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 27-MAR-2024, entry version 180. 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 MUTAGENESIS OF PRO-38; GLY-92; GLU-129; 135-SER-GLY-136; CYS-139; ASP-146; RP ASN-164; CYS-182; GLU-184; 190-LYS-LYS-191; ASN-291; ASN-327; TYR-396; RP GLU-429; GLU-455; ASP-459 AND 528-VAL-ILE-529, AND FUNCTION. RX PubMed=34576938; DOI=10.3390/molecules26185462; RA Liu S.S., Jin F., Liu Y.S., Murakami Y., Sugita Y., Kato T., Gao X.D., RA Kinoshita T., Hattori M., Fujita M.; RT "Functional analysis of the GPI transamidase complex by screening for amino RT acid mutations in each subunit."; RL Molecules 26:0-0(2021). RN [17] RP VARIANT MCAHS3 PRO-183, AND INVOLVEMENT IN MCAHS3. 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). RN [18] RP VARIANTS MCAHS3 84-GLU--LEU-578 DEL AND TRP-448, INVOLVEMENT IN MCAHS3, AND RP CHARACTERIZATION OF VARIANTS MCAHS3 84-GLU--LEU-578 DEL AND TRP-448. RX PubMed=24906948; DOI=10.1007/s10048-014-0408-y; RA Nakashima M., Kashii H., Murakami Y., Kato M., Tsurusaki Y., Miyake N., RA Kubota M., Kinoshita T., Saitsu H., Matsumoto N.; RT "Novel compound heterozygous PIGT mutations caused multiple congenital RT anomalies-hypotonia-seizures syndrome 3."; RL Neurogenetics 15:193-200(2014). RN [19] RP VARIANT MCAHS3 TRP-448. RX PubMed=25943031; DOI=10.1016/j.ymgme.2015.04.007; RA Lam C., Golas G.A., Davids M., Huizing M., Kane M.S., Krasnewich D.M., RA Malicdan M.C.V., Adams D.R., Markello T.C., Zein W.M., Gropman A.L., RA Lodish M.B., Stratakis C.A., Maric I., Rosenzweig S.D., Baker E.H., RA Ferreira C.R., Danylchuk N.R., Kahler S., Garnica A.D., RA Bradley Schaefer G., Boerkoel C.F., Gahl W.A., Wolfe L.A.; RT "Expanding the clinical and molecular characteristics of PIGT-CDG, a RT disorder of glycosylphosphatidylinositol anchors."; RL Mol. Genet. Metab. 115:128-140(2015). RN [20] RP VARIANT MCAHS3 VAL-360, AND CHARACTERIZATION OF VARIANT MCAHS3 VAL-360. RX PubMed=27916860; DOI=10.3390/genes7120108; RA Skauli N., Wallace S., Chiang S.C., Baroey T., Holmgren A., RA Stray-Pedersen A., Bryceson Y.T., Stroemme P., Frengen E., Misceo D.; RT "Novel PIGT Variant in Two Brothers: Expansion of the Multiple Congenital RT Anomalies-Hypotonia Seizures Syndrome 3 Phenotype."; RL Genes (Basel) 7:0-0(2016). RN [21] RP VARIANTS MCAHS3 GLN-237 AND MET-528, AND CHARACTERIZATION OF VARIANTS RP MCAHS3 GLN-237 AND MET-528. RX PubMed=28327575; DOI=10.1038/ejhg.2017.32; RG DDD Study; RA Pagnamenta A.T., Murakami Y., Taylor J.M., Anzilotti C., Howard M.F., RA Miller V., Johnson D.S., Tadros S., Mansour S., Temple I.K., Firth R., RA Rosser E., Harrison R.E., Kerr B., Popitsch N., Kinoshita T., Taylor J.C., RA Kini U.; RT "Analysis of exome data for 4293 trios suggests GPI-anchor biogenesis RT defects are a rare cause of developmental disorders."; RL Eur. J. Hum. Genet. 25:669-679(2017). RN [22] RP VARIANTS MCAHS3 84-GLU--LEU-578 DEL AND TRP-366. RX PubMed=28728837; DOI=10.1016/j.braindev.2017.06.005; RA Kohashi K., Ishiyama A., Yuasa S., Tanaka T., Miya K., Adachi Y., Sato N., RA Saitsu H., Ohba C., Matsumoto N., Murakami Y., Kinoshita T., Sugai K., RA Sasaki M.; RT "Epileptic apnea in a patient with inherited glycosylphosphatidylinositol RT anchor deficiency and PIGT mutations."; RL Brain Dev. 40:53-57(2018). RN [23] RP VARIANT MCAHS3 LYS-184. RX PubMed=29868109; DOI=10.3389/fgene.2018.00153; RA Yang L., Peng J., Yin X.M., Pang N., Chen C., Wu T.H., Zou X.M., Yin F.; RT "Homozygous PIGT Mutation Lead to Multiple Congenital Anomalies-Hypotonia RT Seizures Syndrome 3."; RL Front. Genet. 