ID   PIGO_HUMAN              Reviewed;        1089 AA.
AC   Q8TEQ8; B1AML3; Q6P154; Q6UX80; Q8TDS8; Q96CS9; Q9BVN9; Q9Y4B0;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 3.
DT   27-MAR-2024, entry version 180.
DE   RecName: Full=GPI ethanolamine phosphate transferase 3;
DE            EC=2.-.-.-;
DE   AltName: Full=Phosphatidylinositol-glycan biosynthesis class O protein;
DE            Short=PIG-O;
GN   Name=PIGO; ORFNames=UNQ632/PRO1249;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lamerdin J.E., McCready P.M., Skowronski E., Adamson A.W.,
RA   Burkhart-Schultz K., Gordon L., Kyle A., Ramirez M., Stilwagen S., Phan H.,
RA   Velasco N., Garnes J., Danganan L., Poundstone P., Christensen M.,
RA   Georgescu A., Avila J., Liu S., Attix C., Andreise T., Trankheim M.,
RA   Amico-Keller G., Coefield J., Duarte S., Lucas S., Bruce R., Thomas P.,
RA   Quan G., Kronmiller B., Arellano A., Montgomery M., Ow D., Nolan M.,
RA   Trong S., Kobayashi A., Olsen A.O., Carrano A.V.;
RT   "Sequence analysis of a human P1 clone containing the XRCC9 DNA repair
RT   gene.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Duodenum, Eye, and Lung;
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   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 601-968.
RX   PubMed=12044878; DOI=10.1016/s0014-5793(02)02775-8;
RA   Takeda S., Kadowaki S., Haga T., Takaesu H., Mitaku S.;
RT   "Identification of G protein-coupled receptor genes from the human genome
RT   sequence.";
RL   FEBS Lett. 520:97-101(2002).
RN   [9]
RP   VARIANT [LARGE SCALE ANALYSIS] MET-686.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [10]
RP   VARIANT HPMRS2 PHE-957.
RX   PubMed=22683086; DOI=10.1016/j.ajhg.2012.05.004;
RA   Krawitz P.M., Murakami Y., Hecht J., Kruger U., Holder S.E., Mortier G.R.,
RA   Delle Chiaie B., De Baere E., Thompson M.D., Roscioli T., Kielbasa S.,
RA   Kinoshita T., Mundlos S., Robinson P.N., Horn D.;
RT   "Mutations in PIGO, a member of the GPI-anchor-synthesis pathway, cause
RT   hyperphosphatasia with mental retardation.";
RL   Am. J. Hum. Genet. 91:146-151(2012).
RN   [11]
RP   VARIANT HPMRS2 TRP-119, CHARACTERIZATION OF VARIANT HPMRS2 TRP-119, AND
RP   FUNCTION.
RX   PubMed=24049131; DOI=10.1212/wnl.0b013e3182a8411a;
RA   Kuki I., Takahashi Y., Okazaki S., Kawawaki H., Ehara E., Inoue N.,
RA   Kinoshita T., Murakami Y.;
RT   "Vitamin B6-responsive epilepsy due to inherited GPI deficiency.";
RL   Neurology 81:1467-1469(2013).
RN   [12]
RP   VARIANT ASN-130.
RX   PubMed=24417746; DOI=10.1111/epi.12508;
RA   Nakamura K., Osaka H., Murakami Y., Anzai R., Nishiyama K., Kodera H.,
RA   Nakashima M., Tsurusaki Y., Miyake N., Kinoshita T., Matsumoto N.,
RA   Saitsu H.;
RT   "PIGO mutations in intractable epilepsy and severe developmental delay with
RT   mild elevation of alkaline phosphatase levels.";
RL   Epilepsia 55:E13-E17(2014).
RN   [13]
RP   VARIANTS HPMRS2 LYS-344; SER-370; 430-GLN--ARG-1089 DEL AND GLU-1047,
RP   CHARACTERIZATION OF VARIANTS HPMRS2 TRP-119; LYS-344; SER-370; PHE-957 AND
RP   GLU-1047, CHARACTERIZATION OF ASN-130, AND FUNCTION.
