SMP3_CANGA
ID SMP3_CANGA Reviewed; 496 AA.
AC Q6FMA9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
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=CAGL0K09548g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380957; CAG61598.1; -; Genomic_DNA.
DR RefSeq; XP_448635.1; XM_448635.1.
DR AlphaFoldDB; Q6FMA9; -.
DR STRING; 5478.XP_448635.1; -.
DR CAZy; GT22; Glycosyltransferase Family 22.
DR EnsemblFungi; CAG61598; CAG61598; CAGL0K09548g.
DR GeneID; 2890237; -.
DR KEGG; cgr:CAGL0K09548g; -.
DR CGD; CAL0134813; CAGL0K09548g.
DR VEuPathDB; FungiDB:CAGL0K09548g; -.
DR eggNOG; KOG4123; Eukaryota.
DR HOGENOM; CLU_022957_2_0_1; -.
DR InParanoid; Q6FMA9; -.
DR OMA; GIMHQNG; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000002428; Chromosome K.
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:0000026; F:alpha-1,2-mannosyltransferase activity; IEA:EnsemblFungi.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006276; P:plasmid maintenance; IEA:EnsemblFungi.
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..496
FT /note="GPI mannosyltransferase 4"
FT /id="PRO_0000246275"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 496 AA; 57033 MW; EBF98F87E4E4DD77 CRC64;
MDNKLIWLLP AIGLVVALQP SYIHPDEHFQ TLEMLMIKFY GISGTVPWEF EPTNNARSYF
PLYAFYGPLF YLMRDILKVQ NPLNILRIIR FYNFMLYLSV LYYALPKLVN ENKLQNKGRV
NEALVFILSS YITWCYQCHS FSNSLETILL LLVLSNYTDI LSNKAGLLQL VSTGFLISVG
TFTRISFPAF LLLPSIQVFL KVLYRKWIQM VVIAVSMTLS TSIIVYFDTF MYESDEIIIA
PLKNVVYNLN VDNLAKHGLH PRYTHLLVNI PLILGPGLLM IRNTKNDFLN LPLLSIISSL
FFLSALRHQE LRFLLPVVPL FSTLLTRFRY RPYLFRIWLV FNAAMCIIMG IFHQGGVIPM
ISNINAEQDL TIDIWWKTYS PPTWLYNNDI LTVSTTSIVN NIENLDLVQF NVKTNHVVDL
KGCDFDLVLE AIQNFRINGV KSLRLIVPNS MTSNVAALNQ TYLVTKENSV FPHLDLDHLD
SGIQNIIGLS EYKVSL
