ID A0A165MVK9_EXIGL Unreviewed; 962 AA.
AC A0A165MVK9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN ORFNames=EXIGLDRAFT_723883 {ECO:0000313|EMBL:KZV99827.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV99827.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV99827.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV99827.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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; KV425906; KZV99827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165MVK9; -.
DR STRING; 1314781.A0A165MVK9; -.
DR InParanoid; A0A165MVK9; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000077266; 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:UP000077266};
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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 407..433
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 473..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..526
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..614
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 635..653
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 918..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 962 AA; 104495 MW; 46857F49A642AB7B CRC64;
MARSIYLLLS LSLVHVAGIF LFCRGFLLSR RALDRVSLCP DGRCTLNATH NRAVVLIIDA
LRFDFVSPHP PEPHSPFHHN VLTLPRELSQ SQPDRSFLYH SFVDPPTTTL QRIKGITTGS
LSTFVDMGSN FGGSEITEDS LIVQLARARR RMVFMGDDTW LTVYPTAFER KFPFDSFNVE
DLHTVDNGVI ANIFPVLEPG APHWDVAIGH FLGVDHVGHR VGPDNTAMRD KLAQMDDVLR
RVVNALDDNT LLVVMGDHGM DEKGDHGGDG ARETSAALWI YSKSLPLSSS PPPEYLAQTT
PFVGAQYEHR LVQQIDLVPS LALLLGLPIP FNNLGTVIPE LFGDRLDDAL KLNAQQIWEY
LKEYRASASG DELDASWETL SGAWRSARSS ADRARFTRLA LEACRAMWAQ FTMGLMFAGL
SIIALSTILG IALFLRSARV EDQELITAAA SSVLSGLFVF ASTWAVFDSK DVVPGHVALF
FGSCLFCFVL LVSTVRSGQL SFSLSWSALP VGLHTISLLS NSFILWEDRM SLFFLLSTTA
PSILVAFLSP DARMRNRILG FSLVLAACGR LMSVSTVCRE EQAPYCTPTY YATGGSQAPP
LLALVLSPLA ALVLPELVRR VLAISASDGG PMRFVLAYVV RGALLVGSAC WVLEYLESSA
QDAPSWIRLA RTILVRLSLL VTLVGGMAFW WYGPLCIEVR RDGTRVEVLG FANAVGAPYL
LFFMLAGVVP LWTSTQISGQ VVLLLAFAAL FAWIEIVDSS RDVRAMRTPK AAQAALAALS
GKQPPATPVP EPDTEVRFGE VAAVALLAQL AFFGTGHQAT LQSIQWKTAF VLSRSVVYPW
SPLMVSISTF GPLVVLGGMG SALIGAWCAG PRGLAKTERN ATRAALGVML YFSCLLLGAA
VSAAALRRHL MVWKVFAPRL MLACAALLAV DVGVLLGVGV GLDRVLNKVR TVFRNVPGVA
DS
//