9:153-153(2018). RN [24] RP VARIANTS MCAHS3 LYS-184; GLN-237; VAL-360; HIS-491 AND MET-528. RX PubMed=30976099; DOI=10.1038/s41436-019-0512-3; RG DDD Study Group; RA Bayat A., Knaus A., Juul A.W., Dukic D., Gardella E., Charzewska A., RA Clement E., Hjalgrim H., Hoffman-Zacharska D., Horn D., Horton R., RA Hurst J.A., Josifova D., Larsen L.H.G., Lascelles K., Obersztyn E., RA Pagnamenta A., Pal D.K., Pendziwiat M., Ryten M., Taylor J., Vogt J., RA Weber Y., Krawitz P.M., Helbig I., Kini U., Moeller R.S.; RT "PIGT-CDG, a disorder of the glycosylphosphatidylinositol anchor: RT description of 13 novel patients and expansion of the clinical RT characteristics."; RL Genet. Med. 21:2216-2223(2019). RN [25] RP VARIANT MCAHS3 PRO-183. RX PubMed=30813157; DOI=10.1097/md.0000000000014524; RA Mason S., Castilla-Vallmanya L., James C., Andrews P.I., Balcells S., RA Grinberg D., Kirk E.P., Urreizti R.; RT "Case report of a child bearing a novel deleterious splicing variant in RT PIGT."; RL Medicine (Baltimore) 98:e14524-e14524(2019). RN [26] RP VARIANTS MCAHS3 139-CYS--LEU-578 DEL AND CYS-172. RX PubMed=32404165; DOI=10.1186/s12920-020-0714-1; RA Issa M.Y., Chechlacz Z., Stanley V., George R.D., McEvoy-Venneri J., RA Belandres D., Elbendary H.M., Gaber K.R., Nabil A., Abdel-Hamid M.S., RA Zaki M.S., Gleeson J.G.; RT "Molecular diagnosis in recessive pediatric neurogenetic disease can help RT reduce disease recurrence in families."; RL BMC Med. Genomics 13:68-68(2020). RN [27] RP VARIANTS MCAHS3 ARG-366; GLN-507 AND MET-528. RX PubMed=32725661; DOI=10.1111/cge.13822; RA Jezela-Stanek A., Szczepanik E., Mierzewska H., Rydzanicz M., Rutkowska K., RA Knaus A., Smigiel R., Stepniak I., Markiewicz M.G., Boniel S., Krawitz P., RA Ploski R.; RT "Evidence of the milder phenotypic spectrum of c.1582G>A PIGT variant: RT Delineation based on seven novel Polish patients."; RL Clin. Genet. 98:468-476(2020). RN [28] RP VARIANTS MCAHS3 VAL-157; CYS-172; ASP-374 AND HIS-527. RX PubMed=32220244; DOI=10.1186/s13023-020-01365-0; RA Jiao X., Xue J., Gong P., Bao X., Wu Y., Zhang Y., Jiang Y., Yang Z.; RT "Analyzing clinical and genetic characteristics of a cohort with multiple RT congenital anomalies-hypotonia-seizures syndrome (MCAHS)."; RL Orphanet J. Rare Dis. 15:78-78(2020). RN [29] RP VARIANTS MCAHS3 84-GLU--LEU-578 DEL AND MET-528. RX PubMed=34162574; RA Hur Y.J., Lee B.L., Chung W.Y., Yu S., Jun K.R., Oh S.H.; RT "Compound Heterozygous PIGT Mutations in Multiple Congenital Anomalies- RT Hypotonia-Seizures Syndrome: First Case in Korea and Characterization by RT Persistent Hypophosphatasia."; RL Ann. Clin. Lab. Sci. 51:422-425(2021). RN [30] RP VARIANTS MCAHS3 330-ARG--LEU-578 DEL; PRO-376; TRP-448; GLN-507; TRP-507; RP SER-527 AND MET-528. RX PubMed=34046058; DOI=10.3389/fgene.2021.663643; RA Bayat A., Pendziwiat M., Obersztyn E., Goldenberg P., Zacher P., RA Doering J.H., Syrbe S., Begtrup A., Borovikov A., Sharkov A., RA Karasinska A., Gizewska M., Mitchell W., Morava E., Moeller R.S., RA Rubboli G.; RT "Deep-Phenotyping the Less Severe Spectrum of PIGT Deficiency and Linking RT the Gene to Myoclonic Atonic Seizures."; RL Front. Genet. 12:663643-663643(2021). RN [31] RP VARIANT MCAHS3 TRP-507, AND CHARACTERIZATION OF VARIANT MCAHS3 TRP-507. RX PubMed=36970549; DOI=10.3389/fneur.2023.1092887; RA Ben Ayed I., Jallouli O., Murakami Y., Souissi A., Mallouli S., Bouzid A., RA Kamoun F., Elloumi I., Frikha F., Tlili A., Weckhuysen S., Kinoshita T., RA Triki C.C., Masmoudi S.; RT "Case report: Functional analysis of the p.Arg507Trp variant of the PIGT RT gene supporting the moderate epilepsy phenotype of mutations in the C- RT terminal region."; RL Front. Neurol. 14:1092887-1092887(2023). 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 ECO:0000269|PubMed:34576938}. 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 -!