MCD4_CANAL
ID MCD4_CANAL Reviewed; 971 AA.
AC Q5A3M6; A0A1D8PFC6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=GPI ethanolamine phosphate transferase 1;
DE EC=2.-.-.-;
GN Name=MCD4; OrderedLocusNames=CAALFM_C112200WA;
GN ORFNames=CaO19.12709, CaO19.5244;
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: Ethanolamine phosphate transferase involved in
CC glycosylphosphatidylinositol-anchor biosynthesis. Transfers
CC ethanolamine phosphate to the first alpha-1,4-linked mannose of the
CC glycosylphosphatidylinositol precursor of GPI-anchor (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 PIGG/PIGN/PIGO family. PIGN subfamily.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW26839.1; -; Genomic_DNA.
DR RefSeq; XP_716313.1; XM_711220.2.
DR AlphaFoldDB; Q5A3M6; -.
DR STRING; 237561.Q5A3M6; -.
DR PRIDE; Q5A3M6; -.
DR GeneID; 3642036; -.
DR KEGG; cal:CAALFM_C112200WA; -.
DR CGD; CAL0000201697; MCD4.
DR VEuPathDB; FungiDB:C1_12200W_A; -.
DR eggNOG; KOG2124; Eukaryota.
DR HOGENOM; CLU_007676_0_0_1; -.
DR InParanoid; Q5A3M6; -.
DR OMA; TISHFCI; -.
DR OrthoDB; 270107at2759; -.
DR UniPathway; UPA00196; -.
DR PRO; PR:Q5A3M6; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051377; F:mannose-ethanolamine phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0015867; P:ATP transport; IEA:EnsemblFungi.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central.
DR CDD; cd16020; GPI_EPT_1; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007070; GPI_EtnP_transferase_1.
DR InterPro; IPR017852; GPI_EtnP_transferase_1_C.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR InterPro; IPR037671; PIGN_N.
DR PANTHER; PTHR12250; PTHR12250; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR Pfam; PF04987; PigN; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW GPI-anchor biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..971
FT /note="GPI ethanolamine phosphate transferase 1"
FT /id="PRO_0000246203"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..477
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..533
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 575..595
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 596..597
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..640
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 641..645
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..682
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..716
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 717..737
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 738..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..813
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 857..877
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 878..885
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 907..923
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 924..944
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 945..971
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 971 AA; 110656 MW; 5FA422330196B699 CRC64;
MDRNRQLLLV IGVLFHFFYL WSIFDIYFVS PLVHGMDHHK STWTPPAKRL FLIVGDGLRA
DKTFQKLTHP RTGEEKYLAP YLRSLALNNG TWGISNTRMP TESRPGHVAM IAGFYEDVSA
VTKGWKENPV DFDSFFNQSK HTYSFGSPDI LPMFAFGDGV VPGRIDVCMY GHEFEDFTAS
SIELDAYVFH HLDELMHNST TNATLNEELR QDGNVFFLHL LGPDTAGHAY RPYSAEYYEN
IEYIDRKLEE VIPQINKFFG DDQTAFVFTA DHGMSDFGSH GDGHPDNTRT PLIAWGAGVK
KPIHLQDVSN LEEQLLKQSP ENSGFESTYF DTWELDHLVR NDVNQADIAS LMAYLIGANY
PANSVGELPL GYIDADPVTK ARALYANSLA IVEQYFVKEQ EVYNHQFKFK PYSPFEEKSI
QKYQQEIESL IDQLEKSGSG SKDEIEKKVI AKIEELMKTT LDGLTYLQTY NWLLLRSIVT
LGFFGWIVYS FNIFLKLFVL NEDELKIPPE FSVTLVGIFG ALAISINYLL FYQNSPFNYY
MYAAFPLYFW YTILNEKKYL ITGIESFLHG ISNTTKFLIV VSFIGMYEGI AYGFFERVMF
SIILIIIGLY PLLVHGAHKV SGLMKTIWFI TCLLMCTFTN LDPVKIESLF QINVGTILAL
IVSIMGTKQV FKRTQVGPIQ KQLIIAQIAI IPIILFATNI SVLSLQARTG LPLYSQILGW
ITFIVSLIVL PILHFLNPSS DYQLRLLIIF LTFVPTFIIL TISFELLFYV GFSLILLQWL
SIEELLKFSH KDLVETFEKT GKLPKGYWLQ VIRITIIGFF FLQLAFFGTG NIASISSFSL
DSVYRLIPIF DPFSMGALLM IKLIIPYVLL STCLGIMNHQ LEIKKFTIST LIISTSDFLS
LNFFFLVRTE GSWLDIGVSI SNYCLAILSS LFMLILELIS SVVLSGVEYN SDGTKLDFEP
ISYRVRKRKV T
