ID   PIGG_HUMAN              Reviewed;         983 AA.
AC   Q5H8A4; B4DKC7; Q2TAK5; Q6UX31; Q7L5Y4; Q8N866; Q8NCC9; Q96SY9; Q9BVT7;
AC   Q9NXG5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2;
DE            EC=2.-.-.-;
DE   AltName: Full=GPI7 homolog;
DE            Short=hGPI7;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class G protein;
DE            Short=PIG-G;
GN   Name=PIGG; Synonyms=GPI7; ORFNames=UNQ1930/PRO4405;
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), FUNCTION, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH PIGF.
RX   PubMed=15632136; DOI=10.1074/jbc.m413755200;
RA   Shishioh N., Hong Y., Ohishi K., Ashida H., Maeda Y., Kinoshita T.;
RT   "GPI7 is the second partner of PIG-F and involved in modification of
RT   glycosylphosphatidylinositol.";
RL   J. Biol. Chem. 280:9728-9734(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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] (ISOFORMS 5 AND 6), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 367-983 (ISOFORM 1), AND VARIANT ILE-699.
RC   TISSUE=Cervix, Colon mucosa, Teratocarcinoma, 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS HIS-458;
RP   ARG-610 AND ILE-699.
RC   TISSUE=Lung, and Placenta;
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   [7]
RP   VARIANT NEDHSCA CYS-669, INVOLVEMENT IN NEDHSCA, AND CHARACTERIZATION OF
RP   VARIANT NEDHSCA CYS-669.
RX   PubMed=26996948; DOI=10.1016/j.ajhg.2016.02.007;
RA   Makrythanasis P., Kato M., Zaki M.S., Saitsu H., Nakamura K., Santoni F.A.,
RA   Miyatake S., Nakashima M., Issa M.Y., Guipponi M., Letourneau A.,
RA   Logan C.V., Roberts N., Parry D.A., Johnson C.A., Matsumoto N., Hamamy H.,
RA   Sheridan E., Kinoshita T., Antonarakis S.E., Murakami Y.;
RT   "Pathogenic variants in PIGG cause intellectual disability with seizures
RT   and hypotonia.";
RL   Am. J. Hum. Genet. 98:615-626(2016).
RN   [8]
RP   VARIANTS TRP-505 DEL AND ASN-538.
RX   PubMed=31303265; DOI=10.1016/j.ajhg.2019.06.007;
RG   DDD Study;
RA   Snijders Blok L., Kleefstra T., Venselaar H., Maas S., Kroes H.Y.,
RA   Lachmeijer A.M.A., van Gassen K.L.I., Firth H.V., Tomkins S., Bodek S.,
RA   Ounap K., Wojcik M.H., Cunniff C., Bergstrom K., Powis Z., Tang S.,
RA   Shinde D.N., Au C., Iglesias A.D., Izumi K., Leonard J., Abou Tayoun A.,
RA   Baker S.W., Tartaglia M., Niceta M., Dentici M.L., Okamoto N., Miyake N.,
RA   Matsumoto N., Vitobello A., Faivre L., Philippe C., Gilissen C., Wiel L.,
RA   Pfundt R., Deriziotis P., Brunner H.G., Fisher S.E.;
RT   "De Novo Variants Disturbing the Transactivation Capacity of POU3F3 Cause a
RT   Characteristic Neurodevelopmental Disorder.";
RL   Am. J. Hum. Genet. 105:403-412(2019).
CC   -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC       glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC       ethanolamine phosphate to the GPI second mannose.
CC       {ECO:0000269|PubMed:15632136}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a complex with PIGF. PIGF is required to stabilize it.
CC       Competes with PIGO for the binding of PIGF.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15632136}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:15632136}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q5H8A4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5H8A4-2; Sequence=VSP_019832;
CC       Name=3;
CC         IsoId=Q5H8A4-3; Sequence=VSP_019828;
CC       Name=4;
CC         IsoId=Q5H8A4-4; Sequence=VSP_019831, VSP_019833;
CC       Name=5;
CC         IsoId=Q5H8A4-5; Sequence=VSP_019827, VSP_019829, VSP_019830;
CC       Name=6;
CC         IsoId=Q5H8A4-6; Sequence=VSP_054387, VSP_054388, VSP_019833;
CC   -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ88902.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA91046.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55130.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB162713; BAD89023.1; -; mRNA.
