GenomeNet

Database: UniProt/SWISS-PROT
Entry: PIGT_HUMAN
LinkDB: PIGT_HUMAN
Original site: PIGT_HUMAN 
ID   PIGT_HUMAN              Reviewed;         578 AA.
AC   Q969N2; B2RND5; B7Z3N1; B7Z7I8; E1P622; G8JLF5; Q2NL69; Q7Z3N7; Q9BQY7;
AC   Q9BQY8; Q9UJG6; Q9Y2Z5;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-DEC-2019, entry version 158.
DE   RecName: Full=GPI transamidase component PIG-T;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class T protein;
DE   Flags: Precursor;
GN   Name=PIGT; ORFNames=CGI-06, PSEC0163, UNQ716/PRO1379;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 22-41,
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX   PubMed=11483512; DOI=10.1093/emboj/20.15.4088;
RA   Ohishi K., Inoue N., Kinoshita T.;
RT   "PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a
RT   complex with GAA1 and GPI8.";
RL   EMBO J. 20:4088-4098(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   TISSUE=Testis, and Thalamus;
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 MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Signet-ring cell carcinoma;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, Leukocyte, Skin, and Testis;
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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-578 (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-578 (ISOFORM 1).
RX   PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA   Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT   "Identification of novel human genes evolutionarily conserved in
RT   Caenorhabditis elegans by comparative proteomics.";
RL   Genome Res. 10:703-713(2000).
RN   [11]
RP   DISULFIDE BOND FORMATION WITH PIGK/GPI8, AND MUTAGENESIS OF CYS-182.
RX   PubMed=12582175; DOI=10.1074/jbc.m300586200;
RA   Ohishi K., Nagamune K., Maeda Y., Kinoshita T.;
RT   "Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T,
RT   form a functionally important intermolecular disulfide bridge.";
RL   J. Biol. Chem. 278:13959-13967(2003).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-164.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   INVOLVEMENT IN PNH2.
RX   PubMed=23733340; DOI=10.1182/blood-2013-01-481499;
RA   Krawitz P.M., Hochsmann B., Murakami Y., Teubner B., Kruger U.,
RA   Klopocki E., Neitzel H., Hoellein A., Schneider C., Parkhomchuk D.,
RA   Hecht J., Robinson P.N., Mundlos S., Kinoshita T., Schrezenmeier H.;
RT   "A case of paroxysmal nocturnal hemoglobinuria caused by a germline
RT   mutation and a somatic mutation in PIGT.";
RL   Blood 122:1312-1315(2013).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [16]
RP   VARIANT MCAHS3 PRO-183.
RX   PubMed=23636107; DOI=10.1136/jmedgenet-2013-101654;
RA   Kvarnung M., Nilsson D., Lindstrand A., Korenke G.C., Chiang S.C.,
RA   Blennow E., Bergmann M., Stodberg T., Makitie O., Anderlid B.M.,
RA   Bryceson Y.T., Nordenskjold M., Nordgren A.;
RT   "A novel intellectual disability syndrome caused by GPI anchor deficiency
RT   due to homozygous mutations in PIGT.";
RL   J. Med. Genet. 50:521-528(2013).
CC   -!- FUNCTION: Component of the GPI transamidase complex. Essential for
CC       transfer of GPI to proteins, particularly for formation of carbonyl
CC       intermediates. {ECO:0000269|PubMed:11483512}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a complex with PIGK/GPI8, PIGS, PIGU and GPAA1/GAA1. Has
CC       a critical role in maintaining the complex by stabilizing the
CC       expression of GPAA1 and GPI8 and linking them to PIGS.
CC       {ECO:0000269|PubMed:11483512}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:11483512}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:11483512}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q969N2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q969N2-2; Sequence=VSP_009537;
CC       Name=3;
CC         IsoId=Q969N2-3; Sequence=VSP_009536, VSP_009539, VSP_009540;
CC       Name=4;
CC         IsoId=Q969N2-4; Sequence=VSP_009538;
CC       Name=5;
CC         IsoId=Q969N2-5; Sequence=VSP_043167;
CC       Name=6;
CC         IsoId=Q969N2-6; Sequence=VSP_009540;
CC   -!- PTM: The disulfide bond between PIGK/GPI8 and PIGT is important for
CC       normal enzyme activity.
CC   -!- DISEASE: Multiple congenital anomalies-hypotonia-seizures syndrome 3
CC       (MCAHS3) [MIM:615398]: An autosomal recessive syndrome characterized by
CC       distinct facial features, intellectual disability, hypotonia and
CC       seizures, in combination with abnormal skeletal, endocrine, and
CC       ophthalmologic findings including impaired vision, as well as abnormal
CC       motility of the eyes. {ECO:0000269|PubMed:23636107}. Note=The disease
CC       is caused by mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Paroxysmal nocturnal hemoglobinuria 2 (PNH2) [MIM:615399]: A
CC       disorder characterized by hemolytic anemia with hemoglobinuria,
CC       thromboses in large vessels, and a deficiency in hematopoiesis. Red
CC       blood cell breakdown with release of hemoglobin into the urine is
CC       manifested most prominently by dark-colored urine in the morning.