RX   PubMed=28337824; DOI=10.1002/humu.23219;
RA   Tanigawa J., Mimatsu H., Mizuno S., Okamoto N., Fukushi D., Tominaga K.,
RA   Kidokoro H., Muramatsu Y., Nishi E., Nakamura S., Motooka D., Nomura N.,
RA   Hayasaka K., Niihori T., Aoki Y., Nabatame S., Hayakawa M., Natsume J.,
RA   Ozono K., Kinoshita T., Wakamatsu N., Murakami Y.;
RT   "Phenotype-genotype correlations of PIGO deficiency with variable
RT   phenotypes from infantile lethality to mild learning difficulties.";
RL   Hum. Mutat. 38:805-815(2017).
RN   [14]
RP   VARIANT ILE-255.
RX   PubMed=28900819; DOI=10.1007/s11011-017-0109-y;
RA   Zehavi Y., von Renesse A., Daniel-Spiegel E., Sapir Y., Zalman L.,
RA   Chervinsky I., Schuelke M., Straussberg R., Spiegel R.;
RT   "A homozygous PIGO mutation associated with severe infantile epileptic
RT   encephalopathy and corpus callosum hypoplasia, but normal alkaline
RT   phosphatase levels.";
RL   Metab. Brain Dis. 32:2131-2137(2017).
RN   [15]
RP   VARIANT HPMRS2 PRO-871.
RX   PubMed=28545593; DOI=10.1186/s13023-017-0654-9;
RA   Morren M.A., Jaeken J., Visser G., Salles I., Van Geet C., Simeoni I.,
RA   Turro E., Freson K.;
RT   "PIGO deficiency: palmoplantar keratoderma and novel mutations.";
RL   Orphanet J. Rare Dis. 12:101-101(2017).
CC   -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC       glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC       ethanolamine phosphate to the GPI third mannose which links the GPI-
CC       anchor to the C-terminus of the proteins by an amide bond.
CC       {ECO:0000269|PubMed:24049131, ECO:0000269|PubMed:28337824}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis.
CC   -!- SUBUNIT: Forms a complex with PIGF. PIGF is required to stabilize PIGO
CC       (By similarity). {ECO:0000250|UniProtKB:Q9JJI6}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9JJI6}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=Q8TEQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TEQ8-2; Sequence=VSP_003944;
CC   -!- DISEASE: Hyperphosphatasia with impaired intellectual development
CC       syndrome 2 (HPMRS2) [MIM:614749]: An autosomal recessive form of
CC       intellectual disability characterized by facial dysmorphism,
CC       brachytelephalangy, and persistent elevated serum alkaline phosphatase
CC       (hyperphosphatasia). Some patients may have additional features, such
CC       as cardiac septal defects or seizures. {ECO:0000269|PubMed:22683086,
CC       ECO:0000269|PubMed:24049131, ECO:0000269|PubMed:28337824,
CC       ECO:0000269|PubMed:28545593}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC07985.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAH01030.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH13987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB84890.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC03414.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAD38806.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AL833956; CAD38806.1; ALT_FRAME; mRNA.
DR   EMBL; AK074064; BAB84890.1; ALT_FRAME; mRNA.
DR   EMBL; AK090433; BAC03414.1; ALT_FRAME; mRNA.
DR   EMBL; AY358472; AAQ88836.1; -; mRNA.
DR   EMBL; AC004472; AAC07985.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL353795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471071; EAW58397.1; -; Genomic_DNA.
DR   EMBL; BC001030; AAH01030.1; ALT_INIT; mRNA.
DR   EMBL; BC013987; AAH13987.1; ALT_INIT; mRNA.
DR   EMBL; BC029271; AAH29271.1; -; mRNA.
DR   EMBL; BC036916; AAH36916.1; -; mRNA.
DR   EMBL; BC065282; AAH65282.1; -; mRNA.
DR   EMBL; AB083625; BAB89338.1; -; Genomic_DNA.
