ID   EPD1_CANMA              Reviewed;         549 AA.
AC   P56092;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Protein EPD1;
DE   AltName: Full=Essential for pseudohyphal development 1;
DE   Flags: Precursor;
GN   Name=EPD1;
OS   Candida maltosa (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5479;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 28140 / CBS 5611 / IAM 12247 / JCM 1504 / NBRC 1977;
RA   Nakazawa T.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family. {ECO:0000305}.
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DR   EMBL; AB005130; BAA21103.1; -; Genomic_DNA.
DR   AlphaFoldDB; P56092; -.
DR   SMR; P56092; -.
DR   CAZy; CBM43; Carbohydrate-Binding Module Family 43.
DR   CAZy; GH72; Glycoside Hydrolase Family 72.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042123; F:glucanosyltransferase activity; IEA:UniProt.
DR   GO; GO:0071840; P:cellular component organization or biogenesis; IEA:UniProt.
DR   GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:UniProt.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR012946; X8.
DR   PANTHER; PTHR31468; PTHR31468; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   Pfam; PF07983; X8; 1.
DR   SMART; SM00768; X8; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..?
FT                   /note="Protein EPD1"
FT                   /id="PRO_0000010487"
FT   PROPEP          ?..549
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010488"
FT   REGION          336..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..358
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        383
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        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        72..101
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        214..347
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        232..263
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        369..420
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        378..444
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        397..402
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
SQ   SEQUENCE   549 AA;  58620 MW;  0CD006E2F831548C CRC64;
     MLLNSLFPSI LAAATFVTSA AAEDLPPIEI VGNKFFYSNN GSQFYIKGIA YQQNNLDSNS
     TFVDPLADAD NCKRDIPYLE QVDTNVIRVY ALDVTQDHTE CMQMLQDAGI YIIADLSQPD
     ESINRNDPQW NLDLFERYTS VVDKFHNYTN VLGFFAGNEV TNNVSNTDAS AFVKAAIRDT
     KAYIKAKGYR TIPVGYSAND DSDIRVSLAR YFACGDEDES ADFFGMNMYE WCGSSSFKAS
     GYESATDDYK NLGIPIFFSE YGCNEVTPRK FQEVGTLFGS DMTDVWSGGI VYMYLQEENN
     YGLVSVSGSS VSTLQDFNSY KSEILDISPS SVQASAESAS GVSRTSCPTN TDNWEASTEL
     PPTPDKDICD CMSSSLKCVV ADNVSTDDYS DLFDYVCAKI DCSGINANAT TGDYGAYSPC
     GAKDKLSFVL NLYYEEQNES KSACDFSGSA SLQSASTASS CAAYLSSAGV SGLGTVQGSV
     RTDTSEATTD SGSGSSNSGS ASSSKSTSSS TSSGSSGSKS AATAVTVTTL TKIAAVGVSI
     IVGFGLITM