HYR3_CANAL
ID HYR3_CANAL Reviewed; 1249 AA.
AC Q59XA7; A0A1D8PN06;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Hyphally regulated cell wall protein 3;
DE AltName: Full=Adhesin-like protein HYR3;
DE Flags: Precursor;
GN Name=HYR3; Synonyms=IFF2; OrderedLocusNames=CAALFM_C500730WA;
GN ORFNames=CaO19.575, CaO19.8206;
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 INDUCTION.
RX PubMed=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA Newport G., Agabian N.;
RT "Regulatory networks affected by iron availability in Candida albicans.";
RL Mol. Microbiol. 53:1451-1469(2004).
RN [6]
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 [7]
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 -!- INDUCTION: Induced in high iron conditions.
CC {ECO:0000269|PubMed:15387822}.
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; AOW29515.1; -; Genomic_DNA.
DR RefSeq; XP_714203.1; XM_709110.2.
DR AlphaFoldDB; Q59XA7; -.
DR STRING; 237561.Q59XA7; -.
DR GeneID; 3644119; -.
DR KEGG; cal:CAALFM_C500730WA; -.
DR CGD; CAL0000179043; HYR3.
DR VEuPathDB; FungiDB:C5_00730W_A; -.
DR eggNOG; KOG1075; Eukaryota.
DR HOGENOM; CLU_006199_0_0_1; -.
DR InParanoid; Q59XA7; -.
DR OrthoDB; 1483197at2759; -.
DR PRO; PR:Q59XA7; -.
DR Proteomes; UP000000559; Chromosome 5.
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; 4.
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..1225
FT /note="Hyphally regulated cell wall protein 3"
FT /id="PRO_0000424754"
FT PROPEP 1226..1249
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424755"
FT REGION 383..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..1217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 1225
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 891
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 940
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 960
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 984
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
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 1010
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1014
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1018
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1022
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1032
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1046
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1050
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1058
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1062
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1086
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1098
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1249 AA; 123069 MW; AA0FB5AD92818CFA CRC64;
MHLFKRIALT LWLIISSTLA VVITEDRVDR GTISVNLGEV TVNSGASWSI INNAVTAFAG
KINVQSGGGL YISSTSPLLA LQVTLTSLLD SITNDGVISL DSRASLTASN YNLIGLSFTN
NGEMYLAASG VLPSTMDLTA ASWTNNGLIV AYQNQRSSGV LNLGTPLGAI TNNGQICLYN
QVYQQQTRIE GSGCITANKN SAIYISNAVL PVATTQNFYL QDSKSSMIVQ AVSSTQTFNV
YGFGNGNKIG ITLPAVGIPP NPAYSYDVDT GILTVRAGLL SQKFNIGLGY YSLFFSVVTD
NGAGLPSTIL GSISYSGPVP SRNLPASCKI ACKPVPTAPG TNPTEYTTTI TTTNSAGNPL
TETGVVDIST DSNGSWFTTT SIFPTTSQSS SSETVASSSQ PDSSSTEPSA FPSSTGDSSA
EPSITSDYSS SELSVVPSSA SESASESSAE PSSASESASE SGSESVASET SASESASEQS
STSESVSSEF ASSDSSSEPS SASESSVESS SASEFVVPSS ATETSVSESA SESSAEPSSA
SESVASESAV SETSASESAA PSSASETSVS ESAASSSASE SFASESSVES SAVPSSASEF
STSESVASET PASETPASET PASESASEQS STSESSAEIS SASESSAEPS SAKSAISESA
SEFSAAPSSA SQSSASQSST NESSSQQSSA ESSSTGTSSV SASAATSEYT ATWTTTNSDG
SVSTESGIIS QSGSSFTTIT TFVPDATSEY TTTWTTTNSD GSVSTESGIV SQSGSSFTTI
TTFAPDATSE YTTTWTTTNS DGSVSTESGV VSQSGTSLTT ITTFAPDVTS EYTTTWTTTN
SDGSVSTESG IVSQSGSSFT TITTFEPPVV CKRDDVNCGS SIGLSTPYYG NSSQPLSSTK
MTDTSATQTV DSSLSSITDA TTTQSVNSLE TPVPTSGSGN GSNNGSDNGS NNGSNNGSNN
GSGSGNGSNN GSNNGSGSGN GFNNGSDNGS NNGSGNASNN GSASGSGSDN GSDNGSDNGS
DNGSNNGSNT DNGSNSGSDS GNGIDNGSGN GSSDGSDNGT TNGSGSGGES NNGSGNGSDN
GSSPDNGSNN GSNNGSNNGS GDGIGTGSNS DTDNGSGNGS NNGSGSVNGS ANGSGNGSNN
GSNSGSNSDN GSNNSSGNGS SSDLGSVSGT GNGSNEGSSN ESGANNGSNN GAGALPAATL
SVVPSPSADS GSTSSASAMV IPNTNGSGKL LNGKVLTLSV LSSMVVVFL
