HWP1_CANAW
ID HWP1_CANAW Reviewed; 633 AA.
AC C4YHA6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Hyphal wall protein 1 {ECO:0000250|UniProtKB:P46593};
DE Flags: Precursor;
GN Name=HWP1 {ECO:0000250|UniProtKB:P46593}; ORFNames=CAWG_03451;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Major hyphal cell wall protein which plays a role of adhesin
CC and is required for mating, normal hyphal development, cell-to-cell
CC adhesive functions necessary for biofilm integrity, attachment to host,
CC and virulence. Promotes interactions with host and bacterial molecules,
CC thus leading to effective colonization within polymicrobial
CC communities. Plays a crucial role in gastrointestinal colonization, in
CC mucosal symptomatic and asymptomatic infections, in vaginitis, as well
CC as in lethal oroesophageal candidiasis, caused by the combined action
CC of fungal virulence factors and host inflammatory responses when
CC protective immunity is absent. {ECO:0000250|UniProtKB:P46593}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000250|UniProtKB:P46593}. Membrane; Lipid-anchor, GPI-anchor
CC {ECO:0000250|UniProtKB:P46593}.
CC -!- DEVELOPMENTAL STAGE: Found in hyphal but not yeast forms.
CC {ECO:0000250|UniProtKB:P46593}.
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 {ECO:0000250|UniProtKB:P46593}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P46593}.
CC -!- MISCELLANEOUS: As a major cell surface protein expressed during
CC infection, HWP1 detection can be used for diagnosis of invasive
CC candidiasis. HWP1 epitopes can also be used to develop vaccines for
CC protection against candidiasis. {ECO:0000250|UniProtKB:P46593}.
CC -!- SIMILARITY: Belongs to the HWP1 family. {ECO:0000305}.
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DR EMBL; CH672349; EEQ45138.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YHA6; -.
DR STRING; 5476.C4YHA6; -.
DR EnsemblFungi; EEQ45138; EEQ45138; CAWG_03451.
DR VEuPathDB; FungiDB:CAWG_03451; -.
DR HOGENOM; CLU_033728_0_0_1; -.
DR OMA; EPCDYPQ; -.
DR Proteomes; UP000001429; Chromosome 4, Supercontig 1.4.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR025928; Flocculin_t3_rpt.
DR Pfam; PF13928; Flocculin_t3; 2.
PE 3: Inferred from homology;
KW Cell adhesion; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..612
FT /note="Hyphal wall protein 1"
FT /id="PRO_0000434105"
FT PROPEP 613..633
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P46593"
FT /id="PRO_0000434106"
FT REPEAT 46..58
FT /note="1; approximate"
FT /evidence="ECO:0000305"
FT REPEAT 59..69
FT /note="2; approximate"
FT /evidence="ECO:0000305"
FT REPEAT 70..81
FT /note="3; approximate"
FT /evidence="ECO:0000305"
FT REPEAT 82..91
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 92..101
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 102..111
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 112..121
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 122..131
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 132..141
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 142..151
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 152..161
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 162..171
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 172..179
FT /note="13; truncated"
FT /evidence="ECO:0000305"
FT REPEAT 180..187
FT /note="14; truncated"
FT /evidence="ECO:0000305"
FT REGION 40..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..187
FT /note="14 X 10 AA tandem repeats of [EVIQ]-P-[CDT]-D-[YNW]-
FT P-[PQ]-[QI]-[QP]-[QDN]"
FT /evidence="ECO:0000305"
FT REGION 411..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 612
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000250|UniProtKB:P46593"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 633 AA; 65327 MW; 3C27A16BAF2CE59B CRC64;
MRLSTAQLIA IAYYMLSIGA TVPQVDGQGE TEEALIQKRS YDYYQEPCDD YPQQQQQQEP
CDYPQQQQQE EPCDYPQQQP QEPCDYPQQP QEPCDYPQQP QEPCDYPQQP QEPCDNPPQP
DVPCDNPPQP DVPCDNPPQP DIPCDNPPQP DIPCDNPPQP DQPDDNPPIP NIPTDWIPNI
PTDWIPDIPE KPTTPATTPN IPATTTTSES SSSSSSSSST TPKTSASTTP ESSVPATTPN
TSVPTTSSES TTPATSPESS VPVTSGSSIL TTTSESSSAP ATTPNTSVPT TTTEAKSSST
PLTTTTEHDT TVVTVTSCSN SVCTESEVTT GVIVITSKDT IYTTYCPLTE TTPVSTAPAT
ETPTGTVSTS TEQSTTVITV TSCSESSCTE SEVTTGVVVV TSEETVYTTF CPLTENTPGT
DSTPEASIPP METIPAGSEP SMPAGETSPA VPKPEVPATE SAPVPEMTPA GSQPSMPAGE
TSPAVPKSDV SATESAPAPE MTPAGTETKP AAPKSSAPAT EPSPVAPGTE SAPAGPGASS
SPKSSVLASE TSPIAPGAET APAGSSGAIT IPESSAVVST TEGAIPTTLE SVPLMQPSAN
YSSVAPISTF EGAGNNMRLT FGAAIIGIAA FLI
