PIGG_HUMAN
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
