ID SMP3_CANAL Reviewed; 498 AA. AC Q5A0L9; A0A1D8PGU9; DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2017, sequence version 2. DT 27-MAR-2024, entry version 96. DE RecName: Full=GPI mannosyltransferase 4; DE EC=2.4.1.-; DE AltName: Full=CaSMP3; DE AltName: Full=GPI mannosyltransferase IV; DE Short=GPI-MT-IV; GN Name=SMP3; OrderedLocusNames=CAALFM_C203070CA; GN ORFNames=CaO19.13214, CaO19.5792; OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida. OX NCBI_TaxID=237561; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=15123810; DOI=10.1073/pnas.0401648101; RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., RA Scherer S.; RT "The diploid genome sequence of Candida albicans."; RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004). RN [2] RP GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52; RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D., RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M., RA Chibana H., Nantel A., Magee P.T.; RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned RT on the eight chromosomes."; RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=SC5314 / ATCC MYA-2876; RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97; RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.; RT "Assembly of a phased diploid Candida albicans genome facilitates allele- RT specific measurements and provides a simple model for repeat and indel RT structure."; RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013). RN [4] RP IDENTIFICATION. RX PubMed=15470093; DOI=10.1099/mic.0.27254-0; RA Grimme S.J., Colussi P.A., Taron C.H., Orlean P.; RT "Deficiencies in the essential Smp3 mannosyltransferase block RT glycosylphosphatidylinositol assembly and lead to defects in growth and RT cell wall biogenesis in Candida albicans."; RL Microbiology 150:3115-3128(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 -!- MISCELLANEOUS: May be used as a target for the development of some new CC fungicide, due the fact the presence of a fourth mannose in GPI-anchor CC proteins is essential for viability in fungi but not in mammals. CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP017624; AOW27344.1; -; Genomic_DNA. DR RefSeq; XP_715333.2; XM_710240.2. DR AlphaFoldDB; Q5A0L9; -. DR STRING; 237561.Q5A0L9; -. DR GlyCosmos; Q5A0L9; 4 sites, No reported glycans. DR EnsemblFungi; C2_03070C_A-T; C2_03070C_A-T-p1; C2_03070C_A. DR GeneID; 3642980; -. DR KEGG; cal:CAALFM_C203070CA; -. DR CGD; CAL0000175734; SMP3. DR VEuPathDB; FungiDB:C2_03070C_A; -. DR HOGENOM; CLU_022957_2_0_1; -. DR InParanoid; Q5A0L9; -. DR OrthoDB; 7417at2759; -. DR UniPathway; UPA00196; -. DR PRO; PR:Q5A0L9; -. DR Proteomes; UP000000559; Chromosome 2. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central. DR GO; GO:0000026; F:alpha-1,2-mannosyltransferase activity; IMP:CGD. DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IMP:CGD. DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:CGD. DR InterPro; IPR005599; GPI_mannosylTrfase. DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1. DR PANTHER; PTHR22760:SF3; GPI MANNOSYLTRANSFERASE 4; 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..498 FT /note="GPI mannosyltransferase 4" FT /id="PRO_0000246274" FT TRANSMEM 11..31 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 63..83 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 96..116 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 140..160 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 222..242 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 247..267 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 282..302 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 310..330 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 332..348 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 350..370 FT /note="Helical" FT /evidence="ECO:0000255" FT CARBOHYD 47 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 84 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 408 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 473 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 498 AA; 57971 MW; 98A3C4952410BCE5 CRC64; MIKINFNWRT FYLLTIVFRF VFTLSDSYIH PDEHFQSLEV LTNRILNYST NIPWEFQDDP ARSLAPLYFI YGPLLYFIKF FKLNLTALQI WYIARLQISI LSWIITDFCL YWMLPSKPER IKAIFFTSTS YITLVYQNHL FSNSIETLLL LVTILLIDDL RYVQESKDQD VQNLNKNKNL FYTGVLISLG IFNRITFPAF LILPGWFVMK YVLKHYVSGL YLVMGFFSTT ALLILVDTIL FGNINNVVAE PFNVSSYIIA PLNNLLYNAR YENLAQHGIH PYYTHILVNM PQILGPGLIF FVSKSYTKTT PFLTVISGLL FLSVIPHQEL RFLIPLLPLA CCSFDFTLKW VQPWMLYTWY IFNIFMSILM GKLHQGGVVP VLDHIKSEAS VQVWWRTYTP PSWILGSNST ETTHLGEKLN DNKFINIVDC MGADSKEVQQ ILQTISTNKP VYLITPIASF KHFDESRFSP VWNYTFHLDL DHLDFADIQP GLGVYQLL //