ID   HWP2_CANAL              Reviewed;         908 AA.
AC   Q59PF9; A0A1D8PLU3;
DT   26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Hyphal wall protein 2;
DE   AltName: Full=GPI-anchored protein 8;
DE   Flags: Precursor;
GN   Name=HWP2; Synonyms=PGA8; OrderedLocusNames=CAALFM_C403510CA;
GN   ORFNames=CaO19.10888, CaO19.3380;
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=12492856; DOI=10.1046/j.1365-2958.2003.03300.x;
RA   Sohn K., Urban C., Brunner H., Rupp S.;
RT   "EFG1 is a major regulator of cell wall dynamics in Candida albicans as
RT   revealed by DNA microarrays.";
RL   Mol. Microbiol. 47:89-102(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=15814840; DOI=10.1091/mbc.e05-01-0073;
RA   Kadosh D., Johnson A.D.;
RT   "Induction of the Candida albicans filamentous growth program by relief of
RT   transcriptional repression: a genome-wide analysis.";
RL   Mol. Biol. Cell 16:2903-2912(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=19837954; DOI=10.1128/ec.00245-09;
RA   Ene I.V., Bennett R.J.;
RT   "Hwp1 and related adhesins contribute to both mating and biofilm formation
RT   in Candida albicans.";
RL   Eukaryot. Cell 8:1909-1913(2009).
RN   [8]
RP   FUNCTION.
RX   PubMed=19616419; DOI=10.1016/j.micres.2009.03.006;
RA   Hayek P., Dib L., Yazbeck P., Beyrouthy B., Khalaf R.A.;
RT   "Characterization of Hwp2, a Candida albicans putative GPI-anchored cell
RT   wall protein necessary for invasive growth.";
RL   Microbiol. Res. 165:250-258(2010).
RN   [9]
RP   FUNCTION.
RX   PubMed=20869222; DOI=10.1016/j.micres.2010.08.004;
RA   Younes S., Bahnan W., Dimassi H.I., Khalaf R.A.;
RT   "The Candida albicans Hwp2 is necessary for proper adhesion, biofilm
RT   formation and oxidative stress tolerance.";
RL   Microbiol. Res. 166:430-436(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=21602216; DOI=10.1099/mic.0.049395-0;
RA   Heilmann C.J., Sorgo A.G., Siliakus A.R., Dekker H.L., Brul S.,
RA   de Koster C.G., de Koning L.J., Klis F.M.;
RT   "Hyphal induction in the human fungal pathogen Candida albicans reveals a
RT   characteristic wall protein profile.";
RL   Microbiology 157:2297-2307(2011).
RN   [11]
RP   FUNCTION.
RX   PubMed=23558263; DOI=10.1099/mic.0.067249-0;
RA   Younes S., Khalaf R.;
RT   "The Candida albicans Hwp2p can complement the lack of filamentation of a
RT   Saccharomyces cerevisiae flo11 null strain.";
RL   Microbiology 159:1160-1164(2013).
CC   -!- FUNCTION: GPI-anchored cell wall protein required for mating
CC       efficiency, biofilm formation, adhesion, filamentous growth, and
CC       oxidative stress tolerance. Involved in normal disseminated infection
CC       in a mouse systemic candidiasis model. {ECO:0000269|PubMed:19616419,
CC       ECO:0000269|PubMed:19837954, ECO:0000269|PubMed:20869222,
CC       ECO:0000269|PubMed:23558263}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:21602216}. Membrane {ECO:0000269|PubMed:21602216};
CC       Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:21602216}. Note=localizes
CC       to the cell wall of hyphae.
CC   -!- INDUCTION: Expressed in hyphae. Regulated by the EFG1 and TUP1
CC       transcription factors. {ECO:0000269|PubMed:12492856,
CC       ECO:0000269|PubMed:15814840}.
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 (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; CP017626; AOW29109.1; -; Genomic_DNA.
DR   RefSeq; XP_711600.2; XM_706508.2.
DR   AlphaFoldDB; Q59PF9; -.
DR   BioGRID; 1229883; 12.
DR   PRIDE; Q59PF9; -.
DR   GeneID; 3646803; -.
DR   KEGG; cal:CAALFM_C403510CA; -.
DR   CGD; CAL0000197192; HWP2.
DR   VEuPathDB; FungiDB:C4_03510C_A; -.
DR   HOGENOM; CLU_322093_0_0_1; -.
DR   InParanoid; Q59PF9; -.
DR   OrthoDB; 1604754at2759; -.
DR   PHI-base; PHI:3511; -.
DR   PRO; PR:Q59PF9; -.
DR   Proteomes; UP000000559; Chromosome 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   1: Evidence at protein level;
KW   Cell adhesion; Cell wall; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..887
FT                   /note="Hyphal wall protein 2"
FT                   /id="PRO_0000422908"
FT   PROPEP          888..908
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000422909"
FT   REGION          110..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..844
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           887
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        449
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        634
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        684
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        764
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   908 AA;  93432 MW;  5E39CBCC9E0B01ED CRC64;
     MRFATTQLAT LACFILTAEA TFPLRGLFND APVDVDLGVY HEESGNNKEQ KVDGFNMSPN
     IKKRTNENNA ANVVSTNGGL FITSTKELKT TVVVTSCFNN VCSETSITTP KTAVTATTSK
     HSTSKPTYTT TSKHSTSHSS TPASTSKHST STSTHPATSE HSTSKSTHAT SSKHSTSKSS
     VSVTTSKHST HDTTSKSFVT PPASSTTSEH TKHKSHKPSK TVVTLTSCSN NACSQSEITT
     GAIVVTDKET VYTTYCPLTD TETETESTTA TTSKHSTHTT TSKHSSVEST SVTSSSKHSV
     SKSTDVTTSK HSSSESSHAT TMKHSTSKHS THATTSKHST TESTSGITSK HSTHATSSKY
     STVESSSSFA STSESSVPVS SSKSTTFESS ISTTTSKHLT LKSSTPASTL EYSTSIPPAP
     ATTSNSLSTK STTLTTISRS STSGSSVPNT TRESSTSTTT PNSSSSESKV SSAIPKYSSS
     EVSSSATTLK SYSTTHSIPT TLVYSSSTSL GFSVTEFRNL TTTSKSSLST STTELLTSGT
     TVRSSTSESS VTSATSIYTS SESTTSSEST TSIETPKSIA SKSSSSVTLP KSSTFAWSTS
     TTTPESSPIT LKLSTSKPPK PSATMESSAS TTKNSSIQST SEATTSGSSG VESSVLTATT
     KSSVPVTTSE WSSVVTTPKS SAPNTTLEHS TSASETSSGS VYTTFDQSTT VITVTSCSDN
     LCSKTEVTTG VTVITSDTTS YTTYCPLTGT TTVSSALESL VTANKSTSYV GATPIVSSVV
     STTPIISSAS TTPIISSAST TSVISSASTT SVISNAISNP VSTDVKPTTS SQGTKSTPVD
     TDSKSTSETT VMVYTTKSVT PTTVESISVA VSSAAQSSIA AISSYEGTGN NMKLSFGVVI
     AGVAAFAI