DFI1_CANAL
ID DFI1_CANAL Reviewed; 337 AA.
AC Q5AFI4; A0A1D8PQK9; Q3MPU3;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cell-surface associated glycoprotein DFI1 {ECO:0000305};
DE AltName: Full=Defective in filamentous invasion protein 1 {ECO:0000303|PubMed:20384695};
GN Name=DFI1 {ECO:0000303|PubMed:20384695};
GN OrderedLocusNames=CAALFM_C700360WA; ORFNames=CaO19.7084;
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).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, MUTAGENESIS OF GLY-273 AND GLY-277,
RP SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=20384695; DOI=10.1111/j.1365-2958.2010.07137.x;
RA Zucchi P.C., Davis T.R., Kumamoto C.A.;
RT "A Candida albicans cell wall-linked protein promotes invasive
RT filamentation into semi-solid medium.";
RL Mol. Microbiol. 76:733-748(2010).
RN [5]
RP FUNCTION, DOMAIN, CALMODULIN-BINDING, AND DISRUPTION PHENOTYPE.
RX PubMed=24155896; DOI=10.1371/journal.pone.0076239;
RA Davis T.R., Zucchi P.C., Kumamoto C.A.;
RT "Calmodulin binding to Dfi1p promotes invasiveness of Candida albicans.";
RL PLoS ONE 8:E76239-E76239(2013).
CC -!- FUNCTION: Cell-surface associated glycoprotein that acts as a plasma
CC membrane receptor-type protein which senses the presence of matrix.
CC Binds to calmodulin in response to environmental conditions and
CC initiates a signaling cascade that activates CEK1, thus promoting
CC invasive filamentation. Involved in the maintenance of the cell wall.
CC {ECO:0000269|PubMed:20384695, ECO:0000269|PubMed:24155896}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20384695};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20384695}. Cell septum
CC {ECO:0000269|PubMed:20384695}. Secreted, cell wall
CC {ECO:0000269|PubMed:20384695}. Note=A part becomes cross-linked to the
CC cell wall and thus links the cell wall to the plasma membrane and
CC cytoplasm. {ECO:0000269|PubMed:20384695}.
CC -!- DOMAIN: The GxxxG glycophorin motif in the transmembrane domain is
CC required for CEK1 activation and subsequent invasive filamentation on
CC agar medium. {ECO:0000269|PubMed:20384695}.
CC -!- DOMAIN: The cytoplasmic C-terminal calmodulin-binding motif (residues
CC 301 to 317) is important for CEK1 activation and subsequent invasive
CC filamentation on agar medium. {ECO:0000269|PubMed:24155896}.
CC -!- PTM: Cross-linked to the carbohydrate polymers of the cell wall.
CC {ECO:0000269|PubMed:20384695}.
CC -!- PTM: O-glycosylated by MNT1 and MNT2. Also N-glycosylated.
CC {ECO:0000269|PubMed:20384695}.
CC -!- DISRUPTION PHENOTYPE: Shows defects in invasion of agar medium and
CC attenuated virulence in a murine model of disseminated candidiasis.
CC Leads to hypersensibility to the glucan synthase inhibitor capsofungin
CC and the cell wall disturbing agents Congo red and calcofluor white.
CC {ECO:0000269|PubMed:20384695, ECO:0000269|PubMed:24155896}.
CC -!- SIMILARITY: Belongs to the MID2 like cell wall stress sensor family.
CC {ECO:0000305}.
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DR EMBL; CP017629; AOW30415.1; -; Genomic_DNA.
DR RefSeq; XP_720375.1; XM_715282.1.
DR AlphaFoldDB; Q5AFI4; -.
DR STRING; 237561.Q5AFI4; -.
DR PRIDE; Q5AFI4; -.
DR EnsemblFungi; KHC71732; KHC71732; W5Q_05091.
DR EnsemblFungi; KHC80853; KHC80853; I503_05047.
DR GeneID; 3638038; -.
DR KEGG; cal:CAALFM_C700360WA; -.
DR CGD; CAL0000194442; DFI1.
DR VEuPathDB; FungiDB:C7_00360W_A; -.
DR eggNOG; ENOG502S35T; Eukaryota.
DR HOGENOM; CLU_823854_0_0_1; -.
DR InParanoid; Q5AFI4; -.
DR OMA; LVFWRMK; -.
DR OrthoDB; 1616984at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IDA:CGD.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0007155; P:cell adhesion; IMP:CGD.
DR InterPro; IPR007567; Mid2_dom.
DR Pfam; PF04478; Mid2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall; Glycoprotein; Membrane; Reference proteome;
KW Secreted; Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..337
FT /note="Cell-surface associated glycoprotein DFI1"
FT /id="PRO_0000431721"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 22..42
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..269
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..337
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 124..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..277
FT /note="Glycophorin A"
FT /evidence="ECO:0000303|PubMed:20384695"
FT MOTIF 301..314
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:24155896"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 273
FT /note="G->L: Impairs CEK1 activation and invasive
FT filamentation; when associated with L-277."
FT /evidence="ECO:0000269|PubMed:20384695"
FT MUTAGEN 277
FT /note="G->L: Impairs CEK1 activation and invasive
FT filamentation; when associated with L-273."
FT /evidence="ECO:0000269|PubMed:20384695"
SQ SEQUENCE 337 AA; 36489 MW; 82A80BD065DD7D31 CRC64;
MEKLSINNNN NNRRYQSRRF DGITIIRIVV LVFIVTVSTY FVNSYTCNQP HHNHSTRPSH
YLPINGTHGL MNNDDSLHNK GAIGHYNTTV SLERRADENN STTNGLFPST SSSTFIFTPS
SSSSSTFQQS RSSPQTTSTS SFVATTSSFQ QETSQTSIPD TTTDFSFSSF SEAPTTSTTS
STSEFSSTPQ ETSNTVTSTS STSTSSSSSP TSSPATTSAS QHVTTFSSVD NGKTIVVTRT
SVISSSPTAS NSNNNKNNDN GGGLSHTNRI VVGVVVGVGG SILIGLLAVL FYLRKRNNRD
YEGGWTFWRK NEKLGSDEFF NGELGVRDRN INQGSNF
