ID A0A0M8ZUR4_9HYME Unreviewed; 819 AA.
AC A0A0M8ZUR4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
GN ORFNames=WN51_02421 {ECO:0000313|EMBL:KOX71550.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX71550.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX71550.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX71550.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX71550.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) 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; KQ435834; KOX71550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8ZUR4; -.
DR STRING; 166423.A0A0M8ZUR4; -.
DR OrthoDB; 5479199at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000053105; 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:UP000053105};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KOX71550.1};
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..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 555..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..636
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 698..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 745..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..810
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..591
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
SQ SEQUENCE 819 AA; 93790 MW; 4E1BACCCC6206ED3 CRC64;
MDKNIIMLSY IVFIGPLSIA LFLYGFFPLM YCDNTIATQG DIPKFIENTR VKIDTLYEPI
AKRLIVMIID ALRWDFIKGS VGKIAMPVTN SLIANSSAYL LQTKVQPPTV TMPRIKAITT
GMIPSFIDVA LNFGSKPVTG DSLLFQAKKA GYKSVFYGDD TWITLFPSIF DRYDGTTSFF
VTDFTEVDDN VTRHIHKELY NNNDWSIMIL HYLGLDHIGH VHGPFSPLIK TKLKEMDNVI
AKIQIKVQEW NQNNDSTVFI ICGDHGMKDS GGHGGSTVSE TTVPFVIIGT ENHQNYIKDP
IEISQIDIAS TLSVILGVPI PYSNIGTVFL DALYNLPISK KLFILYYNSK QVFNHFQKLV
GYESKYAYHK YLEAIKLHNA WLNTKDHPDD MTDDIVLSYK AALKGMKEIL ISSIIICILV
GETSFKSASL KGVAFFISLN VLLWLIVNCF WKYESTALLH TNPSEMGEWL LSFGTLIHAI
SFIGTSFVEE EHQTWYFYWS QALCFSHYQR NAQISIKLFL LLIGHRILRK LNSTGDKYAH
LPDIAGFLIR QESRLGMTIV LIAGLALLMW IDFIHENKTH KKLSLVLNFI ISICIYLRHM
HNNRVAKIPF YPPTRGIFEV QIFWFLLVMN LVKYIYELIC IRKRYSRFFP RVSLYFILQT
WIMIAAMLHQ PHNVILLPFQ IIFSSVIYEI IKNNTTQNIW VLLYIWIGNV FYFYQGNSNS
LATVDVAAGY VGVQSYMPFI NGSLLIINTY AAPLLSYFLL IYHAILQHPH NIQRHHLFVW
SVFSPKLLYE AVHSTVVCSA VFIMLILATV QKAINNCNR
//
