MCD4_SCHPO
ID MCD4_SCHPO Reviewed; 935 AA.
AC Q8WZK2; Q9US89;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
DE AltName: Full=Immunosuppresant and temperature-sensitive protein 8;
GN Name=its8; Synonyms=mcd4; ORFNames=SPBC839.08c;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 206-384, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-288.
RX PubMed=11297516; DOI=10.1074/jbc.m009260200;
RA Yada T., Sugiura R., Kita A., Itoh Y., Lu Y., Hong Y., Kinoshita T.,
RA Shuntoh H., Kuno T.;
RT "Its8, a fission yeast homolog of Mcd4 and Pig-n, is involved in GPI anchor
RT synthesis and shares an essential function with calcineurin in
RT cytokinesis.";
RL J. Biol. Chem. 276:13579-13586(2001).
CC -!- FUNCTION: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor.
CC {ECO:0000269|PubMed:11297516}.
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:11297516}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:11297516}.
CC -!- MISCELLANEOUS: Target of the inhibitor of GPI biosynthesis
CC YW3548/BE49385A.
CC -!- SIMILARITY: Belongs to the PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB46701.1; -; Genomic_DNA.
DR EMBL; AB027957; BAA87261.1; -; Genomic_DNA.
DR PIR; T40715; T40715.
DR RefSeq; NP_595248.1; NM_001021154.2.
DR AlphaFoldDB; Q8WZK2; -.
DR SMR; Q8WZK2; -.
DR BioGRID; 277713; 5.
DR STRING; 4896.SPBC839.08c.1; -.
DR MaxQB; Q8WZK2; -.
DR PaxDb; Q8WZK2; -.
DR PRIDE; Q8WZK2; -.
DR EnsemblFungi; SPBC839.08c.1; SPBC839.08c.1:pep; SPBC839.08c.
DR GeneID; 2541199; -.
DR KEGG; spo:SPBC839.08c; -.
DR PomBase; SPBC839.08c; its8.
DR VEuPathDB; FungiDB:SPBC839.08c; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q8WZK2; -.
DR OMA; TISHFCI; -.
DR PhylomeDB; Q8WZK2; -.
DR Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q8WZK2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:PomBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; ISO:PomBase.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:PomBase.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250; PTHR12250; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..935
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000024106"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..449
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 484..503
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..509
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 548..568
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..576
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 601..621
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..626
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 648..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 664..684
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..688
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..737
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..792
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..835
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 836..856
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 857..865
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 866..886
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 887..894
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 895..915
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 916..935
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 288
FT /note="P->S: In its8-1; confers sensitivity to calcineurin
FT inhibitor FK506."
FT /evidence="ECO:0000269|PubMed:11297516"
SQ SEQUENCE 935 AA; 106404 MW; A92DADCF1D932CE2 CRC64;
MFGRLLLLGI LFHVVFLKSI FDIYFVTPLI HGMKQYSAGE APAKRLFLIV GDGLRPDKLL
QPHSEKVIGE EQTYAAPFLR SIIQNNGTFG VSHTRVPTES RPGHVALIAG FYEDVSAVTK
GWKKNPVNFD SVFNQSRHTY SFGSEDILPM FSEGASDPSR VDTFMYSSEL EDFSSNGIVL
DEWVFDRLDE LLAQSLEDKE LWDMLHRDKI VFFLHLLGID TIGHNKHPDS VEYVENIQYI
DGKIQELVDK MNNYYNNDGA SSWVFTADHG MSDFGSHGDG NLDNTRTPII AWGAGIQSPT
HEKNYGHDEY SLPWNLTEIK RIDIQQADIA ALMSYLVGLN FPVNSVGQIP LDYLDCSSRR
KAEVALMNAL EIGEQYNLKS ASKDQTSIFF RPYSPLRNYT EVQASFYNSV IADIESGEYE
IAIEHCFHFS QTVLSGLRYL QRYDWLLLRS IVFFGYLSWI GYVICFVFSL NIEPSSKIVK
PVSVVKRVAF NIPFLLICIF FYIQSSPPFY YGYALFPTIF LQLIHSIFPN TKLGFKNFLT
VAKQKHGFSL LKILFISLCI LCLLQFIVYS YFHREGFSVI LMGLAAWPWL LHADYAFSHK
TISVSWSVLT SLLCFFTILP VNKKESLLFI FAGGFAMSVA GVFYILYRRN QAFQYSSTVT
NKQLVLQVLI IMATVPVTLK IADSLQRNIA IPPILRLVAF GLFITSYIIP SHHIRSCKHY
FLDRLAILFL TFSPTMCMLS ISFEALFYVV LFITLGLWME LETELQKYTE QLHPEYSRKK
DAKFHLSLSH IRISLFFYIF INVAFFGTGN VASLSTFALD SVKRFIPVFN PVTQGALLMY
TILVPFIALS AAFGIMNKRL GGIQQVTFFL AVGMADIVTI NFFYLVKDEG SWKDIGVSIS
HFCISNFLIL FITALEHASA ILCKNITYTI HEKVN
