FGR23_CANAL
ID FGR23_CANAL Reviewed; 1114 AA.
AC Q5AJV5; A0A1D8PJI3; Q5AJH8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Filamentous growth regulator 23;
DE AltName: Full=Predicted GPI-anchored protein 40;
DE Flags: Precursor;
GN Name=FGR23; Synonyms=PGA40; OrderedLocusNames=CAALFM_C302300WA;
GN ORFNames=CaO19.1616, CaO19.9183;
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 DISRUPTION PHENOTYPE.
RX PubMed=12773383; DOI=10.1093/emboj/cdg256;
RA Uhl M.A., Biery M., Craig N., Johnson A.D.;
RT "Haploinsufficiency-based large-scale forward genetic analysis of
RT filamentous growth in the diploid human fungal pathogen C.albicans.";
RL EMBO J. 22:2668-2678(2003).
RN [5]
RP INDUCTION.
RX PubMed=14585977; DOI=10.1128/mcb.23.22.8189-8201.2003;
RA Bennett R.J., Uhl M.A., Miller M.G., Johnson A.D.;
RT "Identification and characterization of a Candida albicans mating
RT pheromone.";
RL Mol. Cell. Biol. 23:8189-8201(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=21496229; DOI=10.1186/1471-2164-12-192;
RA Chaudhuri R., Ansari F.A., Raghunandanan M.V., Ramachandran S.;
RT "FungalRV: adhesin prediction and immunoinformatics portal for human fungal
RT pathogens.";
RL BMC Genomics 12:192-192(2011).
RN [8]
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 [9]
RP INDUCTION.
RX PubMed=21414038; DOI=10.1111/j.1365-2958.2011.07626.x;
RA Bonhomme J., Chauvel M., Goyard S., Roux P., Rossignol T., d'Enfert C.;
RT "Contribution of the glycolytic flux and hypoxia adaptation to efficient
RT biofilm formation by Candida albicans.";
RL Mol. Microbiol. 80:995-1013(2011).
CC -!- FUNCTION: Putative adhesin which may be involved in cell adhesion and
CC virulence (By similarity). Involved in the regulation of filamentous
CC growth. {ECO:0000250, ECO:0000269|PubMed:21496229}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- INDUCTION: Induced in biofilms and by alpha factor. Repressed by HAP43.
CC {ECO:0000269|PubMed:14585977, ECO:0000269|PubMed:21414038,
CC ECO:0000269|PubMed:21592964}.
CC -!- DISRUPTION PHENOTYPE: Affects filamentous growth.
CC {ECO:0000269|PubMed:12773383}.
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DR EMBL; CP017625; AOW28267.1; -; Genomic_DNA.
DR RefSeq; XP_721695.2; XM_716602.2.
DR AlphaFoldDB; Q5AJV5; -.
DR GeneID; 3636555; -.
DR KEGG; cal:CAALFM_C302300WA; -.
DR CGD; CAL0000178630; FGR23.
DR VEuPathDB; FungiDB:C3_02300W_A; -.
DR HOGENOM; CLU_281042_0_0_1; -.
DR PRO; PR:Q5AJV5; -.
DR Proteomes; UP000000559; Chromosome 3.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1089
FT /note="Filamentous growth regulator 23"
FT /id="PRO_0000424943"
FT PROPEP 1090..1114
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424944"
FT REGION 232..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1089
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1114 AA; 116305 MW; D38B9832E72FCA56 CRC64;
MFASYLLLVL WIIRLVPTTH AHTGNDAEYL LNTVLKRDAT SLSRNAYLDS EATSGATNYC
SDCDNDEVIV TVDGTSTIWT ILLDSTISTL VTTTSTEKTT LTSCGQSCTK SKDASSVSSS
SASSSTSRSL IFRTSTKTVT DTTTLPTVTE INTFTTTDSH IVLVYTDINS ESTITGDYTF
IKNKNTRTVI ITDYVTSTVG GETQIVTQTT TSVVYELVVT CPDHDFATTL TGSETFVPPT
TAPKPVETPS PEPSTTILSI KSESSVPSAT TSVLDTSITL ETSSSSIEFS TSTQESSSIG
PSSSSSIGSC TSSSISTEES LSTTKLSSSF TSISSWEELS SSFTQSTTSS NAEPSSSFAE
SFTTESLSST IEATSSMEDI SNNSVLTSSI FSETTTNESS SYTDEPSSSE EITNTYEPSS
STESSTTDQF SSLLSSSLPV TSTSSTTISS ATPITTVLST SITSQDTNCE ATITNISTNT
LIETITVNGN TTIYTETQLS TYLTSNTSIN CPNTNSATTT TTQVIPTATT EQIHTTTLNG
SIIVSTETAT LKTTVIITHC PECTNESSTS EYSSSLKAES SQQSIPTIES NLSELSVSST
LSLVESTASG KCSGLTTTTF TSIVSTTTES IYTITSNEST FEMTTTVTNI GTIVITTCPT
ITPVSSSYSS SESLSSSVST SLLTESNSTI SQSTVSTDKS SLTNDNQIST VSTETPLTSI
TIIETTSKTT ESLYTTTSND STHIFTTTII DVQTNTIVTC PTTTSTLTSS HTSDNEKPAS
LSSSSLIESD HIADGTTTST TFQSTSTTTV DHHCSSCSEI LLSTSSSIIG NKSTSTSISS
IETSASSSYH SSEPEVMSSS SSTSIKQSSD SIPSTSQTHV STTSSSVSSL ETTTTTTENS
PTSNGFSSSS IVTSVNVPDY VSSSVSSTSS TTSSPSTESS SNGLVSTVTE SSTANENTSE
ITTIDNTSIT SEKVTGTNSN PKTSEIIKDA TITTSGNVES LHSTTPISST SIISTNAISS
SDTTTLTITN TLTYSIDSIT TMKTSSITTA PPPPQQKESS SVLSSSLIIN SSTPTIIPTI
NIPITFEGNA NSLGLKNGDN SWIIGIMMIG LLMI