DR   EMBL; AY358538; AAQ88902.1; ALT_SEQ; mRNA.
DR   EMBL; AK074815; BAC11227.1; -; mRNA.
DR   EMBL; AK000272; BAA91046.1; ALT_INIT; mRNA.
DR   EMBL; AK027465; BAB55130.1; ALT_INIT; mRNA.
DR   EMBL; AK097244; BAC04984.1; -; mRNA.
DR   EMBL; AK296507; BAG59139.1; -; mRNA.
DR   EMBL; AC092574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC000937; AAH00937.2; -; mRNA.
DR   EMBL; BC001249; AAH01249.2; -; mRNA.
DR   EMBL; BC110878; AAI10879.1; -; mRNA.
DR   CCDS; CCDS3336.1; -. [Q5H8A4-2]
DR   CCDS; CCDS46992.1; -. [Q5H8A4-1]
DR   CCDS; CCDS75080.1; -. [Q5H8A4-3]
DR   CCDS; CCDS75083.1; -. [Q5H8A4-5]
DR   RefSeq; NP_001120650.1; NM_001127178.2. [Q5H8A4-1]
DR   RefSeq; NP_001275980.1; NM_001289051.1.
DR   RefSeq; NP_001275981.1; NM_001289052.1. [Q5H8A4-3]
DR   RefSeq; NP_001275984.1; NM_001289055.1. [Q5H8A4-6]
DR   RefSeq; NP_001275986.1; NM_001289057.1. [Q5H8A4-5]
DR   RefSeq; NP_060203.3; NM_017733.4. [Q5H8A4-2]
DR   AlphaFoldDB; Q5H8A4; -.
DR   SMR; Q5H8A4; -.
DR   BioGRID; 120220; 110.
DR   IntAct; Q5H8A4; 11.
DR   MINT; Q5H8A4; -.
DR   STRING; 9606.ENSP00000415203; -.
DR   GlyGen; Q5H8A4; 1 site.
DR   iPTMnet; Q5H8A4; -.
DR   PhosphoSitePlus; Q5H8A4; -.
DR   BioMuta; PIGG; -.
DR   DMDM; 74707851; -.
DR   EPD; Q5H8A4; -.
DR   jPOST; Q5H8A4; -.
DR   MassIVE; Q5H8A4; -.
DR   MaxQB; Q5H8A4; -.
DR   PaxDb; Q5H8A4; -.
DR   PeptideAtlas; Q5H8A4; -.
DR   PRIDE; Q5H8A4; -.
DR   ProteomicsDB; 4448; -.
DR   ProteomicsDB; 62844; -. [Q5H8A4-1]
DR   ProteomicsDB; 62845; -. [Q5H8A4-2]
DR   ProteomicsDB; 62846; -. [Q5H8A4-3]
DR   ProteomicsDB; 62847; -. [Q5H8A4-4]
DR   ProteomicsDB; 62848; -. [Q5H8A4-5]
DR   Antibodypedia; 3105; 10 antibodies from 9 providers.
DR   DNASU; 54872; -.
DR   Ensembl; ENST00000310340.9; ENSP00000311750.5; ENSG00000174227.16. [Q5H8A4-2]
DR   Ensembl; ENST00000383028.8; ENSP00000372494.4; ENSG00000174227.16. [Q5H8A4-3]
DR   Ensembl; ENST00000453061.7; ENSP00000415203.2; ENSG00000174227.16. [Q5H8A4-1]
DR   Ensembl; ENST00000503111.5; ENSP00000426002.1; ENSG00000174227.16. [Q5H8A4-5]
DR   GeneID; 54872; -.
DR   KEGG; hsa:54872; -.
DR   MANE-Select; ENST00000453061.7; ENSP00000415203.2; NM_001127178.3; NP_001120650.1.
DR   UCSC; uc003gaj.6; human. [Q5H8A4-1]
DR   CTD; 54872; -.
DR   DisGeNET; 54872; -.