- INTERACTION: CC Q969N2; O43292: GPAA1; NbExp=11; IntAct=EBI-726383, EBI-720225; CC Q969N2; Q92643: PIGK; NbExp=10; IntAct=EBI-726383, EBI-8617711; CC Q969N2; Q96S52: PIGS; NbExp=11; IntAct=EBI-726383, EBI-2908273; 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, CC ECO:0000269|PubMed:24906948, ECO:0000269|PubMed:25943031, CC ECO:0000269|PubMed:27916860, ECO:0000269|PubMed:28327575, CC ECO:0000269|PubMed:28728837, ECO:0000269|PubMed:29868109, CC ECO:0000269|PubMed:30813157, ECO:0000269|PubMed:30976099, CC ECO:0000269|PubMed:32220244, ECO:0000269|PubMed:32404165, CC ECO:0000269|PubMed:32725661, ECO:0000269|PubMed:34046058, CC ECO:0000269|PubMed:34162574, ECO:0000269|PubMed:36970549}. Note=The CC disease is caused by variants affecting the gene represented in this CC 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 variants affecting the gene represented in this 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7W72; EM; 3.10 A; T=27-552. DR PDB; 7WLD; EM; 2.53 A; T=2-578. DR PDB; 8IMX; EM; 2.85 A; T=2-578. DR PDB; 8IMY; EM; 3.22 A; T=2-578. DR PDBsum; 7W72; -. DR PDBsum; 7WLD; -. DR PDBsum; 8IMX; -. DR PDBsum; 8IMY; -. DR AlphaFoldDB; Q969N2; -. DR EMDB; EMD-32336; -. DR EMDB; EMD-32582; -. DR SMR; Q969N2; -. DR BioGRID; 119633; 245. DR ComplexPortal; CPX-6503; GPI-anchor transamidase complex. DR CORUM; Q969N2; -. DR IntAct; Q969N2; 51. DR MINT; Q969N2; -. DR STRING; 9606.ENSP00000279036; -. DR GlyConnect; 1286; 2 N-Linked glycans (1 site). DR GlyCosmos; Q969N2; 3 sites, 2 glycans. DR GlyGen; Q969N2; 5 sites, 4 N-linked glycans (1 site), 1 O-linked glycan (1 site). 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; 9606-ENSP00000279036; -. DR PeptideAtlas; 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 Pumba; Q969N2; -. DR Antibodypedia; 27619; 168 antibodies from 24 providers. DR DNASU; 51604; -. DR Ensembl; ENST00000279035.14; ENSP00000279035.8; ENSG00000124155.19. [Q969N2-4] DR Ensembl; ENST00000279036.12; ENSP00000279036.6; ENSG00000124155.19. [Q969N2-1] DR Ensembl; ENST00000372689.9; ENSP00000361774.4; ENSG00000124155.19. [Q969N2-6] DR Ensembl; ENST00000543458.7; ENSP00000441577.1; ENSG00000124155.19. [Q969N2-5] DR Ensembl; ENST00000545755.3; ENSP00000443963.3; ENSG00000124155.19. [Q969N2-2] DR GeneID; 51604; -. DR KEGG; hsa:51604; -. DR MANE-Select; ENST00000279036.12; ENSP00000279036.6; NM_015937.6; NP_057021.2. DR UCSC; uc002xoh.4; human. [Q969N2-1] DR AGR; HGNC:14938; -. DR CTD; 51604; -. DR DisGeNET; 51604; -. DR GeneCards; PIGT; -. DR HGNC; HGNC:14938; PIGT. DR HPA; ENSG00000124155; Low tissue specificity. 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 VEuPathDB; HostDB:ENSG00000124155; -. DR eggNOG; KOG2407; Eukaryota. DR GeneTree; ENSGT00390000018558; -. DR HOGENOM; CLU_021459_0_1_1; -. DR InParanoid; Q969N2; -. DR OMA; NHGHYIG; -. DR OrthoDB; 197863at2759; -. DR PhylomeDB; Q969N2; -. DR TreeFam; TF105921; -. DR PathwayCommons; Q969N2; -. DR Reactome; R-HSA-162791; Attachment of GPI anchor to uPAR. DR SignaLink; Q969N2; -. DR UniPathway; UPA00196; -. DR BioGRID-ORCS; 51604; 18 hits in 1157 CRISPR screens. 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 cardia of stomach and 180 other cell types or tissues. DR ExpressionAtlas; Q969N2; baseline and differential. 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:0016020; C:membrane; HDA:UniProtKB. 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:SF11; GPI TRANSAMIDASE COMPONENT PIG-T; 1. DR PANTHER; PTHR12959; GPI TRANSAMIDASE COMPONENT PIG-T-RELATED; 1. DR Pfam; PF04113; Gpi16; 2. DR Genevisible; Q969N2; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disease variant; Disulfide bond; Endoplasmic reticulum; Epilepsy; KW Glycoprotein; GPI-anchor biosynthesis; Membrane; 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 84..578 FT /note="Missing (in MCAHS3; loss of function in GPI-anchor FT attachment to protein)" FT /evidence="ECO:0000269|PubMed:24906948, FT ECO:0000269|PubMed:28728837, ECO:0000269|PubMed:34162574" FT /id="VAR_088155" FT VARIANT 139..578 FT /note="Missing (in MCAHS3)" FT /evidence="ECO:0000269|PubMed:32404165" FT /id="VAR_088156" FT VARIANT 