GPI7_DEBHA
ID GPI7_DEBHA Reviewed; 877 AA.
AC Q6BZ57;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 25-MAY-2022, entry version 87.
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=DEHA2A04378g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84467.2; -; Genomic_DNA.
DR RefSeq; XP_456512.2; XM_456512.1.
DR AlphaFoldDB; Q6BZ57; -.
DR SMR; Q6BZ57; -.
DR STRING; 4959.XP_456512.2; -.
DR EnsemblFungi; CAG84467; CAG84467; DEHA2A04378g.
DR GeneID; 2899847; -.
DR KEGG; dha:DEHA2A04378g; -.
DR VEuPathDB; FungiDB:DEHA2A04378g; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q6BZ57; -.
DR OMA; HIGHKTG; -.
DR OrthoDB; 848878at2759; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000000599; Chromosome A.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IEA:InterPro.
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..877
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000246195"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 634..654
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 758..778
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 877 AA; 100433 MW; 8E4376F4E643BB29 CRC64;
MGSSKWGVLF GLLILHVIGY SIFLKGFFPS KVVVPGFNEF HTGQSPFMEH NEAKFDKLIL
MVVDAMRSDF LYSDHSHMKF VHQLINENCA LPFTSYSNPP TVTLPRLKGI TTGGTPSFLD
AILNIADDKD NSQSLLNQDS WLHQFQNNSK VFNFFGDDTW LKLFPPEKFF NQYEGTNSFF
VNDFTDVDNN VTRHLNDDLF NSKWDALILH YLGLDHIGHK GGPNSIFMRG KQEEMDGIIE
KLYKETIDSN TLLVVMGDHG MNEIGNHGGS SMGETNPGLL FASPKFKMLK KNLKSPLAYN
NDYKYYNYIN QIDLVPTLAT LLNFPIPKNN LGIVIKDILG LWKPEAQKSI LMENSEQFMN
IYEAKHANDT DIINEWKKSQ DSGSIDVHYD FLSKIQGLLT SAATEYKYVD IYIGLSILVA
MAIVAFGLFN WYFLVQATIN PKYNWYFIGI SIVYSIHFHA SSLIEEEYQI WWFFSIICLF
ALYFNNHLKS LKYFWLILVG LRIIRSWSIT GQKFTTPYTF SAYLLQNVDL LWVLNIATYF
LTAILIYSQG SLIHCVTLRE YESLRENVKD FGSLVTFIVT FVTCSISFSF KLCQYFNDGK
RVPDWLLAFL NWTCESYGIT IDPKEKNQLH ELNIHLSKIL FYCIGVLIIV RIVLGKIRKL
HYGLLTDLSN VLTLFLLHQS RPEIVPIFLI FSLVKFSAAK LLANNEIVLR KNIDQLMIII
TLFSLCMQNL SFFSMGNTNS LATVDLSNSY NGFKSYDVFL VGVLTYCSNF AGPIFWSLAS
LQLIFENNVV CFDTKKSSKD LVNLKFLKYQ ILYVKSLAGF LFYSMAGLSL VASCFNLRFH
LFIWSVFSPK LLFFASWTLL TNILIDTISS LSILALC