DR   CCDS; CCDS6575.1; -. [Q8TEQ8-1]
DR   CCDS; CCDS6576.1; -. [Q8TEQ8-2]
DR   PIR; T02245; T02245.
DR   RefSeq; NP_001188413.1; NM_001201484.1. [Q8TEQ8-2]
DR   RefSeq; NP_116023.2; NM_032634.3. [Q8TEQ8-1]
DR   RefSeq; NP_690577.2; NM_152850.3. [Q8TEQ8-2]
DR   RefSeq; XP_005251676.1; XM_005251619.3. [Q8TEQ8-1]
DR   RefSeq; XP_016870711.1; XM_017015222.1.
DR   RefSeq; XP_016870712.1; XM_017015223.1.
DR   RefSeq; XP_016870713.1; XM_017015224.1.
DR   AlphaFoldDB; Q8TEQ8; -.
DR   SMR; Q8TEQ8; -.
DR   BioGRID; 124223; 87.
DR   ComplexPortal; CPX-2679; Glycosylphosphatidylinsitol ethanolamine-phosphate transferase III complex.
DR   IntAct; Q8TEQ8; 17.
DR   MINT; Q8TEQ8; -.
DR   STRING; 9606.ENSP00000367880; -.
DR   GlyCosmos; Q8TEQ8; 1 site, No reported glycans.
DR   GlyGen; Q8TEQ8; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8TEQ8; -.
DR   PhosphoSitePlus; Q8TEQ8; -.
DR   SwissPalm; Q8TEQ8; -.
DR   BioMuta; PIGO; -.
DR   DMDM; 61252289; -.
DR   EPD; Q8TEQ8; -.
DR   jPOST; Q8TEQ8; -.
DR   MassIVE; Q8TEQ8; -.
DR   MaxQB; Q8TEQ8; -.
DR   PaxDb; 9606-ENSP00000367880; -.
DR   PeptideAtlas; Q8TEQ8; -.
DR   ProteomicsDB; 74479; -. [Q8TEQ8-1]
DR   ProteomicsDB; 74480; -. [Q8TEQ8-2]
DR   Pumba; Q8TEQ8; -.
DR   Antibodypedia; 11435; 158 antibodies from 23 providers.
DR   DNASU; 84720; -.
DR   Ensembl; ENST00000298004.9; ENSP00000298004.5; ENSG00000165282.15. [Q8TEQ8-2]
DR   Ensembl; ENST00000361778.7; ENSP00000354678.2; ENSG00000165282.15. [Q8TEQ8-2]
DR   Ensembl; ENST00000378617.4; ENSP00000367880.3; ENSG00000165282.15. [Q8TEQ8-1]
DR   Ensembl; ENST00000700254.1; ENSP00000514892.1; ENSG00000165282.15. [Q8TEQ8-2]
DR   Ensembl; ENST00000700257.1; ENSP00000514894.1; ENSG00000165282.15. [Q8TEQ8-1]
DR   GeneID; 84720; -.
DR   KEGG; hsa:84720; -.
DR   MANE-Select; ENST00000378617.4; ENSP00000367880.3; NM_032634.4; NP_116023.2.
DR   UCSC; uc003zwd.4; human. [Q8TEQ8-1]
DR   AGR; HGNC:23215; -.
DR   CTD; 84720; -.
DR   DisGeNET; 84720; -.
DR   GeneCards; PIGO; -.
DR   HGNC; HGNC:23215; PIGO.
DR   HPA; ENSG00000165282; Low tissue specificity.
DR   MalaCards; PIGO; -.
DR   MIM; 614730; gene.
DR   MIM; 614749; phenotype.
DR   neXtProt; NX_Q8TEQ8; -.
DR   OpenTargets; ENSG00000165282; -.
DR   Orphanet; 247262; Hyperphosphatasia-intellectual disability syndrome.
DR   PharmGKB; PA134993507; -.
DR   VEuPathDB; HostDB:ENSG00000165282; -.
DR   eggNOG; KOG2126; Eukaryota.
DR   GeneTree; ENSGT00910000144278; -.
DR   HOGENOM; CLU_004298_2_1_1; -.
