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Cell-surface associated glycoprotein DFI1 (Defective in filamentous invasion protein 1)

 DFI1_CANAL              Reviewed;         337 AA.
Q5AFI4; A0A1D8PQK9; Q3MPU3;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
23-MAY-2018, entry version 66.
RecName: Full=Cell-surface associated glycoprotein DFI1 {ECO:0000305};
AltName: Full=Defective in filamentous invasion protein 1 {ECO:0000303|PubMed:20384695};
Name=DFI1 {ECO:0000303|PubMed:20384695};
OrderedLocusNames=CAALFM_C700360WA; ORFNames=CaO19.7084;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, MUTAGENESIS OF GLY-273 AND
GLY-277, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=20384695; DOI=10.1111/j.1365-2958.2010.07137.x;
Zucchi P.C., Davis T.R., Kumamoto C.A.;
"A Candida albicans cell wall-linked protein promotes invasive
filamentation into semi-solid medium.";
Mol. Microbiol. 76:733-748(2010).
[5]
FUNCTION, DOMAIN, CALMODULIN-BINDING, AND DISRUPTION PHENOTYPE.
PubMed=24155896; DOI=10.1371/journal.pone.0076239;
Davis T.R., Zucchi P.C., Kumamoto C.A.;
"Calmodulin binding to Dfi1p promotes invasiveness of Candida
albicans.";
PLoS ONE 8:E76239-E76239(2013).
-!- FUNCTION: Cell-surface associated glycoprotein that acts as a
plasma membrane receptor-type protein which senses the presence of
matrix. Binds to calmodulin in response to environmental
conditions and initiates a signaling cascade that activates CEK1,
thus promoting invasive filamentation. Involved in the maintenance
of the cell wall. {ECO:0000269|PubMed:20384695,
ECO:0000269|PubMed:24155896}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20384695};
Multi-pass membrane protein {ECO:0000269|PubMed:20384695}. Cell
septum {ECO:0000269|PubMed:20384695}. Secreted, cell wall
{ECO:0000269|PubMed:20384695}. Note=A part becomes cross-linked to
the cell wall and thus links the cell wall to the plasma membrane
and cytoplasm. {ECO:0000269|PubMed:20384695}.
-!- DOMAIN: The GxxxG glycophorin motif in the transmembrane domain is
required for CEK1 activation and subsequent invasive filamentation
on agar medium. {ECO:0000269|PubMed:20384695}.
-!- DOMAIN: The cytoplasmic C-terminal calmidulin-binding motif
(residues 301 to 317) is important for CEK1 activation and
subsequent invasive filamentation on agar medium.
{ECO:0000269|PubMed:24155896}.
-!- PTM: Cross-linked to the carbohydrate polymers of the cell wall.
{ECO:0000269|PubMed:20384695}.
-!- PTM: O-glycosylated by MNT1 and MNT2. Also N-glycosylated.
{ECO:0000269|PubMed:20384695}.
-!- DISRUPTION PHENOTYPE: Shows defects in invasion of agar medium and
attenuated virulence in a murine model of disseminated
candidiasis. Leads to hypersensibility to the glucan synthase
inhibitor capsofungin and the cell wall disturbing agents Congo
red and calcofluor white. {ECO:0000269|PubMed:20384695,
ECO:0000269|PubMed:24155896}.
-!- SIMILARITY: Belongs to the MID2 like cell wall stress sensor
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; CP017629; AOW30415.1; -; Genomic_DNA.
RefSeq; XP_720375.1; XM_715282.1.
ProteinModelPortal; Q5AFI4; -.
EnsemblFungi; AOW30415; AOW30415; CAALFM_C700360WA.
GeneID; 3638038; -.
KEGG; cal:CAALFM_C700360WA; -.
CGD; CAL0000194442; DFI1.
InParanoid; Q5AFI4; -.
OMA; LENYHQP; -.
OrthoDB; EOG092C58ML; -.
Proteomes; UP000000559; Chromosome 7.
GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IDA:CGD.
GO; GO:0005886; C:plasma membrane; IDA:CGD.
GO; GO:0007155; P:cell adhesion; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
InterPro; IPR007567; Mid2_dom.
Pfam; PF04478; Mid2; 1.
1: Evidence at protein level;
Cell membrane; Cell wall; Complete proteome; Glycoprotein; Membrane;
Reference proteome; Secreted; Transmembrane; Transmembrane helix;
Virulence.
CHAIN 1 337 Cell-surface associated glycoprotein
DFI1.
/FTId=PRO_0000431721.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000305}.
TRANSMEM 22 42 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 43 269 Extracellular. {ECO:0000305}.
TRANSMEM 270 290 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 291 337 Cytoplasmic. {ECO:0000305}.
MOTIF 273 277 Glycophorin A.
{ECO:0000303|PubMed:20384695}.
MOTIF 301 314 Calmodulin-binding.
{ECO:0000269|PubMed:24155896}.
COMPBIAS 7 12 Poly-Asn. {ECO:0000255}.
COMPBIAS 102 240 Thr-rich. {ECO:0000255|PROSITE-
ProRule:PRU00017}.
COMPBIAS 109 252 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 273 273 G->L: Impairs CEK1 activation and
invasive filamentation; when associated
with L-277.
{ECO:0000269|PubMed:20384695}.
MUTAGEN 277 277 G->L: Impairs CEK1 activation and
invasive filamentation; when associated
with L-273.
{ECO:0000269|PubMed:20384695}.
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


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