GPI7_SCHPO
ID GPI7_SCHPO Reviewed; 758 AA.
AC Q09782;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=GPI ethanolamine phosphate transferase 2;
DE EC=2.-.-.-;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 7;
GN Name=las21; Synonyms=gpi7; ORFNames=SPAC13G6.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(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 -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGG subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAA91096.1; -; Genomic_DNA.
DR PIR; S62432; S62432.
DR RefSeq; NP_592829.1; NM_001018230.2.
DR AlphaFoldDB; Q09782; -.
DR SMR; Q09782; -.
DR BioGRID; 279281; 1.
DR STRING; 4896.SPAC13G6.03.1; -.
DR MaxQB; Q09782; -.
DR PaxDb; Q09782; -.
DR EnsemblFungi; SPAC13G6.03.1; SPAC13G6.03.1:pep; SPAC13G6.03.
DR GeneID; 2542835; -.
DR KEGG; spo:SPAC13G6.03; -.
DR PomBase; SPAC13G6.03; -.
DR VEuPathDB; FungiDB:SPAC13G6.03; -.
DR eggNOG; KOG2125; Eukaryota.
DR HOGENOM; CLU_004770_0_0_1; -.
DR InParanoid; Q09782; -.
DR OMA; HIGHKTG; -.
DR PhylomeDB; Q09782; -.
DR Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q09782; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:PomBase.
DR GO; GO:0051267; F:CP2 mannose-ethanolamine phosphotransferase activity; ISO:PomBase.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISO:PomBase.
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; 2.
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..758
FT /note="GPI ethanolamine phosphate transferase 2"
FT /id="PRO_0000116402"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 561..581
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 758 AA; 85646 MW; F0FE169B570ACC57 CRC64;
MRFAFFGIFW LQIFGSILFL LGFFPHKNDS TGKAMSNQFS PPAVIDQVVF VMVDALRADF
VFSKSHNMPF TQSLLYNSTH GIGFSAFARS PTVTMPRLKA LTTGTIPGFL DVLLNIAESD
TGSSIEAQDS WVYQLNSFNK KIEFYGDDTW LKLFPSAFSK FEGTTSFFVS DYTEVDNNVT
RNFDHALPSS LSHSWDALIL HYLGVDHIGH LYGPSSPLLN IKLLEIDTII SRIYKYLQEY
DEKTNTHSLI VLCGDHGMNE VGNHGGSSSG ETTAALSLLF PSNELSHINK PILNMDDNPY
SILERVEQVD VVPTICLLLG IPIPKGNMGK VLSPVTELWK DTKTAKMAAL SNLFQLSLLK
NPSLTTSELS TQFQDSDLND IRLALENLQS QMVAQSSSYS LDRMLVAISI LGACSILSLI
LFRNLYNYKE LLAFAPFVVQ NIIIVFSSSF IEEEHVIWYF AAVSLSLLQL LNPKTRLAGS
LQLFCLSIIK RWNQTGQKYS DLRDIVDDFI APSTFMKTIL CVTSAFMPAI RSPSPINFLS
SMFIAFYKLM PIISKHLNEL PIIASFDYTF FVRIIWSLLL ISFLSKPTFK QLRCQLSLFI
LLLTRLENMG LYLLYDIWQR TMPEEGTLAS VMYYVAEQVA FFSLGNSNSL ATVDLSQAYT
GLDSYNIFAV GILLFTSVFA GALWWCLHQP KRMMDRSVKT FWIMSSISLT FLCISCFIMR
HHLFVWSVFS PKLLYNASWA SMYFLAKCLI STIMVRLR
