SMP3_SCHPO
ID SMP3_SCHPO Reviewed; 533 AA.
AC Q09837;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=GPI mannosyltransferase 4;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase IV;
DE Short=GPI-MT-IV;
GN Name=smp3; ORFNames=SPAC4G8.12c;
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: Alpha-1,2-mannosyltransferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth
CC mannose to trimannosyl-GPIs during GPI precursor assembly. The presence
CC of a fourth mannose in GPI is essential in fungi (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 glycosyltransferase 22 family. PIGZ
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA91213.1; -; Genomic_DNA.
DR PIR; T38857; S62489.
DR RefSeq; NP_593072.1; NM_001018470.2.
DR AlphaFoldDB; Q09837; -.
DR STRING; 4896.SPAC4G8.12c.1; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR MaxQB; Q09837; -.
DR PaxDb; Q09837; -.
DR EnsemblFungi; SPAC4G8.12c.1; SPAC4G8.12c.1:pep; SPAC4G8.12c.
DR GeneID; 2542832; -.
DR KEGG; spo:SPAC4G8.12c; -.
DR PomBase; SPAC4G8.12c; smp3.
DR VEuPathDB; FungiDB:SPAC4G8.12c; -.
DR eggNOG; KOG4123; Eukaryota.
DR HOGENOM; CLU_022957_2_0_1; -.
DR InParanoid; Q09837; -.
DR OMA; GIMHQNG; -.
DR PhylomeDB; Q09837; -.
DR Reactome; R-SPO-162710; Synthesis of glycosylphosphatidylinositol (GPI).
DR UniPathway; UPA00196; -.
DR PRO; PR:Q09837; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISS:PomBase.
DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; ISS:PomBase.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; ISS:PomBase.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..533
FT /note="GPI mannosyltransferase 4"
FT /id="PRO_0000215790"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 533 AA; 62201 MW; F14519C995884687 CRC64;
MFKNRKYAII YTFLLILRFW FSQGSSYIHP DEHLQSFQIF ANKLFGWKVE LPWEFTTKKP
IRSVVPLNVM LLPIFLLCRC ICKSNCSPYP ILLFTRLYMC LISLLIDLSI WNIVPLNARW
SALLLYSSSF MATTFQTHTF TNSIETIFFF LTILFLSKLN SVPLNKKISY LYTFLLAIVS
VLGFFTRITF LAFVIAPYIY FSVRCFKKNV NNPKDIFLHL CIFVSVSFAT VLACILEDYK
FYGVFVITFW NNLKYNSQIE NLSQHGLHSR LTHFFTNMPL LCGPLIFVPK LWDVRKPATW
LWLLPVFILS LFPHQEPRFL LPAASIFIVN SGCLVRSYWI KFLFVMYAVV LAVFFGIMHQ
NGVIPAVLEV KNIIEQRNVT TMENCNLYFN PEMPTTIYFW KIYSAPTWML ARPKFSQINT
SHLYNYSTKQ MISKFWETYY EEVKVVNLPE ENTTEFQAST LLVCPVAMLQ TSSYLQNLTM
LHYIPYHVDL DDTDELPLAE LIMNHGIGIF TAKEICENNT ITNELPTVLR SVG
