IFF4_CANAL
ID IFF4_CANAL Reviewed; 1526 AA.
AC Q5AAL9; A0A1D8PRR0;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cell wall protein IFF4;
DE AltName: Full=Adhesin-like protein IFF4;
DE Flags: Precursor;
GN Name=IFF4; OrderedLocusNames=CAALFM_CR00610WA; ORFNames=CaO19.7472;
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 PREDICTION OF GPI-ANCHOR.
RX PubMed=12734798; DOI=10.1002/yea.988;
RA Lee S.A., Wormsley S., Kamoun S., Lee A.F., Joiner K., Wong B.;
RT "An analysis of the Candida albicans genome database for soluble secreted
RT proteins using computer-based prediction algorithms.";
RL Yeast 20:595-610(2003).
RN [5]
RP PREDICTION OF GPI-ANCHOR.
RX PubMed=12845604; DOI=10.1002/yea.1007;
RA De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT "Genome-wide identification of fungal GPI proteins.";
RL Yeast 20:781-796(2003).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17481864; DOI=10.1016/j.colsurfb.2007.03.017;
RA Kempf M., Apaire-Marchais V., Saulnier P., Licznar P., Lefrancois C.,
RA Robert R., Cottin J.;
RT "Disruption of Candida albicans IFF4 gene involves modifications of the
RT cell electrical surface properties.";
RL Colloids Surf. B Biointerfaces 58:250-255(2007).
RN [7]
RP IDENTIFICATION IN THE HYR1/IFF FAMILY.
RX PubMed=17371861; DOI=10.1128/iai.00102-07;
RA Bates S., de la Rosa J.M., MacCallum D.M., Brown A.J., Gow N.A., Odds F.C.;
RT "Candida albicans Iff11, a secreted protein required for cell wall
RT structure and virulence.";
RL Infect. Immun. 75:2922-2928(2007).
RN [8]
RP FUNCTION.
RX PubMed=18178776; DOI=10.1128/ec.00445-07;
RA Fu Y., Luo G., Spellberg B.J., Edwards J.E. Jr., Ibrahim A.S.;
RT "Gene overexpression/suppression analysis of candidate virulence factors of
RT Candida albicans.";
RL Eukaryot. Cell 7:483-492(2008).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=21841123; DOI=10.1128/ec.05044-11;
RA Boisrame A., Cornu A., Da Costa G., Richard M.L.;
RT "Unexpected role for a serine/threonine-rich domain in the Candida albicans
RT Iff protein family.";
RL Eukaryot. Cell 10:1317-1330(2011).
RN [10]
RP INDUCTION.
RX PubMed=21592964; DOI=10.1074/jbc.m111.233569;
RA Singh R.P., Prasad H.K., Sinha I., Agarwal N., Natarajan K.;
RT "Cap2-HAP complex is a critical transcriptional regulator that has dual but
RT contrasting roles in regulation of iron homeostasis in Candida albicans.";
RL J. Biol. Chem. 286:25154-25170(2011).
RN [11]
RP INDUCTION.
RX PubMed=23490206; DOI=10.1111/cmi.12135;
RA She X., Zhang L., Chen H., Calderone R., Li D.;
RT "Cell surface changes in the Candida albicans mitochondrial mutant
RT goa1Delta are associated with reduced recognition by innate immune cells.";
RL Cell. Microbiol. 15:1572-1584(2013).
CC -!- FUNCTION: GPI-anchored cell wall protein involved in cell wall
CC organization, hyphal growth, as well as in host-fungal interaction and
CC virulence. Plays a role in adherence to plastic and to host epithelial
CC cells. Promotes the tissue fungal burden during murine vaginal
CC candidiasis. Increases also susceptibility to neutrophil-mediated
CC killing. Furthermore, contributes to the severity of hematogenously
CC disseminated candidiasis in normal mice, but not in neutropenic mice.
CC {ECO:0000269|PubMed:17481864, ECO:0000269|PubMed:18178776}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:21841123}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Repressed by HAP43 and in absence of GOA1.
CC {ECO:0000269|PubMed:21592964, ECO:0000269|PubMed:23490206}.
CC -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC reticulum and serves to target the protein to the cell surface. There,
CC the glucosamine-inositol phospholipid moiety is cleaved off and the
CC GPI-$modified mannoprotein is covalently attached via its lipidless GPI
CC glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
CC -!- DISRUPTION PHENOTYPE: Leads to decreased adherence of germ tubes to
CC plastic and epithelial cells, but not endothelial cells.
CC {ECO:0000269|PubMed:17481864}.
CC -!- SIMILARITY: Belongs to the HYR1/IFF family. {ECO:0000305}.
