
Ensembl; ENST00000399098; ENSP00000382049; ENSG00000185808. [P57054-3]
Ensembl; ENST00000399102; ENSP00000382053; ENSG00000185808. [P57054-2]
Ensembl; ENST00000399103; ENSP00000382054; ENSG00000185808. [P57054-2]
Ensembl; ENST00000464265; ENSP00000420037; ENSG00000185808. [P57054-1]
GeneID; 51227; -.
KEGG; hsa:51227; -.
UCSC; uc002yvw.2; human. [P57054-1]
CTD; 51227; -.
DisGeNET; 51227; -.
EuPathDB; HostDB:ENSG00000185808.13; -.
GeneCards; PIGP; -.
HGNC; HGNC:3046; PIGP.
HPA; HPA026921; -.
MalaCards; PIGP; -.
MIM; 605938; gene.
MIM; 617599; phenotype.
neXtProt; NX_P57054; -.
OpenTargets; ENSG00000185808; -.
PharmGKB; PA27498; -.
eggNOG; KOG2257; Eukaryota.
eggNOG; ENOG41121KH; LUCA.
GeneTree; ENSGT00390000013771; -.
HOVERGEN; HBG000430; -.
InParanoid; P57054; -.
KO; K03861; -.
OMA; SEVNRMF; -.
PhylomeDB; P57054; -.
TreeFam; TF323799; -.
BRENDA; 2.4.1.198; 2681.
Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
UniPathway; UPA00196; -.
ChiTaRS; PIGP; human.
GeneWiki; PIGP; -.
GenomeRNAi; 51227; -.
PRO; PR:P57054; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000185808; Expressed in 235 organ(s), highest expression level in caput epididymis.
CleanEx; HS_PIGP; -.
ExpressionAtlas; P57054; baseline and differential.
Genevisible; P57054; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000506; C:glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0017176; F:phosphatidylinositol N-acetylglucosaminyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:UniProtKB.
GO; GO:0016254; P:preassembly of GPI anchor in ER membrane; TAS:Reactome.
InterPro; IPR013717; PIG-P.
InterPro; IPR016542; PIG-P_GPI19.
Pfam; PF08510; PIG-P; 1.
PIRSF; PIRSF008765; PIG-P_GPI19; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Direct protein sequencing;
Disease mutation; Epilepsy; Glycosyltransferase;
GPI-anchor biosynthesis; Membrane; Polymorphism; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 158 Phosphatidylinositol N-
acetylglucosaminyltransferase subunit P.
/FTId=PRO_0000191783.
TRANSMEM 40 60 Helical. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
VAR_SEQ 1 50 Missing (in isoform C).
{ECO:0000303|PubMed:10814524,
ECO:0000303|PubMed:10907851,
ECO:0000303|PubMed:19054851}.
/FTId=VSP_004203.
VAR_SEQ 1 24 Missing (in isoform A).
{ECO:0000303|PubMed:10814524,
ECO:0000303|PubMed:10907851,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.5}.
/FTId=VSP_004202.
VAR_SEQ 51 52 FI -> MV (in isoform C).
{ECO:0000303|PubMed:10814524,
ECO:0000303|PubMed:10907851,
ECO:0000303|PubMed:19054851}.
/FTId=VSP_004204.
VARIANT 9 9 T -> A (in dbSNP:rs2507733).
/FTId=VAR_061521.
VARIANT 25 25 M -> T (in EIEE55; reduced GPI-anchor
biosynthetic process; may affect
expression of isoform A;
dbSNP:rs768633670).
{ECO:0000269|PubMed:28334793}.
/FTId=VAR_079291.
VARIANT 118 118 Y -> C (in dbSNP:rs16994704).
/FTId=VAR_050538.
VARIANT 136 136 R -> S (in dbSNP:rs2276231).
/FTId=VAR_050539.
CONFLICT 3 3 P -> S (in Ref. 1; BAA96872).
{ECO:0000305}.
CONFLICT 90 90 I -> V (in Ref. 1; BAA96873 and 2;
AAF32289). {ECO:0000305}.
SEQUENCE 158 AA; 18089 MW; 9309CEAC1DD777CF CRC64;
MVPRSTSLTL IVFLFHRLSK APGKMVENSP SPLPERAIYG FVLFLSSQFG FILYLVWAFI
PESWLNSLGL TYWPQKYWAV ALPVYLLIAI VIGYVLLFGI NMMSTSPLDS IHTITDNYAK
NQQQKKYQEE AIPALRDISI SEVNQMFFLA AKELYTKN


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