GPI7_KLULA
ID GPI7_KLULA Reviewed; 787 AA.
AC Q6CLN2;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=KLLA0F01705g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382126; CAG97864.1; -; Genomic_DNA.
DR RefSeq; XP_455157.1; XM_455157.1.
DR AlphaFoldDB; Q6CLN2; -.
DR SMR; Q6CLN2; -.
DR STRING; 28985.XP_455157.1; -.
DR PRIDE; Q6CLN2; -.
DR EnsemblFungi; CAG97864; CAG97864; KLLA0_F01705g.
DR GeneID; 2895006; -.
DR KEGG; kla:KLLA0_F01705g; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q6CLN2; -.
DR OMA; HIGHKTG; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IEA:EnsemblFungi.
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; -; 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..787
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246196"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 617
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 787 AA; 88974 MW; 887073AA5FCAC596 CRC64;
MGRKLYYVLA TLQLVAVFLF CGGFFPQKVV LKNDSKFIVN PEVQLASKPV FKKLVLVVID
ALRSDFLFQK DSSDFEFLHG LLNSGEAWGY TAYSNPPTVT LPRLKGITTG SAPNFLDAIL
NVAEDDTSSN LKEQDSLLKQ FHTHHYKMNF FGDDTWLKLF PLEFFSEYDG TNSFFVSDFE
EVDFNVTRHV PYQMEHQKNW DVLILHYLGL DHIGHKGGSK SHFMPSKHRE MDSVIKQIYE
KIDGDTLMVV LGDHGMNDLG NHGGSSSGET SAALAFLSKR LKKYQSSDIQ QSSNVPVEDA
HPDYKYLKEV EQIDIVPTLS MLFNLPIPKN SMGVIIDELL QLLPSKLAAI KVQDNYLQLT
KLKPGYEAQL EKKSAGTLLE EMREIQSSLA MAATNYNYTF LTYGTTLMII GTLIVTVWNF
QLSQEYIEHV GTSVLLGISM FASSFIEEEH QIWWWITISV LLLMQISNGK KLVVLSGLRL
IRGWNNSGQK YIYDNVLHTL LKSHTSVLWW LNVVTFLSVG FPFLRNKDES EKMVSLLSVS
FLALSSITYK ICFAIVNGDK VPSGLYTFAL RSCAMYLANE NATESDISQC LVPIARIFFQ
ICGVSIIILL FMKYALNKST NMLNKLLSVI KFVLLLQTSS ANIPLFLIFE ILTSVTPDIT
PIFSLCLQNL TFFQFGGTNS IATVNLTNAY NGVSSNYNIY VVGVLMFLSN YAPSIYWALS
LIPQSYKQKT LRLQHYYITG TCLMIACIAL RYHLFIWSVF SPKLCYYAAW SLYNVVMDFA
ITLLGVL
