IFF8_CANAL
ID IFF8_CANAL Reviewed; 714 AA.
AC Q59XB0; A0A1D8PMZ9;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Cell wall protein IFF7;
DE AltName: Full=Adhesin-like protein IFF7;
DE Flags: Precursor;
GN Name=IFF8; OrderedLocusNames=CAALFM_C500710WA;
GN ORFNames=CaO19.570, CaO19.8201;
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 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 [7]
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. {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: Expression is down-regulated in absence of GOA1.
CC {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 -!- SIMILARITY: Belongs to the HYR1/IFF family. {ECO:0000305}.
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DR EMBL; CP017627; AOW29514.1; -; Genomic_DNA.
DR RefSeq; XP_714201.2; XM_709108.2.
DR AlphaFoldDB; Q59XB0; -.
DR SMR; Q59XB0; -.
DR STRING; 237561.Q59XB0; -.
DR GeneID; 3644117; -.
DR KEGG; cal:CAALFM_C500710WA; -.
DR CGD; CAL0000190849; IFF8.
DR VEuPathDB; FungiDB:C5_00710W_A; -.
DR HOGENOM; CLU_006199_2_0_1; -.
DR InParanoid; Q59XB0; -.
DR OrthoDB; 1483197at2759; -.
DR PRO; PR:Q59XB0; -.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
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 GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
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..690
FT /note="Cell wall protein IFF7"
FT /id="PRO_0000424766"
FT PROPEP 691..714
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424767"
FT REGION 320..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 690
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 663
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 714 AA; 72110 MW; 9773734A63BB14DE CRC64;
MLFTLSILST LLFSTSISAI EITQNRVDHG TITTSIGDIT IDSGAYWSII DNSISTFIGN
LDIKSNAGLY ISSTISNLPL LVLLNSGSAS ITNDGIVSLD ARTSTQGSSQ FNLVGGSFEN
NGEFYLAASG AIPMTMGLTG KSWNNNGLIV AYQNERSSGS VKFGVIGQTI TNKGQICLTN
QVYQQTSKID GSGCVTAKKN ASIYISNVLD PQSVSTEQNY FLADDKSSII TQAVGFNTQV
INVFGFGNGN KIGLTLPLKS GNGGQAYSYD SDSGVLSLSS GLFGQKFNIG PGYDSKLFSI
VTDNSEGIPS VNNGAVSYSG PVPSQKSLPS ACNVECKPVP NAPDDGSSSS SSVVSSTTST
ASTDSASLSS TSGEESSAST TTTESSETSN TSSNASETNG SSTESETTGS ATTSEASETI
NSSESSETSG ASETSQSTGT SESSETESSV TESSETDSIT ATTSDTTSSG NDNSSVTSSS
DASTDSITSE TASSSSTPLS GDSSQVSSLT TGTSPDTIAS FQTDSTSFGF GSGSPSSGAV
QSSGVTNSTP NTGDVNTQSN TANIATSDNT ATSTASNDTG VNTATATTTG TGTGPDNNNN
NNNNNNNNNN NNNNNNNNNN NNTNNSGVSA ADSKASGDIS TVTASSTTLI SVASVSSTYP
IANESSSPSS SSSSSSSSSG TPGEVIPNAN GSSKLSIGMT FMISGFATMF ALFM
