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Database: UniProt
Entry: E3LGD4_CAERE
LinkDB: E3LGD4_CAERE
Original site: E3LGD4_CAERE 
ID   E3LGD4_CAERE            Unreviewed;       786 AA.
AC   E3LGD4;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN   ORFNames=CRE_01547 {ECO:0000313|EMBL:EFO86364.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) 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}.
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DR   EMBL; DS268408; EFO86364.1; -; Genomic_DNA.
DR   RefSeq; XP_003117498.1; XM_003117450.1.
DR   AlphaFoldDB; E3LGD4; -.
DR   STRING; 31234.E3LGD4; -.
DR   EnsemblMetazoa; CRE01547.1; CRE01547.1; WBGene00053941.
DR   eggNOG; KOG2125; Eukaryota.
DR   HOGENOM; CLU_004770_2_0_1; -.
DR   InParanoid; E3LGD4; -.
DR   OMA; NWVYQFK; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000008281; 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; 2.
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; 2.
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:UP000008281};
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        417..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        446..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        469..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        544..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        585..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        616..638
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        650..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        696..718
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        739..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          421..514
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
FT   DOMAIN          671..779
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
FT   REGION          35..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   786 AA;  90242 MW;  32F99297E921F3DC CRC64;
     MKNLIKFLFQ TSRLLVVVAC ILLVYSFVAL EGRGKEDGET DGDDRKTNRR TTENEKEKKD
     RIPLQDLNFQ FPETPRLVFM VIDAFRLSFL TSPESPMTFT KSSIANNSAL LFDAYARMPT
     VTLPRITAYI TGTLPSFGTI LTNLATDEIK IDNWISRIHA LKKRIHFFGD DTWIRLLPGK
     FKKYDGVTSF YVNDYTEVDQ NVTRHLRKEF SGFRKWDVLI LHYLGLDHIG HSLGGNSPKI
     PEKLKEMDEV IVRIHEFLRN SSSDSRENYL IVCGDHGMTA AGSHGGASPE ETRVPVVMWK
     IGRQTNEKMV KNTEKPPKIE QIDVSATIFD LFGLEMPSES YGISLASWFR DENFEEENLK
     KQHEHFKNII EEKHLSISDI CDENCDYTDK FLQKSLKKWF KTVQEELIGT STEMPNISMF
     ISFALLLQVS ATVLSANAWF FRTPQLNLSI FLVNIMCFAS SLIEEEHEIW FYLGSTVVAI
     RAIRWLRNRE QKELKPIIAL AVLHRIAYGY MQSTRRRWSM DQSLLPESLF SEVFDRNVTD
     FNTFLKFDAI LVMIGSFIYW WIYIKKNHSL IFLPMLSQYL RYMEFAPIGI FNISAQIHIL
     IQLCVVPIGI ITGTMLFGFL PLILAIVPVS QVLLALFTYR IGHLSAKLQF GDVENLIFCM
     ASFFYFFCND NFQFQGNSNS LSTLSLTSAY VGLLDYYPIL VGAQLIVYTF AGPVLYMAGR
     TSFVSTKSPA TSHWLQLHFS FRISALATSL ICLYIFQNHL FVWSVYSPKV VYDIAHVIVF
     GVISAF
//
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