IFF6_CANAL
ID IFF6_CANAL Reviewed; 1085 AA.
AC Q59XL0; A0A1D8PIC5; Q59X60;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Cell wall protein IFF6;
DE AltName: Full=Adhesin-like protein IFF6;
DE AltName: Full=Hyphally regulated cell wall protein 10;
DE Flags: Precursor;
GN Name=IFF6; Synonyms=HYR10; OrderedLocusNames=CAALFM_C209130CA;
GN ORFNames=CaO19.11553, CaO19.4072;
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=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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RX PubMed=17164403; DOI=10.1074/mcp.m600210-mcp200;
RA Fernandez-Arenas E., Cabezon V., Bermejo C., Arroyo J., Nombela C.,
RA Diez-Orejas R., Gil C.;
RT "Integrated proteomics and genomics strategies bring new insight into
RT Candida albicans response upon macrophage interaction.";
RL Mol. Cell. Proteomics 6:460-478(2007).
RN [7]
RP INDUCTION.
RX PubMed=20735781; DOI=10.1111/j.1365-2958.2010.07331.x;
RA Lohse M.B., Johnson A.D.;
RT "Temporal anatomy of an epigenetic switch in cell programming: the white-
RT opaque transition of C. albicans.";
RL Mol. Microbiol. 78:331-343(2010).
RN [8]
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 [9]
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).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:21841123}. Membrane {ECO:0000305}; Lipid-anchor,
CC GPI-anchor {ECO:0000305}.
CC -!- INDUCTION: Opaque-specific transcript. Repressed by HAP43 and induced
CC by macrophages. {ECO:0000269|PubMed:17164403,
CC ECO:0000269|PubMed:20735781, ECO:0000269|PubMed:21592964}.
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 -!- SIMILARITY: Belongs to the HYR1/IFF family. {ECO:0000305}.
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DR EMBL; CP017624; AOW27899.1; -; Genomic_DNA.
DR RefSeq; XP_714246.2; XM_709153.2.
DR AlphaFoldDB; Q59XL0; -.
DR SMR; Q59XL0; -.
DR STRING; 237561.Q59XL0; -.
DR GeneID; 3644087; -.
DR KEGG; cal:CAALFM_C209130CA; -.
DR CGD; CAL0000183650; IFF6.
DR VEuPathDB; FungiDB:C2_09130C_A; -.
DR HOGENOM; CLU_006199_0_0_1; -.
DR OrthoDB; 1483197at2759; -.
DR PRO; PR:Q59XL0; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IEA:UniProt.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:UniProt.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1062
FT /note="Cell wall protein IFF6"
FT /id="PRO_0000424764"
FT PROPEP 1063..1085
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424765"
FT REGION 339..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1062
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 864
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 874
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 882
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 886
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 896
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 924
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 968
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1008
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1085 AA; 105454 MW; F1CB29885B5060F1 CRC64;
MLLKQIFLPF FVLFNAINAI DIYQNQVSRG TIDLSIGAIT IHSGAYWSII DNAISALVGT
LTVQQDAGFY ITGLNPLLGL QVELLGVLNS IKNDGIVSFN GLNSLVGPIY NLVGLSFQNN
GEFYLSASGV APPVFSITAA DWHNNGLLVL AQAKRTSALA NLGFPTGSIE NQGSICLFGT
AYQQLTSITG SGCISADRDS TIYIFSSLLP IATTQTLYLA DRASSIVIQP VTLPATYTVR
GFGNGNKVGI SLPLLSVPLL GQPAYSYDPS SGVLTLRGLG VGLLSQRFQI GTGYDSSLLE
IVTDDGAGLP TTLLGSVRYN GPVPNNAVPA SCNCKYVPPS PGTDESSSLS SSTSEQSSSS
ATSVSASETS DTSSTQESSL SSEVSSTQEP SSSTPEPSSS SETSSTQESS STEGPSSSTD
SSTEASSSES STAPSSSAEA SSSTESSTEE PSSSTEGPSS SQESSSSEES STQEPSSSTK
ESSSTEGPSS TEESSSTEGP SSSTDSSTDI TSASSTDEQS SSGTGQSSTE DEPIDSTESD
TSSATDSSTA TDSSATNTDT NSESTDSSTA TDTSSTDSNT ASSTETNTDV TDSSTDSNTG
ATESSTATDT NTDATDSSTV SETGATDSST ATDTNTGATE SSTDSNTGAT DSSTATDTNT
SATNTDTNTG SNTATNTDDN TATDTSSTET NTATNTDGTE TNTGTTETNT DTSASNTDDN
TGSNTATNTG GTDTNTDTNT GGTDTNTGTN TGGTDTKTGT NTATGTNTGA TETNTATNTN
GNGTNTNTGA TDTATNTATG TNTNTGATDT NTNTNTGATV TNTATNTGDV SATKDIPSPT
STDEGSNNGG GSNNGSGSNN GSGNGSGSGS GSGNGSGDGS NNGSGNGSDN GSGSGNGSDN
GSGSGSGSDN GSGSGSGSGS GSGNGSGSGS DNGSGSGNGS GSGSGSGSGS DNGSGSGSNN
GSGNGSGNGS GSGSDNGSGN GSGSGSGSGS GNGSGNGSGS GSGSGSGNGS GSNNNNGSGS
GSGSGNGQDN GIITSSIGQP GSSTSTQGPS SSNSATIPEQ ANSGNHIKFT LFNGLLIGLV
PIVFM
