ID A0A176VV59_MARPO Unreviewed; 869 AA.
AC A0A176VV59;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN ORFNames=AXG93_1052s1260 {ECO:0000313|EMBL:OAE24303.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24303.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE24303.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24303.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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. PIGG subfamily.
CC {ECO:0000256|ARBA:ARBA00005315}.
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:OAE24303.1}.
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DR EMBL; LVLJ01002657; OAE24303.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176VV59; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000077202; 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; cd16024; GPI_EPT_2; 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; IPR037674; PIG-G_N.
DR InterPro; IPR039527; PIGG/GPI7.
DR InterPro; IPR045687; PIGG/GPI7_C.
DR PANTHER; PTHR23072:SF0; GPI ETHANOLAMINE PHOSPHATE TRANSFERASE 2; 1.
DR PANTHER; PTHR23072; PHOSPHATIDYLINOSITOL GLYCAN-RELATED; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 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:UP000077202};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 657..836
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 869 AA; 96293 MW; 2B4A129276ABC8E4 CRC64;
MASLFRRLVT LGVVALLLQM IGLLLFVLGF FPVKPALDGM SGAESFLPFC KVDDINELDR
PLHDEQYDFQ ERNLDLPAKY DRLVFMVYQV VDGLPAEFVL GRDGRPPARN FKSAMPFTQN
LLSNGSALGY HAKAAPPTVT MPRLKALNSS QAMTSGAIAG FLDVAYNFNT QKLLGDNLIG
QLARAGWRMV MLGDETWLKL FPNLFERHDG VSSFYVKDTV EVDNNVTRHL DYELENTDWD
LLILHYLGLD HVGHLGGRSS PLMDSKLREM DSVIERIHQT VLSKSPLSSR TLLVVVSDHG
MTDGGNHGGA TYQETDALAL FITNPSTKPD LQVSPEASGS TFLQDAAYQV DLVPTLAILL
GMPIPKNSVG ALLQPLFSSL PRRSNWVMFL CLLLVFEMSS AAELQLKALE LNSWQLLRLL
RRRSPHSVCI ADICQNQKTT DGDRSSPPSK QGDNVLRYCT LFNLAEEKRK QWSENGKEAS
GFEETKEAYL QFIRPTSEWL ASGSTEKRLT FVFSGGLLML LSTVLFLLAV YQIHKATFED
HSSKCEVLRV GTSRVLILIA VGGVSVHAAS FGSSSFVEEE QFTWHFMLST LLVALVRASL
QQFKFESDDA ADAISDPKDL MSENSDTLLA DCRVKRKHNP AIGTTADQSR LLLLVTRRKL
ITNQQSVNAV PIALLLFQLL MAVNLFHTAH AWAPRWISVL TLHWLGASAH FGLGNSNTLA
TVDVAGAYIG LSSHSTVLSG ILAFFITYGS PLLYMQGLLL SINRPRALQE KKISEFSQAW
LLEDIILPCI LPLAMNSIIL TSFTGVLYIM QDHLFVWSVF SPKYLYVVAT TVCTYTGTLL
FVAVGGYSIF VTSFRIQQMD GVGVAKRKV
//
