ID   SMP3_YARLI              Reviewed;         510 AA.
AC   Q6CDD0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
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; OrderedLocusNames=YALI0C01485g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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: 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; CR382129; CAG81628.1; -; Genomic_DNA.
DR   RefSeq; XP_501332.1; XM_501332.1.
DR   AlphaFoldDB; Q6CDD0; -.
DR   STRING; 4952.CAG81628; -.
DR   CAZy; GT22; Glycosyltransferase Family 22.
DR   EnsemblFungi; CAG81628; CAG81628; YALI0_C01485g.
DR   GeneID; 2909128; -.
DR   KEGG; yli:YALI0C01485g; -.
DR   VEuPathDB; FungiDB:YALI0_C01485g; -.
DR   HOGENOM; CLU_022957_2_0_1; -.
DR   InParanoid; Q6CDD0; -.
DR   OMA; GIMHQNG; -.
DR   UniPathway; UPA00196; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
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..510
FT                   /note="GPI mannosyltransferase 4"
FT                   /id="PRO_0000246280"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   510 AA;  58174 MW;  1B0C470C14CD6373 CRC64;
     MIWNNRLILA LSLLLRLHLA ISPSYIHPDE HFQGPEYALG NLFDWAHETT WEFRGDSPIR
     SFVPLWILYT APLSVLNFLW KGQLSPREAY WFIRAGHALA YWILGDMALD RLSDSKKSKT
     KTLYLVGCSY VTWSYQSHTF SNSTETLLVL WCLVIIKESQ QRHSMHHQRV HKFMDAGLLG
     LLIVIGTWNR VTFPLWLIVP GLTYLRKYLI HNISSLILLI ASVALTAFFV IHVDSVHYDL
     EWTITPLNSF LYNSQGHNLA EHGIHNRLTH LVSNLPVLLG PLLILLRTPS QYWKSLQFQS
     AISGVFFLSL FPHQEARFLM PAVPLLISCY DINAVPRRFT SAIFLLSYVF NIIMGFLMGT
     LHQGGVVPAQ HYLSKHVDSG SHTVVYWRTY KPPSWLLGIP EGELEILDKD HPLGTNLFKR
     VTDEIENIQI RHKKTMVTVL DLMGSSPEYV NDVIAALAPI NPLLVAPVAG LKELDLPAYK
     EVWKTRFHLG LDHIDGLESL EPGLVVLEVL