ID   EPD2_CANMA              Reviewed;         549 AA.
AC   O74137;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Protein EPD2;
DE   AltName: Full=Essential for pseudohyphal development 2;
DE   Flags: Precursor;
GN   Name=EPD2;
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;
RX   PubMed=10737195; DOI=10.1271/bbb.64.369;
RA   Nakazawa T., Takahashi M., Horiuchi H., Ohta A., Takagi M.;
RT   "Cloning and characterization of EPD2, a gene required for efficient
RT   pseudohyphal formation of a dimorphic yeast, Candida maltosa.";
RL   Biosci. Biotechnol. Biochem. 64:369-377(2000).
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; AB011286; BAA32730.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74137; -.
DR   SMR; O74137; -.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..?
FT                   /note="Protein EPD2"
FT                   /id="PRO_0000010489"
FT   PROPEP          ?..549
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010490"
FT   REGION          470..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        173
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        467
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        82..111
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        224..358
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        242..273
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        381..432
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        390..456
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
FT   DISULFID        409..414
FT                   /evidence="ECO:0000250|UniProtKB:Q06135"
SQ   SEQUENCE   549 AA;  60094 MW;  CAAF5B47E43CD390 CRC64;
     MISVIKSLLT LSVLSTLAAA KFESATPPIE VVGNKFYYSN NGTQFLLRGI AYQQDTSGSV
     SNGYDSDPNR KYNDPLADAD ACKRDVQYFI DTNTNTLRVY GIDPDKDHEE CMKIFSDAGI
     YVIADLSEPT VSVNRINPEW NLDLYERYTK VIDNMQEYSN VLGFFAGNEV TNNRTNTDAS
     PFVKAAVRDM KKYIKDNDYR TIPVGYSSND DEDTRVAIAD YFACGSLDDR ADFFGINMYE
     WCGRSTFATS GYKDRTEDFK NLTIPIFFSE YGCNEVSPRV FQEVGTLYSD QMTDVWSGGI
     VYMYYEEANH YGLVSLNGDR VSTLADYNNY KSAIKSISPS LARRSTIQSE DSTKTMACPD
     NSHSTWRAST ELPPTPDEEF CDCISQSFNC VVADDVDAED YSTLFGEVCG YIDCGDISAN
     GNTGEYGGFS FCSDKDRLSY VLNQYYHDQN ERADACDFAG SASINDNASA STSCSAAGGR
     GLQSGRRSST TRGGSSSSRS SSSSSSSSTG SGSSNAGIKV GGGQMSTVKL ITITTIVTAF
     VGGLSIIFY