DR   InParanoid; Q8TEQ8; -.
DR   OMA; YPSFDIF; -.
DR   OrthoDB; 5479199at2759; -.
DR   PhylomeDB; Q8TEQ8; -.
DR   TreeFam; TF354249; -.
DR   PathwayCommons; Q8TEQ8; -.
DR   Reactome; R-HSA-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR   SignaLink; Q8TEQ8; -.
DR   SIGNOR; Q8TEQ8; -.
DR   UniPathway; UPA00196; -.
DR   BioGRID-ORCS; 84720; 47 hits in 1167 CRISPR screens.
DR   ChiTaRS; PIGO; human.
DR   GenomeRNAi; 84720; -.
DR   Pharos; Q8TEQ8; Tbio.
DR   PRO; PR:Q8TEQ8; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q8TEQ8; Protein.
DR   Bgee; ENSG00000165282; Expressed in mucosa of transverse colon and 187 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IMP:UniProtKB.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:UniProtKB.
DR   CDD; cd16023; GPI_EPT_3; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR037675; PIG-O_N.
DR   InterPro; IPR039524; PIGO/GPI13.
DR   PANTHER; PTHR23071:SF1; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 3; 1.
DR   PANTHER; PTHR23071; PHOSPHATIDYLINOSITOL GLYCAN; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   Genevisible; Q8TEQ8; HS.
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..1089
FT                   /note="GPI ethanolamine phosphate transferase 3"
FT                   /id="PRO_0000058438"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        457..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        482..502
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        510..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        541..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        575..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        668..688
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        747..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        830..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        857..877
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        944..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1014..1034
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1048..1068
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         449..865
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_003944"
FT   VARIANT         119
FT                   /note="R -> W (in HPMRS2; decrease in mannose-ethanolamine
FT                   phosphotransferase activity; dbSNP:rs757441073)"
FT                   /evidence="ECO:0000269|PubMed:24049131,
FT                   ECO:0000269|PubMed:28337824"
FT                   /id="VAR_079410"
FT   VARIANT         130
FT                   /note="T -> N (found in a patient with epileptic
FT                   encephalopathy; likely pathogenic; decrease in
FT                   mannose-ethanolamine phosphotransferase activity; decreased
FT                   protein expression)"
FT                   /evidence="ECO:0000269|PubMed:24417746"
FT                   /id="VAR_071074"
FT   VARIANT         255
FT                   /note="M -> I (found in patients with severe infantile
FT                   epileptic encephalopathy; uncertain significance;
FT                   dbSNP:rs1829550863)"
FT                   /evidence="ECO:0000269|PubMed:28900819"
FT                   /id="VAR_079411"
FT   VARIANT         344
FT                   /note="M -> K (in HPMRS2; uncertain significance; decrease
FT                   in mannose-ethanolamine phosphotransferase activity;
FT                   decreased protein expression; dbSNP:rs779525065)"
FT                   /evidence="ECO:0000269|PubMed:28337824"
FT                   /id="VAR_079412"
FT   VARIANT         370
