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Database: UniProt
Entry: R4XCD8_TAPDE
LinkDB: R4XCD8_TAPDE
Original site: R4XCD8_TAPDE 
ID   R4XCD8_TAPDE            Unreviewed;       969 AA.
AC   R4XCD8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=GPI ethanolamine phosphate transferase 1 {ECO:0000256|ARBA:ARBA00020831, ECO:0000256|RuleBase:RU367138};
DE            EC=2.-.-.- {ECO:0000256|RuleBase:RU367138};
GN   ORFNames=TAPDE_003715 {ECO:0000313|EMBL:CCG83486.1};
OS   Taphrina deformans (strain PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563
OS   / JCM 9778 / NBRC 8474) (Peach leaf curl fungus) (Lalaria deformans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Taphrinomycetes;
OC   Taphrinales; Taphrinaceae; Taphrina.
OX   NCBI_TaxID=1097556 {ECO:0000313|EMBL:CCG83486.1, ECO:0000313|Proteomes:UP000013776};
RN   [1] {ECO:0000313|EMBL:CCG83486.1, ECO:0000313|Proteomes:UP000013776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PYCC 5710 / ATCC 11124 / CBS 356.35 / IMI 108563 / JCM 9778 /
RC   NBRC 8474 {ECO:0000313|Proteomes:UP000013776};
RX   PubMed=23631913; DOI=10.1128/mBio.00055-13;
RA   Cisse O.H., Almeida J.M.G.C.F., Fonseca A., Kumar A.A., Salojaervi J.,
RA   Overmyer K., Hauser P.M., Pagni M.;
RT   "Genome sequencing of the plant pathogen Taphrina deformans, the causal
RT   agent of peach leaf curl.";
RL   MBio 4:e00055-e00013(2013).
CC   -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC       glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC       ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC       glycosylphosphatidylinositol precursor of GPI-anchor.
CC       {ECO:0000256|ARBA:ARBA00024850, ECO:0000256|RuleBase:RU367138}.
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687,
CC       ECO:0000256|RuleBase:RU367138}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367138}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU367138}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC       {ECO:0000256|ARBA:ARBA00008400, ECO:0000256|RuleBase:RU367138}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCG83486.1}.
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DR   EMBL; CAHR02000153; CCG83486.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4XCD8; -.
DR   STRING; 1097556.R4XCD8; -.
DR   VEuPathDB; FungiDB:TAPDE_003715; -.
DR   eggNOG; KOG2124; Eukaryota.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000013776; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd16020; GPI_EPT_1; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR007070; GPI_EtnP_transferase_1.
DR   InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR037671; PIGN_N.
DR   PANTHER; PTHR12250:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 1; 1.
DR   PANTHER; PTHR12250; PHOSPHATIDYLINOSITOL GLYCAN, CLASS N; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF04987; PigN; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU367138};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502,
KW   ECO:0000256|RuleBase:RU367138};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367138};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013776};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367138};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367138};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367138}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        455..477
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        529..551
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        558..575
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        595..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        672..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        723..742
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        762..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        834..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        873..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        908..927
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        933..956
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   DOMAIN          444..932
FT                   /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04987"
SQ   SEQUENCE   969 AA;  107871 MW;  A92652295479D15B CRC64;
     MVSRGWVLTI GVLFHLIYLR SIFDIYFKSP VVSVEEQHGS SLDDPAILHE EGASPADRLF
     LIVGDGLRAD KLFENPQLAP FLHDKAINSG RWGISHTRVP TESRPGHVAL IAGLYEDVSA
     VTTGWKLNPI NFDSVFNQSR KTWAWGSPDI LPMFREGATI KENVICEMYD SEEEDFTEDS
     DKLDTWVFEH VDALFAKAKD DEALARDLRA PKSVFFLHLL GLDTAGHAHR PYSKEYLNNI
     AVVDNGIAQL MKTLEGSWSQ QEMERTTFLF TADHGMSDWG SHGDGHPDNT RTPYIAWGSG
     VRKPSPYDPL VVSASLKTHH TAHERLNWSV EQNSRVDVAQ ADLAAFMSYS VNIPFPKNNV
     GLVPTELLTA DEQSKAVAIF QNARQIHAQY SSKAELKARM LHYSNMIHYT FDKDYYTTGM
     THIRNRDWPE LSAMSQDWIH ESLKGMRYLQ KYDWLFLRTI ISLGYLGWML FALIFVIKSY
     VIPYTGHYQA LAKEKQIELL MGQKIVPGSA TRNANGHPTY LPPAVDPNVT SSSTIVDASF
     GALAVGVLAY LLEKSSPLSY YAYAAFPVYF WYKIIQEIPA ITSSLRTVTT TSKRAWPAAL
     GLALLGVVII QGVVNAYAHR QIISIMWPLA SVTPFLYPGA SSSVQKTAWV MLCTAMSTFT
     SLPTVQTEDI RFVVLGGALM ALIGLAYILL RGGSFTLGAQ VGLVALTTMV TKESSQSLAD
     KQGLPLGCQV LGWTCLVSSL LLPLCHRLER KPGETINYQQ RLIILFLTFA PTFVILSVSY
     EGLFYLVFWA LLVTWMHLES GIADSLAHDS KVVHTTYPSS ESGHRGLQFS DARVALYFFF
     LIQAAFFGTG NIASVSSFSL DSVYRLIPIF SPFAMGLLLL FKLLVPFAVI SATLGLLNRK
     LKVAPSAIFM TVLTFCDILT LNFFWMVRDE GSWLEIGSSI SAFVIGGLLI LFVICLEKVS
     EWMVGDVVM
//
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