ID F8Q3G6_SERL3 Unreviewed; 990 AA.
AC F8Q3G6;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN ORFNames=SERLA73DRAFT_56998 {ECO:0000313|EMBL:EGN97727.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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; GL945482; EGN97727.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q3G6; -.
DR STRING; 936435.F8Q3G6; -.
DR eggNOG; KOG2126; Eukaryota.
DR HOGENOM; CLU_004298_1_1_1; -.
DR InParanoid; F8Q3G6; -.
DR OMA; YPSFDIF; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000008063; 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:UP000008063};
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 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..521
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 580..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 619..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 879..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 953..975
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 990 AA; 108265 MW; F3BED24079DB2F31 CRC64;
MLSKQIYLLL WVLFVHLAGI YLFTKGFLLN RLSLSDSSIC SHDVCTSLAT HKKAILLVID
ALRFDFISND PPHPASPYHH NILTLPRELT EQHPERSFIF NAYADPPTTT LQRIKGLTTG
SLPTFVDIGS SFGGSAIEED SLIHQLQVAG RKIAFMGDDT WTTVFPDIFE SNMSFPYDSF
NVEDLHTVDE GVVMHLLPLL SDRTLSWDFA IAHGLGVDHA GHRVGPDHPT MRAKLAQMND
LLIRVVDLLE DDTLLVVIGD HGMDRTGNHG GDSVLETMSA VWIYSKGPIL SGRTSSIPQT
ILPNIVFPGA SVPHRLIQQV DIVPSLSLLL GLPIPFNNLG SIIPELFDRD TEHYILEQAL
DANAVQIQKY TETYRATSSG KELDAAWLDF QSAWAASQST SSEERVASLF DYNRLVLSSC
RVLWAQFNSI LIGCGLAVII AGVLAGLVLY LGLNYSDKPE QWLSDQLSRC LFGIVGGAVA
GTAVYFLLKS RVEGIGASHS IIFSSAFISS LVIIISSYAS FSFNALKSIS LPLVLHALCF
ASNSFTIWED RLVLYLLLTS MVPSVLTGFT APTPRLRYRI LGYSAVFAIC VRLMAMSTVC
REEQQIHCLV SFYSSSSSSA PHLLPLFLAL PTSFALPRIM KKILSTSKSD GCLAAFFLPY
FLTPALVAGS LFWMLEWAQS ADLFDELAGD NLRVIRTIMA RGVIVGMAVV GLAVWRVVPV
CLEIQRDQQV DTETKGTTHD QDEKKQVTVL GFANAFGSPY LIFWSIFLAL VWATTQLTGQ
IILGLTTIAL LAYLEVADGV RDVVGLNAAF TSGNPSSISD LDLSHIRVPL TFSKIVPLAL
LGIHAFHGTG HQPTIPSMQW KTAFVLAKNV VFPFSQATVI LNTLGPHFLL ALASPLLVLW
NLPPLPPPSL SIPSLRAALG ISLYYSTLLL GSAGSAAALR RHLMVWKIFA PRYMFAAVSL
IAIDLGALIG VVIGVDRIRE RITKIFQAIA
//