DR   GeneCards; PIGG; -.
DR   HGNC; HGNC:25985; PIGG.
DR   HPA; ENSG00000174227; Low tissue specificity.
DR   MalaCards; PIGG; -.
DR   MIM; 616917; phenotype.
DR   MIM; 616918; gene.
DR   neXtProt; NX_Q5H8A4; -.
DR   OpenTargets; ENSG00000174227; -.
DR   Orphanet; 488635; Early-onset epilepsy-intellectual disability-brain anomalies syndrome.
DR   Orphanet; 280; Wolf-Hirschhorn syndrome.
DR   PharmGKB; PA143485575; -.
DR   VEuPathDB; HostDB:ENSG00000174227; -.
DR   eggNOG; KOG2125; Eukaryota.
DR   GeneTree; ENSGT00910000144269; -.
DR   HOGENOM; CLU_055386_0_0_1; -.
DR   InParanoid; Q5H8A4; -.
DR   OMA; RVKFGHD; -.
DR   OrthoDB; 848878at2759; -.
DR   PhylomeDB; Q5H8A4; -.
DR   TreeFam; TF300609; -.
DR   PathwayCommons; Q5H8A4; -.
DR   Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   SignaLink; Q5H8A4; -.
DR   SIGNOR; Q5H8A4; -.
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 54872; 10 hits in 1076 CRISPR screens.
DR   ChiTaRS; PIGG; human.
DR   GenomeRNAi; 54872; -.
DR   Pharos; Q5H8A4; Tbio.
DR   PRO; PR:Q5H8A4; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q5H8A4; protein.
DR   Bgee; ENSG00000174227; Expressed in right uterine tube and 184 other tissues.
DR   ExpressionAtlas; Q5H8A4; baseline and differential.
DR   Genevisible; Q5H8A4; HS.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IDA:MGI.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; TAS:Reactome.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IDA:MGI.
DR   GO; GO:0016254; P:preassembly of GPI anchor in ER membrane; TAS:Reactome.
DR   CDD; cd16024; GPI_EPT_2; 1.
DR   Gene3D; 3.40.720.10; -; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR037674; PIG-G_N.
DR   InterPro; IPR039527; PIGG/GPI7.
DR   InterPro; IPR045687; PIGG/GPI7_C.
DR   PANTHER; PTHR23072; PTHR23072; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF19316; PIGO_PIGG; 1.
DR   SUPFAM; SSF53649; SSF53649; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW   GPI-anchor biosynthesis; Intellectual disability; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..983
FT                   /note="GPI ethanolamine phosphate transferase 2"
FT                   /id="PRO_0000246185"
FT   TOPO_DOM        1..431
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        471..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        506..526
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        552..572
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        699..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        721..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        752..772
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        789..809
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        812..832
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        879..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        919..939
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        955..975
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..122
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054387"
FT   VAR_SEQ         1..89
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_019827"
FT   VAR_SEQ         120..252
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019828"
FT   VAR_SEQ         372..388
FT                   /note="DPGFEQFKMSERLHGNW -> GSHPAPAQRPTGTAQKG (in isoform
FT                   5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_019829"
FT   VAR_SEQ         389..983
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_019830"
FT   VAR_SEQ         430..463
FT                   /note="YDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAEL -> FSPCSCSASHRHCT
FT                   ERLSWKSHCHLLGFLCSFIW (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_019831"
FT   VAR_SEQ         430..463
FT                   /note="YDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAEL -> FSPCSCSASHRHCA
