GPI10_CANAL
ID GPI10_CANAL Reviewed; 482 AA.
AC Q5AK24; A0A1D8PP48; Q5AKI6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=GPI mannosyltransferase 3;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase III;
DE Short=GPI-MT-III;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 10;
GN Name=GPI10; OrderedLocusNames=CAALFM_C505040WA;
GN ORFNames=CaO19.11479, CaO19.3996;
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).
CC -!- FUNCTION: Mannosyltransferase involved in glycosylphosphatidylinositol-
CC anchor biosynthesis. Transfers the third mannose to Man2-GlcN-acyl-PI
CC during GPI precursor assembly (By similarity). {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. PIGB
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017627; AOW29908.1; -; Genomic_DNA.
DR RefSeq; XP_721904.2; XM_716811.2.
DR AlphaFoldDB; Q5AK24; -.
DR STRING; 237561.Q5AK24; -.
DR GeneID; 3636488; -.
DR KEGG; cal:CAALFM_C505040WA; -.
DR CGD; CAL0000192151; orf19.11479.
DR VEuPathDB; FungiDB:C5_05040W_A; -.
DR eggNOG; KOG1771; Eukaryota.
DR HOGENOM; CLU_012353_0_1_1; -.
DR InParanoid; Q5AK24; -.
DR OrthoDB; 901894at2759; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q5AK24; -.
DR Proteomes; UP000000559; Chromosome 5.
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:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
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 InterPro; IPR039521; PIG-B/GPI10.
DR PANTHER; PTHR22760; PTHR22760; 1.
DR PANTHER; PTHR22760:SF4; PTHR22760:SF4; 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..482
FT /note="GPI mannosyltransferase 3"
FT /id="PRO_0000246260"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 482 AA; 57060 MW; 3008E6737D8A7885 CRC64;
MTKSTVLSSY KLFAFIFIFR LANSFAIETF FQADEFFQAL EPAHHFVYGY GYLTWEWKQQ
LRSAIHPLIY VLGYKLVGDN TTLVCISPKV INALIAAIGE YNLYKFIIVY DSEKLAWITL
MLSLFNPFNW YVITRSFSNN LEMVFTVLAL RFWPWNKKIN GRWYISLGFG FVSCIIRPTN
ILIWIPLGIW LLISIRITLK WVALSFLEVV LILLINTALD YYFYQKLTFP LYNFLEFNVF
KNLSIFYGTA PWHFYIFQAI PLMLMLYLPL MIYGLKKNIL LLTGLFYIIG FSLIQHKEFR
FIYPIHPILL YFTARGYVKF KPKFVLIGIL LNICIGLFFT NVHERGVIDL TKYLATQQTP
SVGFITPCHS TPWQSYFHNP NLDTNSWFLA CEPPLHLNKP SMEEIRHYRD QSDQFYDAPE
SFLQTHLGKD LPKTEQLVVF EPLEPLMNDY LGREYYECQR FYNSFFHWDS RRDGDIIVYC
RN
