ID A0A0V0ZEC1_9BILA Unreviewed; 804 AA.
AC A0A0V0ZEC1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=GPI ethanolamine phosphate transferase 2 {ECO:0000256|ARBA:ARBA00020830};
DE Flags: Fragment;
GN Name=las21 {ECO:0000313|EMBL:KRY10643.1};
GN ORFNames=T12_13588 {ECO:0000313|EMBL:KRY10643.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY10643.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY10643.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY10643.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-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}.
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:KRY10643.1}.
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DR EMBL; JYDQ01000222; KRY10643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZEC1; -.
DR STRING; 990121.A0A0V0ZEC1; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000054783; 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; 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:UP000054783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY10643.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 463..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 488..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 544..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..692
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 745..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 633..787
FT /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19316"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY10643.1"
SQ SEQUENCE 804 AA; 91132 MW; FAFEBAA0855F0954 CRC64;
LAVICLVPFD FRRGHISVRC GYTMKLAVCF RISCIIALIS LAAFMLEFLK VRFDGTRESV
NDFEKDHICE KISVNKISDP AVDKVVLIVV DAFREEFFKS QPKSFPFITS MMKQNGGLSY
TAKVHMPTVT LPRIKTLISG SIPSYIDLLY NIGSTEYKFD KDNIIARLKA AGNNVVFYGD
ETWIRLFPRS FLRSDGTTSL IVGDFKEVDN NVSRWIDFEM ANDDWSLMIL HYLGLDHIGH
SLGDKSPLIP VKLEEMDLIA KKIYKALNQK SSNFLIVITA DHGMSDGGSH GDASDLEIHV
PLLFLSPKLS AQSISKVVRQ VDLASTLAIL FKLPIPTSSV GFLLPELIDQ LMPTKNDICL
AYLLNLCQLQ TVSQAQFQKN ISDAITSGAK ECHADSRGYP LEDCNERMRK NLLGLYHNIR
QRSQQSDSSF NLFSMVLPIF GMLGSVFLLC ICIFGIQCIQ PKSSLVLAFL LAQSVSLASS
SYIENELYVW KYSFVFVVAF DLFVDAIKRR MVFTVIYIAI LLTLNRGIEH MVNDAKHAQV
EKYFGVWPCF TSITMQMSLP ALCAGLLILR MKLYYSHLFN RRILIIFGFI CTAFHRLFVT
FGYLNYTPVH IVYGMCMSFL LLEGSASSVA ICLLLMACVL LNVTYISVYI LLLLEEVMLS
VTLNMMNRPT DFRIVLYHIF ARYSFFALGN MNTLSTLNVS AAFTGVKNYF PIINGTLLLV
HTFLGPATMW SWFYRALNKS QRMYALPIIV WLHVVPLLFY LTVVTYLRHH LFIWSVFAPK
LFYLAIENTI CLVLSMVVSY SVYP
//
