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Database: UniProt
Entry: C5M6G0_CANTT
LinkDB: C5M6G0_CANTT
Original site: C5M6G0_CANTT 
ID   C5M6G0_CANTT            Unreviewed;      1028 AA.
AC   C5M6G0;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN   ORFNames=CTRG_01441 {ECO:0000313|EMBL:EER34580.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER34580.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER34580.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
CC   -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGO subfamily.
CC       {ECO:0000256|ARBA:ARBA00008695}.
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DR   EMBL; GG692396; EER34580.1; -; Genomic_DNA.
DR   RefSeq; XP_002547135.1; XM_002547089.1.
DR   AlphaFoldDB; C5M6G0; -.
DR   STRING; 294747.C5M6G0; -.
DR   EnsemblFungi; CTRG_01441-t43_1; CTRG_01441-t43_1-p1; CTRG_01441.
DR   GeneID; 8301329; -.
DR   KEGG; ctp:CTRG_01441; -.
DR   VEuPathDB; FungiDB:CTRG_01441; -.
DR   eggNOG; KOG2126; Eukaryota.
DR   HOGENOM; CLU_004298_1_0_1; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
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.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        57..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        505..530
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        536..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        579..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        609..626
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        638..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        676..696
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        708..727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        739..766
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        813..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        842..861
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        917..941
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        953..976
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        988..1013
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  116713 MW;  45A18908432E7F68 CRC64;
     MTDENGITRR SMSPTQQQQQ PIMHTQAQQQ AQSFAKDPRL QPPTRTRIRQ QKLKYTFVGY
     IIVLIFLAIT QVIGVLFFKE GFLLSRTVLP NISTCKEQND CMNPRFEKAI FLVIDALRFD
     FVIPIPGSEE YYHNNFPILY DLANSKSDHA VLLKFMADPP TTTLQRLKGL TTGSLPTFID
     AGSNFDGDAI DEDNWLLQLH RINKTIAFMG DDTWKALFSE YIHPDYNFPY DSLNVWDLHT
     VDNGVIEHMY PLISKENCTK WDLLVGHFLG VDHVGHRYGP RHYSMKEKLN QMNDVVTKVI
     KSMDDKTLLV IIGDHGMDST GNHGGDSKDE LESTLFMYSK SKKFLKKDKS HYNITDMGKN
     YRSVNQIDLV PTMSLLLGLP IPYNNLGFPI DEAFGSIKEL STASQKTIDQ IKKFRKDTPS
     LSDSLLEEYD SYNSNYDTFG ASKKHFSNLI EQAKLYQYLS LEQCKGLWAT FDLRFIGIGL
     GILFLSLTFM ITYSRSIPAV RVSTMSFEFI GSVIAMSIMG LVLSFSIFIV LKPGDFTLNI
     CLSIGAALGM VIGFWAPIMD RFSVGFLWHQ TIDFFLYNFN SWSFMGIVFV AFHCLIFASN
     SYVVWEDKMV QFFLLTFGGT CIYACYTSNK LSEKAKVLAL SHAITFTMCT RLASMINLCR
     EEQRPYCTPT FATSWWSILL LHLVAYLLPA CIKSFYHLSD SYHSAAPLWI GTGLKFLLFM
     NAVYWTFEFV STNEYFSKIN LLIGTSLLVS FKLAIARLVL FISLVLANFS WSRGPLCVKL
     ELSNSANNSI HLEETDDDDN SDSDSSNNKT ATILGYGNVY GSSYFLLVLN FTVAIMLTTK
     PIGALSISLL IVQILSLLEI LDVLEIRKNL ITPIIFGLLG YQHFFSTGHQ ATLQSIQWEM
     GFMTTETIVF PFTHLNIFLN TMGPFLLTGL AIPLITIWKI IPSSKPITLL SQIITNITTL
     ITYHLFTGLS SLLFAAHFRR HLMVWKIFAP RFMLSGILII SLNIFLIFIT LWFGTGRILS
     QINRIFGK
//
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