FT                   ERLSWKSHCHLLGFLCSFIW (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054388"
FT   VAR_SEQ         437..444
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16303743"
FT                   /id="VSP_019832"
FT   VAR_SEQ         464..983
FT                   /note="Missing (in isoform 4 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:12975309,
FT                   ECO:0000303|PubMed:14702039"
FT                   /id="VSP_019833"
FT   VARIANT         55
FT                   /note="S -> Y (in dbSNP:rs34120878)"
FT                   /id="VAR_057680"
FT   VARIANT         458
FT                   /note="R -> H (in dbSNP:rs13115344)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027022"
FT   VARIANT         505
FT                   /note="Missing (unknown pathological significance)"
FT                   /evidence="ECO:0000269|PubMed:31303265"
FT                   /id="VAR_083080"
FT   VARIANT         538
FT                   /note="K -> N (found in SNIBFIS; unknown pathological
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:31303265"
FT                   /id="VAR_083081"
FT   VARIANT         610
FT                   /note="C -> R (in dbSNP:rs7666425)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027023"
FT   VARIANT         669
FT                   /note="R -> C (in MRT53; almost complete loss of
FT                   ethanolamine phosphate transferase activity, as evidenced
FT                   by abnormal accumulation of the GPI precursors H7 and H7'
FT                   and absence of mature GPI precursor H8 in patient
FT                   lymphocytes; does not affect protein expression levels in
FT                   transfected HEK293 cells; dbSNP:rs372392424)"
FT                   /evidence="ECO:0000269|PubMed:26996948"
FT                   /id="VAR_076775"
FT   VARIANT         699
FT                   /note="V -> I (in dbSNP:rs13114026)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027024"
FT   VARIANT         731
FT                   /note="V -> I (in dbSNP:rs34916638)"
FT                   /id="VAR_060086"
FT   VARIANT         881
FT                   /note="I -> T (in dbSNP:rs34623004)"
FT                   /id="VAR_060087"
FT   VARIANT         932
FT                   /note="F -> S (in dbSNP:rs1127410)"
FT                   /id="VAR_027025"
FT   CONFLICT        624
FT                   /note="D -> G (in Ref. 3; BAC11227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        889
FT                   /note="F -> L (in Ref. 3; BAC11227)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   983 AA;  108173 MW;  18D5DF737B000D2D CRC64;
     MRLGSGTFAT CCVAIEVLGI AVFLRGFFPA PVRSSARAEH GAEPPAPEPS AGASSNWTTL
     PPPLFSKVVI VLIDALRDDF VFGSKGVKFM PYTTYLVEKG ASHSFVAEAK PPTVTMPRIK
     ALMTGSLPGF VDVIRNLNSP ALLEDSVIRQ AKAAGKRIVF YGDETWVKLF PKHFVEYDGT
     TSFFVSDYTE VDNNVTRHLD KVLKRGDWDI LILHYLGLDH IGHISGPNSP LIGQKLSEMD
     SVLMKIHTSL QSKERETPLP NLLVLCGDHG MSETGSHGAS STEEVNTPLI LISSAFERKP
     GDIRHPKHVQ QTDVAATLAI ALGLPIPKDS VGSLLFPVVE GRPMREQLRF LHLNTVQLSK
     LLQENVPSYE KDPGFEQFKM SERLHGNWIR LYLEEKHSEV LFNLGSKVLR QYLDALKTLS
     LSLSAQVAQY DIYSMMVGTV VVLEVLTLLL LSVPQALRRK AELEVPLSSP GFSLLFYLVI
     LVLSAVHVIV CTSAESSCYF CGLSWLAAGG VMVLASALLC VIVSVLTNVL VGGNTPRKNP
     MHPSSRWSEL DLLILLGTAG HVLSLGASSF VEEEHQTWYF LVNTLCLALS QETYRNYFLG
     DDGEPPCGLC VEQGHDGATA AWQDGPGCDV LERDKGHGSP STSEVLRGRE KWMVLASPWL
     ILACCRLLRS LNQTGVQWAH RPDLGHWLTS SDHKAELSVL AALSLLVVFV LVQRGCSPVS
     KAALALGLLG VYCYRAAIGS VRFPWRPDSK DISKGIIEAR FVYVFVLGIL FTGTKDLLKS
     QVIAADFKLK TVGLWEIYSG LVLLAALLFR PHNLPVLAFS LLIQTLMTKF IWKPLRHDAA
     EITVMHYWFG QAFFYFQGNS NNIATVDISA GFVGLDTYVE IPAVLLTAFG TYAGPVLWAS
     HLVHFLSSET RSGSALSHAC FCYALICSIP VFTYIVLVTS LRYHLFIWSV FSPKLLYEGM
     HLLITAAVCV FFTAMDQTRL TQS
//