CC       {ECO:0000269|PubMed:23733340}. Note=Disease susceptibility is
CC       associated with variations affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PIGT family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD27715.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAQ88951.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB57341.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; AB057724; BAB60854.1; -; mRNA.
DR   EMBL; AK296139; BAH12267.1; -; mRNA.
DR   EMBL; AK302093; BAH13624.1; -; mRNA.
DR   EMBL; AK075469; BAC11639.1; -; mRNA.
DR   EMBL; AK225517; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BX537612; CAD97799.1; -; mRNA.
DR   EMBL; AL121742; CAB57341.1; ALT_INIT; mRNA.
DR   EMBL; AL021578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75844.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75845.1; -; Genomic_DNA.
DR   EMBL; CH471077; EAW75846.1; -; Genomic_DNA.
DR   EMBL; BC015022; AAH15022.3; -; mRNA.
DR   EMBL; BC110892; AAI10893.1; -; mRNA.
DR   EMBL; BC136827; AAI36828.1; -; mRNA.
DR   EMBL; BC136828; AAI36829.1; -; mRNA.
DR   EMBL; AY358588; AAQ88951.1; ALT_INIT; mRNA.
DR   EMBL; AF132940; AAD27715.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS13353.1; -. [Q969N2-1]
DR   CCDS; CCDS54464.1; -. [Q969N2-5]
DR   CCDS; CCDS54465.1; -. [Q969N2-6]
DR   CCDS; CCDS54466.1; -. [Q969N2-4]
DR   RefSeq; NP_001171657.1; NM_001184728.2. [Q969N2-5]
DR   RefSeq; NP_001171658.1; NM_001184729.2. [Q969N2-6]
DR   RefSeq; NP_001171659.1; NM_001184730.2. [Q969N2-4]
DR   RefSeq; NP_057021.2; NM_015937.5. [Q969N2-1]
DR   BioGrid; 119633; 44.
DR   CORUM; Q969N2; -.
DR   IntAct; Q969N2; 44.
DR   MINT; Q969N2; -.
DR   STRING; 9606.ENSP00000279036; -.
DR   GlyConnect; 1286; -.
DR   iPTMnet; Q969N2; -.
DR   PhosphoSitePlus; Q969N2; -.
DR   SwissPalm; Q969N2; -.
DR   BioMuta; PIGT; -.
DR   DMDM; 44888284; -.
DR   CPTAC; CPTAC-1499; -.
DR   EPD; Q969N2; -.
DR   jPOST; Q969N2; -.
DR   MassIVE; Q969N2; -.
DR   MaxQB; Q969N2; -.
DR   PaxDb; Q969N2; -.
DR   PeptideAtlas; Q969N2; -.
DR   PRIDE; Q969N2; -.
DR   ProteomicsDB; 34213; -.
DR   ProteomicsDB; 75800; -. [Q969N2-1]
DR   ProteomicsDB; 75801; -. [Q969N2-2]
DR   ProteomicsDB; 75802; -. [Q969N2-3]
DR   ProteomicsDB; 75803; -. [Q969N2-4]
DR   ProteomicsDB; 75804; -. [Q969N2-5]
DR   Ensembl; ENST00000279035; ENSP00000279035; ENSG00000124155. [Q969N2-4]
DR   Ensembl; ENST00000279036; ENSP00000279036; ENSG00000124155. [Q969N2-1]
DR   Ensembl; ENST00000372689; ENSP00000361774; ENSG00000124155. [Q969N2-6]
DR   Ensembl; ENST00000543458; ENSP00000441577; ENSG00000124155. [Q969N2-5]
DR   Ensembl; ENST00000545755; ENSP00000443963; ENSG00000124155. [Q969N2-2]
DR   GeneID; 51604; -.
DR   KEGG; hsa:51604; -.
DR   UCSC; uc002xoh.4; human. [Q969N2-1]
DR   CTD; 51604; -.
DR   DisGeNET; 51604; -.
DR   EuPathDB; HostDB:ENSG00000124155.16; -.
DR   GeneCards; PIGT; -.
DR   HGNC; HGNC:14938; PIGT.
DR   MalaCards; PIGT; -.
DR   MIM; 610272; gene.
DR   MIM; 615398; phenotype.
DR   MIM; 615399; phenotype.
DR   neXtProt; NX_Q969N2; -.
DR   OpenTargets; ENSG00000124155; -.
DR   Orphanet; 369837; Intellectual disability-seizures-hypophosphatasia-ophthalmic-skeletal anomalies syndrome.
