ID   IFF3_CANAL              Reviewed;         941 AA.
AC   Q5A029; A0A1D8PSJ2;
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 IFF3;
DE   AltName: Full=Adhesin-like protein IFF3;
DE   Flags: Precursor;
GN   Name=IFF3; OrderedLocusNames=CAALFM_CR03630WA;
GN   ORFNames=CaO19.11839, CaO19.4361;
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).
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   -!- 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; CP017630; AOW31101.1; -; Genomic_DNA.
DR   RefSeq; XP_715137.2; XM_710044.2.
DR   AlphaFoldDB; Q5A029; -.
DR   SMR; Q5A029; -.
DR   STRING; 237561.Q5A029; -.
DR   PRIDE; Q5A029; -.
DR   GeneID; 3643189; -.
DR   KEGG; cal:CAALFM_CR03630WA; -.
DR   CGD; CAL0000187251; IFF3.
DR   VEuPathDB; FungiDB:CR_03630W_A; -.
DR   HOGENOM; CLU_006199_1_0_1; -.
DR   InParanoid; Q5A029; -.
DR   OrthoDB; 1661813at2759; -.
DR   PRO; PR:Q5A029; -.
DR   Proteomes; UP000000559; Chromosome R.
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; IPR031573; Cell_wall_rpt.
DR   InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR   Pfam; PF11765; Hyphal_reg_CWP; 1.
DR   Pfam; PF15789; Hyr1; 3.
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..917
FT                   /note="Cell wall protein IFF3"
FT                   /id="PRO_0000424758"
FT   PROPEP          918..941
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424759"
FT   LIPID           917
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        367
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        686
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        732
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        790
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        818
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        825
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        884
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        917
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   941 AA;  98731 MW;  27E6743D8CB8EA33 CRC64;
     MQLFQNILVS IALLTQVVFA IEITENKVDR GTVTLNLSDI TIYPGASWSI IDNAYTSFVG
     KLDVRDGAGL YISSTSHLLA LQVSLTALLH SITNNGVVSF DSRISRTSSS YDLRGVSFTN
     NGEMYFAASG EFSSSTALTS ASWTNTRLLS FYQNQRTSGT VSLGMPLGSI TNNGQVCLNN
     QVYEQTTQIK GSGCFTANGD STIYISNVLL AVSPKQNFYL TDKGSSMIVQ AVSTTQTFNV
     YGFGEGNKIG LTIPLMGNLW NSAYAYDTTS GILTLRNLLL EQKFNIGTGY DPSKFQVVTD
     SGSGIPSTIL GSVAYYGRVP ERTLPKSCQI PCKPIPEAPG TTPTQYTTTI TKTNTAGNTV
     TESGVVNVST DKGGSWFTTT SMFPALSTAP STATVFSSDT IMSTVEPDTT ELASLTDIPI
     ETSSVEELLS VMSNWEPSSA PTLSIETPVS SHHSSMQHSS FESSADINTV FSSESAFETA
     SDYIVSTPSS ISHSTMVPQS SVSALSVVSE SLASAEPSFV VPSESFIFSA SSAAPQPSSS
     TYSVSFTTQF ETPSSAGPSL VTSVESNTEL ISSATQSSDI QTEFTSTWTT TNSDGSVVTE
     SGIISQSGTS LTTLTTFQPA TSLVVPPYSV IETEFTSTWT TTNSDSSVAT ESGVVSQSDT
     LLTTVTTFPP APSAIVPEFT SPWKINTSIE SSETLTVSAS SYETVGESLA AATSSYLSSA
     TVVVAPSESE INTSSSILNN EEIASAPVSD TTSIAEHHDG SLSMTTTEFV NSNSLPSSHS
     IVTATITSCN KSKCSESVVT YVSSVSCATI TVGDSEKNSS IVGNNISSIV GDDVSNTQAI
     TMATSTESAT TLTSVSGAKP SVANDATNSV HTTDYTTATT GVQNGSSLSI PSDIPIEISD
     ITPTDSSSSA VTISYENGSN KESIENIKYL TLVVFGLMMF M