FT                   /note="N -> S (in HPMRS2; decrease in mannose-ethanolamine
FT                   phosphotransferase activity; decreased protein expression;
FT                   dbSNP:rs1214104267)"
FT                   /evidence="ECO:0000269|PubMed:28337824"
FT                   /id="VAR_079413"
FT   VARIANT         430..1089
FT                   /note="Missing (in HPMRS2)"
FT                   /evidence="ECO:0000269|PubMed:28337824"
FT                   /id="VAR_079414"
FT   VARIANT         686
FT                   /note="L -> M (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036332"
FT   VARIANT         871
FT                   /note="H -> P (in HPMRS2; uncertain significance;
FT                   dbSNP:rs909488930)"
FT                   /evidence="ECO:0000269|PubMed:28545593"
FT                   /id="VAR_079415"
FT   VARIANT         957
FT                   /note="L -> F (in HPMRS2; dbSNP:rs142164373)"
FT                   /evidence="ECO:0000269|PubMed:22683086"
FT                   /id="VAR_068809"
FT   VARIANT         1047
FT                   /note="K -> E (in HPMRS2; decrease in mannose-ethanolamine
FT                   phosphotransferase activity; increased protein expression)"
FT                   /evidence="ECO:0000269|PubMed:28337824"
FT                   /id="VAR_079416"
FT   CONFLICT        179..181
FT                   /note="DDT -> ARG (in Ref. 7; AAH13987)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225..231
FT                   /note="DVLIAHF -> EVSNQHV (in Ref. 7; AAH01030)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="G -> W (in Ref. 7; AAH29271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        353
FT                   /note="D -> Y (in Ref. 7; AAH29271)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        415..416
FT                   /note="KG -> R (in Ref. 1; CAD38806)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        884..969
FT                   /note="PFTVPWQAVSAWALMATQTFYSTGHQPVFPAIHWHAAFVGFPEGHGSCTWLP
FT                   ALLVGANTFASHLLFAVGCPLLLLWPFLCESQGL -> KYLSSDSLKDNSDVSSAPLVF
FT                   KEVLLLMFLSLTEGPMPHTTRKVFLVSSLLPAIAKQIDPSCWFPGFMERRDKESSKTPC
FT                   GNAASS (in Ref. 8; BAB89338)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1089 AA;  118699 MW;  0F47404F6FAD50B6 CRC64;
     MQKASVLLFL AWVCFLFYAG IALFTSGFLL TRLELTNHSS CQEPPGPGSL PWGSQGKPGA
     CWMASRFSRV VLVLIDALRF DFAQPQHSHV PREPPVSLPF LGKLSSLQRI LEIQPHHARL
     YRSQVDPPTT TMQRLKALTT GSLPTFIDAG SNFASHAIVE DNLIKQLTSA GRRVVFMGDD
     TWKDLFPGAF SKAFFFPSFN VRDLDTVDNG ILEHLYPTMD SGEWDVLIAH FLGVDHCGHK
     HGPHHPEMAK KLSQMDQVIQ GLVERLENDT LLVVAGDHGM TTNGDHGGDS ELEVSAALFL
     YSPTAVFPST PPEEPEVIPQ VSLVPTLALL LGLPIPFGNI GEVMAELFSG GEDSQPHSSA
     LAQASALHLN AQQVSRFLHT YSAATQDLQA KELHQLQNLF SKASADYQWL LQSPKGAEAT
     LPTVIAELQQ FLRGARAMCI ESWARFSLVR MAGGTALLAA SCFICLLASQ WAISPGFPFC
     PLLLTPVAWG LVGAIAYAGL LGTIELKLDL VLLGAVAAVS SFLPFLWKAW AGWGSKRPLA
     TLFPIPGPVL LLLLFRLAVF FSDSFVVAEA RATPFLLGSF ILLLVVQLHW EGQLLPPKLL
     TMPRLGTSAT TNPPRHNGAY ALRLGIGLLL CTRLAGLFHR CPEETPVCHS SPWLSPLASM
     VGGRAKNLWY GACVAALVAL LAAVRLWLRR YGNLKSPEPP MLFVRWGLPL MALGTAAYWA
     LASGADEAPP RLRVLVSGAS MVLPRAVAGL AASGLALLLW KPVTVLVKAG AGAPRTRTVL
     TPFSGPPTSQ ADLDYVVPQI YRHMQEEFRG RLERTKSQGP LTVAAYQLGS VYSAAMVTAL
     TLLAFPLLLL HAERISLVFL LLFLQSFLLL HLLAAGIPVT TPGPFTVPWQ AVSAWALMAT
     QTFYSTGHQP VFPAIHWHAA FVGFPEGHGS CTWLPALLVG ANTFASHLLF AVGCPLLLLW
     PFLCESQGLR KRQQPPGNEA DARVRPEEEE EPLMEMRLRD APQHFYAALL QLGLKYLFIL
     GIQILACALA ASILRRHLMV WKVFAPKFIF EAVGFIVSSV GLLLGIALVM RVDGAVSSWF
     RQLFLAQQR
//