ID   GPI7_CANAL              Reviewed;         885 AA.
AC   Q8TGB2; A0A1D8PDH8; Q59LX3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 3.
DT   27-MAR-2024, entry version 98.
DE   RecName: Full=GPI ethanolamine phosphate transferase 2;
DE            EC=2.-.-.-;
DE   AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
GN   Name=GPI7; Synonyms=LAS21; OrderedLocusNames=CAALFM_C105070CA;
GN   ORFNames=CaO19.11547, CaO19.4064;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=11994163; DOI=10.1046/j.1365-2958.2002.02926.x;
RA   Richard M., Ibata-Ombetta S., Dromer F., Bordon-Pallier F., Jouault T.,
RA   Gaillardin C.;
RT   "Complete glycosylphosphatidylinositol anchors are required in Candida
RT   albicans for full morphogenesis, virulence and resistance to macrophages.";
RL   Mol. Microbiol. 44:841-853(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12101300; DOI=10.1099/00221287-148-7-2125;
RA   Richard M., De Groot P., Courtin O., Poulain D., Klis F., Gaillardin C.;
RT   "GPI7 affects cell-wall protein anchorage in Saccharomyces cerevisiae and
RT   Candida albicans.";
RL   Microbiology 148:2125-2133(2002).
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: Cell-wall protein anchorage defects.
CC       {ECO:0000269|PubMed:12101300}.
CC   -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF348498; AAL83897.1; -; Genomic_DNA.
DR   EMBL; CP017623; AOW26178.1; -; Genomic_DNA.
DR   RefSeq; XP_710733.2; XM_705641.2.
DR   AlphaFoldDB; Q8TGB2; -.
DR   SMR; Q8TGB2; -.
DR   STRING; 237561.Q8TGB2; -.
DR   GlyCosmos; Q8TGB2; 5 sites, No reported glycans.
DR   EnsemblFungi; C1_05070C_A-T; C1_05070C_A-T-p1; C1_05070C_A.
DR   GeneID; 3647672; -.
DR   KEGG; cal:CAALFM_C105070CA; -.
DR   CGD; CAL0000200443; GPI7.
DR   VEuPathDB; FungiDB:C1_05070C_A; -.
DR   eggNOG; KOG2125; Eukaryota.
DR   HOGENOM; CLU_004770_3_0_1; -.
DR   InParanoid; Q8TGB2; -.
DR   OrthoDB; 5479199at2759; -.
DR   UniPathway; UPA00196; -.
DR   PHI-base; PHI:259; -.
DR   PRO; PR:Q8TGB2; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR   GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR   GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR   GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006505; P:GPI anchor metabolic process; IMP:CGD.
DR   CDD; cd16024; GPI_EPT_2; 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; 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; Glycoprotein; GPI-anchor biosynthesis; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..885
FT                   /note="GPI ethanolamine phosphate transferase 2"
FT                   /id="PRO_0000246193"
FT   TRANSMEM        413..433
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        581..601
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        648..668
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        697..717
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        726..746
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        768..788
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        820..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        865..885
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        82
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        443
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        516
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CONFLICT        54
FT                   /note="Q -> H (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        57
FT                   /note="N -> T (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        94
FT                   /note="R -> H (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="K -> E (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        376
FT                   /note="S -> T (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="A -> V (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        877..885
FT                   /note="ILAVIVLLF -> YFGNNSIVVLKTNILL (in Ref. 1; AAL83897)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   885 AA;  100727 MW;  1ED8089BF74EA234 CRC64;
     MSGSLNSRWV VQVSLTIINI IGFLVFLRGF FPSKVVLPGF NSFQDSTKSP FSDQYGNPQF
     NKFILMVVDA MRSDFCFSDR SNFSFLHQLI NQGRALPFTA FSNPPTVTLP RLKGITTGGT
     PNFLDAILNV ADDQDDSQGL HNQDSWVHQF RHSNNKTINF FGDDTWLKLF QDQFTEFEGT
     NSFFVSDFTE VDNNVTRHLD DQLSSNKWDG LILHYLGLDH IGHKGGPESP YMKPKQIEMD
     KILQRLYTYV TKNDDTLIVL MGDHGMNEIG NHGGSSPGET SAALSFISPK FNHKGESPLP
     YNSDYSYHHK ISQIDLVPTL AALLNFPIPK NSLGVIAKEI LEIWPENQRI KILLENCAQI
     MNLYEAKYGP SGKVWSQWEN LQAKQHPIAD YYEFLQDIQS EMASSATNYG YKDIYAGALI
     LVITALAVIV VFNRYFLTAS NMNISSVMFY ELFVVLYSLH FHGSSLIEEE HQIWYFFTTA
     TLLFLAITFF DTFKSLQNFI SFGVLFACIR FMRSWNNSGQ KYSSQYNIAY YLSHSNPNLM
     WGLIILTYFV LTLCIYIQGS LVPTFAFSFG KRLPDVKDPG GLISFIVVFV ATSVSFSFKL
     LQYYIDGNTI PKWLNRFLLW IIESHHIDLS SATLEDNELK FQLQSVSIQL SKFTTIILLL
     LVISRVIIGK IRKIRYGTIT DITNIMTIYL IHQTRHENIP IFLALMFAKF ALSKLIYRKT
     NRIDQYILTV TMTVLCLQNL TFFCMGNTNS LATVDLSNAY NGVKAYNVFL VGLLTFVSNF
     AGPIFWSLSG LQLLYEPSLL NFNGPATTDL LHYTGLKKSI LLVKSLISLF FYTVSAVNLV
     GSCINLRFHL FIWTVFSPKL LFFGSWILFV NVLIDLILAV IVLLF
//