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DR EMBL; CP017630; AOW30829.1; -; Genomic_DNA.
DR RefSeq; XP_718630.1; XM_713537.1.
DR AlphaFoldDB; Q5AAL9; -.
DR SMR; Q5AAL9; -.
DR BioGRID; 1222788; 10.
DR STRING; 237561.Q5AAL9; -.
DR GeneID; 3639694; -.
DR KEGG; cal:CAALFM_CR00610WA; -.
DR CGD; CAL0000197990; IFF4.
DR VEuPathDB; FungiDB:CR_00610W_A; -.
DR eggNOG; KOG1216; Eukaryota.
DR HOGENOM; CLU_006199_1_0_1; -.
DR InParanoid; Q5AAL9; -.
DR OMA; DTINTEY; -.
DR OrthoDB; 1658843at2759; -.
DR PHI-base; PHI:3513; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:CGD.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
PE 1: Evidence at protein level;
KW Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1502
FT /note="Cell wall protein IFF4"
FT /id="PRO_0000424760"
FT PROPEP 1503..1526
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424761"
FT REGION 512..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1180..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1502
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1526 AA; 160456 MW; B972CB3515E4BC06 CRC64;
MKFLQKFIIT VALLTNIVFA IDITENKVDR GSVTLSFGEI IIHPGASWSI IDNAFSNFIG
KLDVKAKSAL YISSTSHLLA LQVSLTTLLH SINNSGIISF DSRVSLTPSS YDLRGLSFTN
SGEMYFAASG RVPSTMSLTS ASWTNTGLLS FYQNQRTSGA VCLGFPLGSI TNSGKICLNN
QVYQQTTQIK GSGCFSANGD STIYIANVLL SVSANQNFHL VDKDSSMIVQ AISTTQTFNV
YGFGNGNKIG LTLPLIGIIL ESAHSYDSST GILTLRNFLL EQRFNIGLGY DSSKFSVVTD
SGSGIPSTIW GSVTYTGRVP TRALPKSCQM ACKPIPEAPG VKPTDYTTTI TKTNTAGNTV
TETGAVTIST DKSGSWFTTT SIFPTLTTAT STSITTTLSN EAHIKTTDNT LAKVSSTVDY
ISAPISSSEF ISLESFVDET LSNENPISTS TDYASENSFA ISESTFITAS DFQATESLVT
ESYFSKSQSS DSESFVINTS SAVDNSYVSS SSSAGGSSFP EETHMLQTSD SDLSSTAGSE
SDVTEFSDVS LATASDSSIA DKSIGTESLY SEISLVSASE STGSIGELSI SGDTLLKTAS
ETKFVKSSFS SDLISETSSE LFVSSSVSTD MILETANDSF ITSDKVVETP SYSNELAFET
VSETIINSFV SSESSLNTAS NSLIASKPST DSSSYTTDID FETTTKSFAE SPSYFSETVS
EIASKSSLSM VEPSCWSELP FETSIESLIA PSYISSEPAP ETASESFIVK PSYSEIASES
ITKSIISTIE ASISSDIFSD ATTGSIVVQP SVSSGISLEI PSESMLFSES SISKPFISSQ
SIHECTSDSI LVVPSFFSSD VSFETVEYSS TVSTSVDAEP SYSSEISLKT PSESFIVSET
FLEPSYSGEV VLATPSESVV ASETDVNKPS YSNEAVLQTP SESYILSETG VKESSESSEF
ALSTPSTSFI ASETFTVQSF ASSEVSFGSD RESTISTEAI QVEPSISNDV VLETASESFI
SKAPTTSEFT ILSETSIVEP SILSDLRFET TSQSTEMAPS ATGVSYFSST ETPLASSSSY
ESSFATSSVS AIQSINSQVA SASFVSADST DSSEVGSSYT TASAFGPASS ASEEKFISVW
ETSNSGGSFT LESSTSVASV VTTPLPFTSN DIITEISSTW NGAKSDSPHT SESDITSQYN
SHSTSVATRS DSISLTDTFE IGFASTWTTG GSGNGGSMKS DVSNQDSYAT MLPTSFLDTS
NSDITTGVVS TWDAKNSNSY TSAELSTDPY SSDGYASSAT AALSITESIP TTDTINTEYH
SNGDITTSGG FKEISLTSHY EGGFTSESAG YTIASPSGST QEFATATITS CFESKCSENV
VTYISSVSHS TVTTGYEDTR FTGSIFSGDL ASTGDNIVSA SGRSVTDATN PFATNTDIGT
TSTVSLYGDL NDSDSSVSGY PTNRSDSNGY ANTPTTGSNT SGDFSQTIET GSSSFTAIPF
ENGSTNISNK YLKFLGTVVS ILILLI
