GPI7_ASHGO
ID GPI7_ASHGO Reviewed; 806 AA.
AC Q758B8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=GPI ethanolamine phosphate transferase 2;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
GN Name=LAS21; Synonyms=GPI7; OrderedLocusNames=AEL166C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 544.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the GPI second mannose (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
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DR EMBL; AE016818; AAS52519.2; -; Genomic_DNA.
DR RefSeq; NP_984695.2; NM_210048.2.
DR AlphaFoldDB; Q758B8; -.
DR SMR; Q758B8; -.
DR STRING; 33169.AAS52519; -.
DR EnsemblFungi; AAS52519; AAS52519; AGOS_AEL166C.
DR GeneID; 4620880; -.
DR KEGG; ago:AGOS_AEL166C; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q758B8; -.
DR OMA; HIGHKTG; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000591; Chromosome V.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR CDD; cd16024; GPI_EPT_2; 1.
DR Gene3D; 3.40.720.10; -; 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; PTHR23072; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF19316; PIGO_PIGG; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..806
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246186"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..804
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 806 AA; 90435 MW; E9ED4FCF477FC580 CRC64;
MRFKEVGLLF CQLLAVLIFA AGFFPQKKVL KGDAQFQYMA ETQRALEPAF DKLVLVVIDA
LRADFLFQQN VSHFDFVHEL LNRGEAWGFT AYSNPPTVTL PRLKGITTGS APNFLDAILN
VAEDDSSSNL KDQDSWISQF AKHGKKIHFF GDDTWLKLFP EEFFQKHDGT NSFFVSDFEE
VDTNVTRHLP HELQHKDWDV LILHYLGLDH IGHKGGAASQ FMPPKHREMD AVIRQIYDQV
DNRTLLCVMG DHGMNDLGNH GGSSAGETSA GMVFISKMLS SYPRPAAQDG VSSPVTAAED
YQFFTRIQQV DFVPTIASLF NIPIPKNSLG VFVREFSSLL GQHATTKIIE NYHQLMQLAA
KKTAARGNDD IDSMLAEMKD VQATLARTAT NYNYAMLFLG VGMLSIVTAA TAYCYISSAR
LNEASVLMIA VTALLGSSVF GSSFVEEEHQ IWWWIIIAVV GYSWATRPSC TPSHLVFLVC
ARLLRGWNNS GQKFMYDFTV AELLKSHPSI KWLLVCATLA VVALDGFTER PLLSIFNLLA
GLLCFVYKTC WANVNGEVSP TYAQTLVTKA CSLLFAGGTP WDDKQLLVPL ARLFFKVTAA
IVCMRIAYNV VFAKRKFLSE LFPLFTIVLI MQTASQNIPL FLVFTIMRSS LRNILRVGYP
QQRCEMFFVL SLILQNLSFF QFGGTNSIAT IDLTNSYNGI SENYNIYVVG LLMCIGNMAP
AIYWSLAAVV DHQLYSKKSY AQQKLSSMFF YSVNSLLLLV ACICMRYHLF IWSVFSPKLC
YLLGWNILIH FLTETVLEPF LLMVAG