157 FT /note="F -> V (in MCAHS3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32220244" FT /id="VAR_088157" FT VARIANT 172 FT /note="R -> C (in MCAHS3)" FT /evidence="ECO:0000269|PubMed:32220244, FT ECO:0000269|PubMed:32404165" FT /id="VAR_088158" FT VARIANT 183 FT /note="T -> P (in MCAHS3; decreased function in GPI-anchor FT attachment to protein; flow cytometric analysis of patient FT granulocytes and monocytes show decreased amounts of FT GPI-anchored proteins CD16B and CD59 compared to controls; FT dbSNP:rs587777027)" FT /evidence="ECO:0000269|PubMed:23636107, FT ECO:0000269|PubMed:30813157" FT /id="VAR_070448" FT VARIANT 184 FT /note="E -> K (in MCAHS3; decreased function in GPI-anchor FT attachment to protein; reduced amounts of GPI-anchored FT proteins in homozygous patient cells)" FT /evidence="ECO:0000269|PubMed:29868109, FT ECO:0000269|PubMed:30976099" FT /id="VAR_088159" FT VARIANT 237 FT /note="E -> Q (in MCAHS3; decreased function in GPI-anchor FT attachment to protein; does not rescue GPI-anchored CD59 FT surface expression as efficiently as the wild-type in FT PIGT-knockout cells)" FT /evidence="ECO:0000269|PubMed:28327575, FT ECO:0000269|PubMed:30976099" FT /id="VAR_088160" FT VARIANT 330..578 FT /note="Missing (in MCAHS3)" FT /evidence="ECO:0000269|PubMed:34046058" FT /id="VAR_088161" FT VARIANT 360 FT /note="G -> V (in MCAHS3; decreased function in GPI-anchor FT attachment to protein; reduced amounts of GPI-anchored FT proteins in homozygous patient cells)" FT /evidence="ECO:0000269|PubMed:27916860, FT ECO:0000269|PubMed:30976099" FT /id="VAR_088162" FT VARIANT 366 FT /note="G -> R (in MCAHS3)" FT /evidence="ECO:0000269|PubMed:32725661" FT /id="VAR_088163" FT VARIANT 366 FT /note="G -> W (in MCAHS3)" FT /evidence="ECO:0000269|PubMed:28728837" FT /id="VAR_088164" FT VARIANT 374 FT /note="N -> D (in MCAHS3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32220244" FT /id="VAR_088165" FT VARIANT 376 FT /note="H -> P (in MCAHS3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34046058" FT /id="VAR_088166" FT VARIANT 448 FT /note="R -> W (in MCAHS3; decreased function in GPI-anchor FT attachment to protein)" FT /evidence="ECO:0000269|PubMed:24906948, FT ECO:0000269|PubMed:25943031, ECO:0000269|PubMed:34046058" FT /id="VAR_088167" FT VARIANT 473 FT /note="A -> T (in dbSNP:rs36056071)" FT /id="VAR_053583" FT VARIANT 491 FT /note="L -> H (in MCAHS3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:30976099" FT /id="VAR_088168" FT VARIANT 507 FT /note="R -> Q (in MCAHS3)" FT /evidence="ECO:0000269|PubMed:32725661, FT ECO:0000269|PubMed:34046058" FT /id="VAR_088169" FT VARIANT 507 FT /note="R -> W (in MCAHS3; decreased function in GPI-anchor FT attachment to protein; does not rescue GPI-anchored FT proteins surface expression as efficiently as the wild-type FT in PIGT-knockout cells)" FT /evidence="ECO:0000269|PubMed:34046058, FT ECO:0000269|PubMed:36970549" FT /id="VAR_088170" FT VARIANT 527 FT /note="N -> H (in MCAHS3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32220244" FT /id="VAR_088171" FT VARIANT 527 FT /note="N -> S (in MCAHS3; uncertain significance)" FT /evidence="ECO:0000269|PubMed:34046058" FT /id="VAR_088172" FT VARIANT 528 FT /note="V -> M (in MCAHS3; decreased function in GPI-anchor FT attachment to protein; does not rescue GPI-anchored CD59 FT surface expression as efficiently as the wild-type in FT PIGT-knockout cells)" FT /evidence="ECO:0000269|PubMed:28327575, FT ECO:0000269|PubMed:30976099, ECO:0000269|PubMed:32725661, FT ECO:0000269|PubMed:34046058, ECO:0000269|PubMed:34162574" FT /id="VAR_088173" FT MUTAGEN 38 FT /note="P->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 92 FT /note="G->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 129 FT /note="E->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 135..136 FT /note="SG->AA: