IFF5_CANAL
ID IFF5_CANAL Reviewed; 1308 AA.
AC Q5A1E0; A0A1D8PMM4; Q5A1J8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cell wall protein IFF5;
DE AltName: Full=Adhesin-like protein IFF5;
DE Flags: Precursor;
GN Name=IFF5; OrderedLocusNames=CAALFM_C406550CA;
GN ORFNames=CaO19.10397, CaO19.2879;
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; CP017626; AOW29378.1; -; Genomic_DNA.
DR RefSeq; XP_715535.1; XM_710442.1.
DR AlphaFoldDB; Q5A1E0; -.
DR SMR; Q5A1E0; -.
DR STRING; 237561.Q5A1E0; -.
DR GeneID; 3642782; -.
DR KEGG; cal:CAALFM_C406550CA; -.
DR CGD; CAL0000184616; IFF5.
DR VEuPathDB; FungiDB:C4_06550C_A; -.
DR eggNOG; KOG1216; Eukaryota.
DR HOGENOM; CLU_006199_1_0_1; -.
DR OrthoDB; 1660355at2759; -.
DR PRO; PR:Q5A1E0; -.
DR Proteomes; UP000000559; Chromosome 4.
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 InterPro; IPR031573; Cell_wall_rpt.
DR InterPro; IPR021031; Hyphal-reg_cell_wall_N.
DR Pfam; PF11765; Hyphal_reg_CWP; 1.
DR Pfam; PF15789; Hyr1; 6.
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..1284
FT /note="Cell wall protein IFF5"
FT /id="PRO_0000424762"
FT PROPEP 1285..1308
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424763"
FT REGION 487..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1284
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 607
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1003
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1308 AA; 136893 MW; E4790EEEEBA56519 CRC64;
MKLFQNILIS IALLTQLIFA IEIAENKVDR GSITLNLGDI IIYTGATWSI IDNAYTNFVG
KLDVRADAGL YITSTSHLLA LQVSLTTILH SITNNGIISF DSRISRTSSS YDLRGISFTN
NGEMYFGSSG ESSSSTSLTS ASWSNTGLLS FFQNQRTSGT VNLGVSMGSI TNDGQICLNN
QVYEQTTQIK GSGCFTAKGD STIYIANVVL AVSSKQNFYL TDKGSSMIVQ AVSTTQTFNV
YGFGDGNKIG LTLPLVGTIF NSAFTYDTAS GILTLRNTLL EQKFNIGTGY EPSKFQVVTD
SGSGTPSTVL GSVAYYGHVP TRTLPKSCQI PCKPIPKAPG TQPTEYTTTI TKTNTAGNTV
TETGVVNIST DKAGSWFTTT SIFPTLTTAI AAPTSTAMST DLSSSVNIPV ETSSNESSSI
TLASSESSAV QTSSIEIPVS SHISANQESS SIGESSVNGS TMISSESALE SASEFTIAQS
SDVESYSSSE HSITHESSAI TSSSTTIETH VTESSVVVDS FTSDSLFVSE TQDPKASSFS
IVTPSDSIIV NESSIPELST SVGAVSTSTS SSEISSNSYF PSETHISKVS SSAEPTFVTP
SESIIINISE PAVSTDSVQP STEPQPDMSS VIAESLISST VSASEIELSS TMELSHSESL
LAKQSETINQ SESNYISETS AVPTAKSTIS DSKLTSTWES SSLVNMESTY SVVISESEIT
PIPVHTSESA TESAAESSDI QTQFTSTWTA TKSDGSFVTE SGVISQSGTS FTTIATFPPL
YTSSDITTEF ISTWTATNSD GSVTTEIGVV SQSGTSLTTI ATFPPSSTES GITSEFISTW
TTTSSDGSVA TKSGVVIQSG TSLTTIATFP PMSTSSDIIT EFTSTWTTTN SDGSITTESG
IVSQSGTSLT TLTIFEPVTS LAVPSYTVIE TEFTSTWTTT KSDGSIVTGS GIVSQSGTSL
TTLSTFAPSS SSSEIAPEFT STWEIGSSNE SNVVESSIVN QSNESLTNSV SSYEPATESA
IVSPSDQVLT SSATSFVSAS EFSAVTTTTV DSASASSSTD INNDVTVLVS PSESEINTSS
SIWNNENNVS GAVSTSESTS IANNHDGSLS MTKTESEING FYSTESSTMF VTATITSCNK
SDCFENVVTY VSNDSYTTVT TGHSNDNTSV DNNNVPSTLI ENVSNTETIP VVTNTEEVST
TVYNPLTSTS TSNIVESSNT SIVDNENNGV HINSDDMTAM VTAVETGNGI TNGTNFVSPS
TIPNEISETG SPATSIVGTL PYENGSNQLS IENIKYLILV VFGLMMIM
