GPI7_CANAL
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 25-MAY-2022, entry version 92.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 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; 848878at2759; -.
DR UniPathway; UPA00196; -.
DR PHI-base; PHI:259; -.
DR PRO; PR:Q8TGB2; -.
DR Proteomes; UP000000559; Chromosome 1.
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..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
