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Database: UniProt
Entry: A0A1X7VW15_AMPQE
LinkDB: A0A1X7VW15_AMPQE
Original site: A0A1X7VW15_AMPQE 
ID   A0A1X7VW15_AMPQE        Unreviewed;       861 AA.
AC   A0A1X7VW15;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=GPI ethanolamine phosphate transferase 3 {ECO:0000256|ARBA:ARBA00020841};
GN   Name=100633835 {ECO:0000313|EnsemblMetazoa:Aqu2.1.44303_001};
OS   Amphimedon queenslandica (Sponge).
OC   Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC   Haplosclerida; Niphatidae; Amphimedon.
OX   NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.44303_001, ECO:0000313|Proteomes:UP000007879};
RN   [1] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20686567; DOI=10.1038/nature09201;
RA   Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA   Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA   Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA   Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA   Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA   Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The Amphimedon queenslandica genome and the evolution of animal
RT   complexity.";
RL   Nature 466:720-726(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA   Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA   Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA   Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA   Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA   Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT   "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT   evolution of animal complexity.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.44303_001}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2017) to UniProtKB.
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   RefSeq; XP_019852954.1; XM_019997395.1.
DR   AlphaFoldDB; A0A1X7VW15; -.
DR   STRING; 400682.A0A1X7VW15; -.
DR   EnsemblMetazoa; Aqu2.1.44303_001; Aqu2.1.44303_001; Aqu2.1.44303.
DR   GeneID; 100633835; -.
DR   eggNOG; KOG2126; Eukaryota.
DR   InParanoid; A0A1X7VW15; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000007879; 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; IPR045687; PIGG/GPI7_C.
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   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:UP000007879};
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        432..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        465..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        603..620
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        626..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        656..678
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..703
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..738
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        758..782
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        803..822
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        842..860
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          686..847
FT                   /note="GPI ethanolamine phosphate transferase 2 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF19316"
SQ   SEQUENCE   861 AA;  98481 MW;  7B2C828DB5535BD6 CRC64;
     MRRTVLLHLS LITLLFLFQA LGIVLFLKGY LLTRVVIPQD SPVCFNCSPR YFQSVVWILV
     DALRHDFVLH NSSLGFKDDR PFYINQMRNI QHFLAHKPRH TKLYRFIADP PTTTMQRLKA
     LTTGTLPTFI DIGSNFNSYQ IQEDNIIRQS KRNGLKVTFL GDDTWMSMYP DMFYESYPFP
     SLNVKDLDTV DKGVYANIIP VLKRNDSDFI IGHFLGVDHC GHTYGPNNHI MRDKLIYIDD
     VIRSIFELVN NNTIVFVFGD HGMTSTGDHG GQTLLETEAA LVVYSKRPLF DAKQDYGQTV
     YQTDLVPTVS LLLGLPIPFS NLGMIIPELF IPVLEHISPY QSKMHLINSL RTNSQQLHAF
     IKAQNRFSND IPHHEVLKLQ NEYSILEKMY TSISSTNELS DFKTIENQYI NYMAKVREIC
     LSVWTKFDTN KMNAGVIVLI LHVILLLTIL FFMTKLSFSL ILAKVKLLDA VSVITVAFHS
     VSLFSNSFVV YEGKMVTFLM QSFMAALIVT KFREEVLQLI LNHRNLKWNV FIIQLYKNVE
     PCFKIMVCVH ISRYSHVCRD QQDDCTVLEF FSKPDAPFSS VYVLKLIKSV FQPFVFEKHA
     QKLIVYSLVV ALCGIFSEIL SVFMYWIYVA GVIILIFSMV KLSVNQYRKN EAKKNFSITL
     DSYSWILLLI WISVSFIVKG MNNMLLIPLS ISLIQFILLT QILSKMHTIS SLSRATLCSL
     LSYQFFFSFG HQATITSLHF DAAFVGVYGE MTPLKLPIAG LFVTINTLAS QVLSALVVPL
     LLPCQTWLKN GKVVLSTMHQ MQLICTLLGT VKLLCSVVAA FALRRHLMVW AVFGPRFMYE
     AAFQFIFIVT TVSSYLLVLL L
//
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