PIGO_HUMAN
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 03-AUG-2022, entry version 171.
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 intellectual disability syndrome 2
CC (HPMRS2) [MIM:614749]: An autosomal recessive form of intellectual
CC disability characterized by facial dysmorphism, brachytelephalangy, and
CC persistent elevated serum alkaline phosphatase (hyperphosphatasia).
CC Some patients may have additional features, such as cardiac septal
CC 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};
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; 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. [Q8TEQ8-1]
DR RefSeq; XP_016870712.1; XM_017015223.1. [Q8TEQ8-2]
DR RefSeq; XP_016870713.1; XM_017015224.1. [Q8TEQ8-2]
DR AlphaFoldDB; Q8TEQ8; -.
DR SMR; Q8TEQ8; -.
DR BioGRID; 124223; 83.
DR IntAct; Q8TEQ8; 17.
DR MINT; Q8TEQ8; -.
DR STRING; 9606.ENSP00000367880; -.
DR GlyGen; Q8TEQ8; 1 site.
DR iPTMnet; Q8TEQ8; -.
DR PhosphoSitePlus; Q8TEQ8; -.
DR BioMuta; PIGO; -.
DR DMDM; 61252289; -.
DR EPD; Q8TEQ8; -.
DR jPOST; Q8TEQ8; -.
DR MassIVE; Q8TEQ8; -.
DR MaxQB; Q8TEQ8; -.
DR PaxDb; Q8TEQ8; -.
DR PeptideAtlas; Q8TEQ8; -.
DR PRIDE; Q8TEQ8; -.
DR ProteomicsDB; 74479; -. [Q8TEQ8-1]
DR ProteomicsDB; 74480; -. [Q8TEQ8-2]
DR Antibodypedia; 11435; 151 antibodies from 23 providers.
DR DNASU; 84720; -.
DR Ensembl; ENST00000298004.9; ENSP00000298004.5; ENSG00000165282.14. [Q8TEQ8-2]
DR Ensembl; ENST00000361778.6; ENSP00000354678.2; ENSG00000165282.14. [Q8TEQ8-2]
DR Ensembl; ENST00000378617.4; ENSP00000367880.3; ENSG00000165282.14. [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 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; LGDSTWT; -.
DR OrthoDB; 848878at2759; -.
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 1086 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 185 other tissues.
DR Genevisible; Q8TEQ8; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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; PTHR23071; 1.
DR Pfam; PF01663; Phosphodiest; 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..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 (probable disease-associated variant found in
FT a patient with epileptic encephalopathy; 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; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28900819"
FT /id="VAR_079411"
FT VARIANT 344
FT /note="M -> K (in HPMRS2; decrease in mannose-ethanolamine
FT phosphotransferase activity; decreased protein expression;
FT unknown pathological significance; 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; unknown pathological
FT significance; 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
