GPI7_YARLI
ID GPI7_YARLI Reviewed; 860 AA.
AC Q6C7Q6; Q96X26;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=YALI0D26235g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 20460 / W29;
RX PubMed=11325938; DOI=10.1128/jb.183.10.3098-3107.2001;
RA Richard M., Quijano R.R., Bezzate S., Bordon-Pallier F., Gaillardin C.;
RT "Tagging morphogenetic genes by insertional mutagenesis in the yeast
RT Yarrowia lipolytica.";
RL J. Bacteriol. 183:3098-3107(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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 -!- DISRUPTION PHENOTYPE: Defects in hyphal formation.
CC {ECO:0000269|PubMed:11325938}.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
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DR EMBL; AF321466; AAK52677.1; -; Genomic_DNA.
DR EMBL; CR382130; CAG81512.1; -; Genomic_DNA.
DR RefSeq; XP_503306.1; XM_503306.1.
DR AlphaFoldDB; Q6C7Q6; -.
DR SMR; Q6C7Q6; -.
DR STRING; 4952.CAG81512; -.
DR EnsemblFungi; CAG81512; CAG81512; YALI0_D26235g.
DR GeneID; 2911071; -.
DR KEGG; yli:YALI0D26235g; -.
DR VEuPathDB; FungiDB:YALI0_D26235g; -.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q6C7Q6; -.
DR OMA; HIGHKTG; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000001300; Chromosome D.
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..860
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246197"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..506
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..575
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..854
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 525..527
FT /note="HPV -> QPS (in Ref. 1; AAK52677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 860 AA; 96503 MW; 46949D1997F18343 CRC64;
MLWKRWTLAV TIVVLQLAAV LLFARGFLPS RVLLPGYTES RVSTEAPFQK AIIMVVDAFR
SDFAFSDQSN CPQLHKRINS GGAIPFTAHS TPPTVTLPRI KGLTTGSTPN FLDAVLNIAE
SDNSSTLANQ DSWLAQASRD GRKIHMFGDD TWIKLFPGMF DDCEGTASFF VSDYTEVDNN
VTRHIDTQLD QKTEWDVLIL HYLGLDHIGH KTGPESPFMP AKQKEMDDIF DKLYNSCDDD
TVLILLGDHG MNEVGNHGGS SAGETSAAMV FASPKFETAQ LTETAETSPL PWTDTYKYHS
RMDQTDLVPT LTALLGLNTP KNNLGVLVSQ MLGLWSPEDQ LNVLKNNADQ MVQILQGQAS
RESDAKEVYE LYDTLNSNPS VKDYYNFLYE AQSYLTHASS NYNTNDMLGG IGLGLLSTIL
ALTVFSALTL AVQGLKRLYL IILLVYFISV FGSSTVEEEH QIWYWITSGW MAFLYISGSR
NKFGDGFNWM FVQVFVRMMI SWNQTGQKFT KKDDIVTWLS KDGNHPVLWI LILVTYGVAF
NKVWRYGFSK VESKLAFLLT LITTFASVGF KITQAWEAGE VVPAPLLYLM GLPGTLNEVN
ARMAGLARFA FSTIAAGSLY RVLSLAGTDK VNLIRDLHAF LTLFLITQSR IQNIPLFMVY
YFLEIFLRKA TNRSFIFSSR DIYQTEALFQ KLVLVLSVST LLLEQVSFFS MGNSNSMASI
DLSNAYNGVT LYQIEFVGVL TFVSNWIGPL YWSTAGLSFL LEDHVRNAIF AKIAEKNNDV
KLTTKLVQQA LTLRVYVVLA FSSVAISAVM ITCFFLREHL FIWTVFSPKL LYQFVWTVLQ
FALVDVILSS IFVVLVYRSV