No effect on function in GPI-anchor FT attachment to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 139 FT /note="C->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 146 FT /note="D->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 164 FT /note="N->Q: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 182 FT /note="C->S: Decreased function in GPI-anchor attachment to FT protein." FT /evidence="ECO:0000269|PubMed:12582175, FT ECO:0000269|PubMed:34576938" FT MUTAGEN 184 FT /note="E->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 190..191 FT /note="KK->AA: No effect on function in GPI-anchor FT attachment to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 291 FT /note="N->Q: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 327 FT /note="N->Q: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 396 FT /note="Y->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 429 FT /note="E->A: Decreased function in GPI-anchor attachment to FT protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 455 FT /note="E->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 459 FT /note="D->A: No effect on function in GPI-anchor attachment FT to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT MUTAGEN 528..529 FT /note="VI->AA: No effect on function in GPI-anchor FT attachment to protein." FT /evidence="ECO:0000269|PubMed:34576938" FT STRAND 27..38 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 44..54 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 65..69 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 71..74 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 82..92 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 96..99 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 108..116 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 123..138 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 147..149 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 183..191 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 197..199 FT /evidence="ECO:0007829|PDB:7W72" FT HELIX 200..204 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 207..210 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 212..230 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 233..246 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 248..250 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 260..264 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 276..283 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 287..291 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 309..319 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 323..325 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 328..330 FT /evidence="ECO:0007829|PDB:8IMY" FT TURN 343..345 FT /evidence="ECO:0007829|PDB:8IMX" FT STRAND 351..359 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 362..374 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 381..389 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 393..404 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 412..417 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 421..423 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 426..434 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 436..447 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 453..455 FT /evidence="ECO:0007829|PDB:7W72" FT TURN 460..462 FT /evidence="ECO:0007829|PDB:8IMX" FT STRAND 464..466 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 470..476 FT /evidence="ECO:0007829|PDB:7WLD" FT TURN 486..488 FT /evidence="ECO:0007829|PDB:7W72" FT HELIX 491..493 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:8IMX" FT STRAND 503..509 FT /evidence="ECO:0007829|PDB:7WLD" FT STRAND 513..515 FT /evidence="ECO:0007829|PDB:7WLD" FT HELIX 527..548 FT /evidence="ECO:0007829|PDB:7WLD" 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 //