GPI14_CANAL
ID GPI14_CANAL Reviewed; 398 AA.
AC Q5AMR5; A0A1D8PLF8;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=GPI mannosyltransferase 1;
DE EC=2.4.1.-;
DE AltName: Full=GPI mannosyltransferase I;
DE Short=GPI-MT-I;
DE AltName: Full=Glycosylphosphatidylinositol-anchor biosynthesis protein 14;
GN Name=GPI14; OrderedLocusNames=CAALFM_C402100CA;
GN ORFNames=CaO19.12050, CaO19.4581;
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 first alpha-1,4-mannose to GlcN-
CC acyl-PI during GPI precursor assembly. Required for cell wall integrity
CC (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 PIGM family. {ECO:0000305}.
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DR EMBL; CP017626; AOW28981.1; -; Genomic_DNA.
DR RefSeq; XP_722653.1; XM_717560.1.
DR AlphaFoldDB; Q5AMR5; -.
DR SMR; Q5AMR5; -.
DR STRING; 237561.Q5AMR5; -.
DR GeneID; 3635641; -.
DR KEGG; cal:CAALFM_C402100CA; -.
DR CGD; CAL0000197470; GPI14.
DR VEuPathDB; FungiDB:C4_02100C_A; -.
DR eggNOG; KOG3893; Eukaryota.
DR HOGENOM; CLU_024220_1_0_1; -.
DR InParanoid; Q5AMR5; -.
DR OMA; VTSQYFI; -.
DR OrthoDB; 1003258at2759; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q5AMR5; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990529; C:glycosylphosphatidylinositol-mannosyltransferase I complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051751; F:alpha-1,4-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0004376; F:glycolipid mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IMP:CGD.
DR GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR InterPro; IPR007704; PIG-M.
DR PANTHER; PTHR12886; PTHR12886; 1.
DR Pfam; PF05007; Mannosyl_trans; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum;
KW Glycosyltransferase; GPI-anchor biosynthesis; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..398
FT /note="GPI mannosyltransferase 1"
FT /id="PRO_0000246226"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 398 AA; 46549 MW; 4DC724FEFD433E26 CRC64;
MSQLKYLITF SILLRFGFFF FGLYQDEYMP VKYTDIDYLV FNDASKFVYQ GLSPYLRETY
RYTPILAILL IPDNFGKYWY HFGKLLFMVS DVITGLIILK LLSKQQQLSE KKKMILSSIW
LLNPMVITIS TRGSAESVLT VMIMLSLYYL LDKDNVILSA IWLGLSIHFK IYPIIYLPSI
LYYLSSQETP FLASVPGINL VNAKNLKYII ITLTTLAVVN YLMFLKYGWE FIDNSYLYHV
TRLDHRHNFS VYNMVLYYKS ALLEDSNGFD IEKIAFVPQL LLSAVIIPLI FAKEDLISSL
FIQTFVFVAF NKVITSQYFI WFLIFLPHFL SKTKLLTTDK ITGISCLLLW IISQATWLYF
AYKLEFLGEN TFDNGLMYSS VFFFLSNCWC TMKFIQSL
