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Database: UniProt
Entry: C5FG65_ARTOC
LinkDB: C5FG65_ARTOC
Original site: C5FG65_ARTOC 
ID   C5FG65_ARTOC            Unreviewed;       997 AA.
AC   C5FG65;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 61.
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=MCYG_02569 {ECO:0000313|EMBL:EEQ29750.1};
OS   Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX   NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ29750.1, ECO:0000313|Proteomes:UP000002035};
RN   [1] {ECO:0000313|Proteomes:UP000002035}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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}.
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DR   EMBL; DS995702; EEQ29750.1; -; Genomic_DNA.
DR   RefSeq; XP_002849635.1; XM_002849589.1.
DR   AlphaFoldDB; C5FG65; -.
DR   STRING; 554155.C5FG65; -.
DR   GeneID; 9222685; -.
DR   VEuPathDB; FungiDB:MCYG_02569; -.
DR   eggNOG; KOG2124; Eukaryota.
DR   HOGENOM; CLU_007676_0_0_1; -.
DR   OMA; TISHFCI; -.
DR   OrthoDB; 6598at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002035; 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   GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
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:UP000002035};
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        473..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        512..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        536..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        573..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        600..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        625..642
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        654..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        691..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        730..749
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        778..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        842..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        884..904
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        916..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   TRANSMEM        941..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367138"
FT   DOMAIN          462..940
FT                   /note="GPI ethanolamine phosphate transferase 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04987"
SQ   SEQUENCE   997 AA;  110935 MW;  5A42B3339D7C5E32 CRC64;
     MSRTGLFLAL AVLFHLIYTY SIFDIYFVSP IVSGMREYGV ERAPEAKAPA KRLVLFVGDG
     LRADKAFQYF PDPSPPQTIC SRDDEGSIAC PEPDLTPKPL APFLRSRVLE HGTFGVSHTR
     VPTESRPGHV ALIAGLYEDV SAVTTGWKLN PVNFDSVFNR SRHTWSWGSP DILPMFKEGA
     VPGRISVDMY SEEDEDFTRD ATVLDTWVFD RVKEMFATAK EDKNLDAQLR DDKVVFFLHL
     LGLDTTGHFY RPYSKEYLHN IQVVDQGVRE ITELIDDFYG DEETAFVFTA DHGMSDWGSH
     GDGHPDNTRT PLIVWGSGVA KPVKTNGAVA PGHEDGFSSD WHLNNIKRHD VAQADVAALM
     AYLIGLDFPV NSVGELPLSY LDATPREKAK AALANTQGVL EMYRVKEEQK RAATIRYQGY
     TPFTQPQRSP EAQLAAIRKL ISTGKYEQSI LQSRSLFQDA LDGLRYLQTY DWLFLRAIVT
     AGYLGWISYA LVTVIDLHVL PMSLEPDRSI PSFMFFSSVL VVLYSVLWVQ QSTWRYYAYA
     FFPVLFWEEV FARRAALGAG QKVLLGHVKS FTGYLVLLLQ SLLYIGVLQG LVQSYFNREI
     YTVCYLLGAV WPALYGLDFL SNNKFLSAAW TVNCILMSSF TLLPVGKQDN ADTVTYGGIL
     MFGIGMLYLI FEESILSSSK VKTSTGSTFN IGSRIVMGAQ IGIILLSIIV TRSSIASLQA
     RTGLPLGNQV TGWIAMISSF VLPVLHKFFP TGHYLHRLIV LFLTFAPTFI VLTISYEGLF
     YVVYFATLVS WVRLEHSIYR YTLPPKATPS ISREATPRAV TTDSGAPATT SYRTLNLPDA
     RIALFFLFLL QSGFFSTGNI ASISSFSLDS VSRLIPVFNP FSQGALLILK ILVPFALLSA
     TFGILNRRLH VAPSALFMIV MCISDVMTLN FFFMVRDEGS WLDIGTTISH FCISSGLCVF
     VAIIESLSGA FISGVNFDGS HSQENQLDAT EKSAVSD
//
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