DR   PharmGKB; PA33302; -.
DR   eggNOG; KOG2407; Eukaryota.
DR   eggNOG; ENOG410XRR0; LUCA.
DR   GeneTree; ENSGT00390000018558; -.
DR   InParanoid; Q969N2; -.
DR   KO; K05292; -.
DR   OMA; DANHGHY; -.
DR   OrthoDB; 887370at2759; -.
DR   PhylomeDB; Q969N2; -.
DR   TreeFam; TF105921; -.
DR   Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR.
DR   UniPathway; UPA00196; -.
DR   ChiTaRS; PIGT; human.
DR   GeneWiki; PIGT; -.
DR   GenomeRNAi; 51604; -.
DR   Pharos; Q969N2; Tbio.
DR   PRO; PR:Q969N2; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q969N2; protein.
DR   Bgee; ENSG00000124155; Expressed in 95 organ(s), highest expression level in heart.
DR   ExpressionAtlas; Q969N2; baseline and differential.
DR   Genevisible; Q969N2; HS.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0042765; C:GPI-anchor transamidase complex; IDA:UniProtKB.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0003923; F:GPI-anchor transamidase activity; IEA:Ensembl.
DR   GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR   GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR   InterPro; IPR007245; PIG-T.
DR   PANTHER; PTHR12959; PTHR12959; 1.
DR   Pfam; PF04113; Gpi16; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Endoplasmic reticulum; Epilepsy; Glycoprotein;
KW   GPI-anchor biosynthesis; Membrane; Polymorphism; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:11483512"
FT   CHAIN           22..578
FT                   /note="GPI transamidase component PIG-T"
FT                   /id="PRO_0000024107"
FT   TOPO_DOM        22..527
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        528..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        549..578
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        291
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        327
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        182
FT                   /note="Interchain (with C-92 in PIGK/GPI8)"
FT                   /evidence="ECO:0000269|PubMed:12582175"
FT   VAR_SEQ         1..144
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_009536"
FT   VAR_SEQ         63..256
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_009537"
FT   VAR_SEQ         63..164
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_009538"
FT   VAR_SEQ         109..164
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043167"
FT   VAR_SEQ         145..164
FT                   /note="IDSTNTVTPTASFKPLGLAN -> MWIPRGQSPRPTPDRPLSPS (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_009539"
FT   VAR_SEQ         345..412
FT                   /note="EAPPVPFLHAQRYVSGYGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLY
FT                   VHTLTITSKGKENKPS -> G (in isoform 3 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.4"
FT                   /id="VSP_009540"
FT   VARIANT         183
FT                   /note="T -> P (in MCAHS3; flow cytometric analysis of
FT                   patient granulocytes and monocytes show decreased amounts
FT                   of GPI-anchored proteins CD16B and CD59 compared to
FT                   controls; dbSNP:rs587777027)"
FT                   /evidence="ECO:0000269|PubMed:23636107"
FT                   /id="VAR_070448"
FT   VARIANT         473
FT                   /note="A -> T (in dbSNP:rs36056071)"
FT                   /id="VAR_053583"
FT   MUTAGEN         182
FT                   /note="C->S: Decrease in activity."
FT                   /evidence="ECO:0000269|PubMed:12582175"
SQ   SEQUENCE   578 AA;  65700 MW;  AC7865160CFBCBBA CRC64;
     MAAAMPLALL VLLLLGPGGW CLAEPPRDSL REELVITPLP SGDVAATFQF RTRWDSELQR
     EGVSHYRLFP KALGQLISKY SLRELHLSFT QGFWRTRYWG PPFLQAPSGA ELWVWFQDTV
     TDVDKSWKEL SNVLSGIFCA SLNFIDSTNT VTPTASFKPL GLANDTDHYF LRYAVLPREV
     VCTENLTPWK KLLPCSSKAG LSVLLKADRL FHTSYHSQAV HIRPVCRNAR CTSISWELRQ
     TLSVVFDAFI TGQGKKDWSL FRMFSRTLTE PCPLASESRV YVDITTYNQD NETLEVHPPP
     TTTYQDVILG TRKTYAIYDL LDTAMINNSR NLNIQLKWKR PPENEAPPVP FLHAQRYVSG
     YGLQKGELST LLYNTHPYRA FPVLLLDTVP WYLRLYVHTL TITSKGKENK PSYIHYQPAQ
     DRLQPHLLEM LIQLPANSVT KVSIQFERAL LKWTEYTPDP NHGFYVSPSV LSALVPSMVA
     AKPVDWEESP LFNSLFPVSD GSNYFVRLYT EPLLVNLPTP DFSMPYNVIC LTCTVVAVCY
     GSFYNLLTRT FHIEEPRTGG LAKRLANLIR RARGVPPL
//
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