ID   CRYP_CRYPA              Reviewed;         118 AA.
AC   P52753;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Cryparin;
DE   Flags: Precursor;
GN   Name=CRP;
OS   Cryphonectria parasitica (Chestnut blight fungus) (Endothia parasitica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Diaporthales; Cryphonectriaceae;
OC   Cryphonectria-Endothia species complex; Cryphonectria.
OX   NCBI_TaxID=5116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-73.
RC   STRAIN=155/2;
RX   PubMed=8112589; DOI=10.1016/0378-1119(94)90523-1;
RA   Zhang L., Villalon D., Sun Y., Kazmierczak P., van Alfen N.K.;
RT   "Virus-associated down-regulation of the gene encoding cryparin, an
RT   abundant cell-surface protein from the chestnut blight fungus,
RT   Cryphonectria parasitica.";
RL   Gene 139:59-64(1994).
CC   -!- FUNCTION: Contributes to surface hydrophobicity, which is important for
CC       processes such as association of hyphae in reproductive structures,
CC       dispersal of aerial spores and adhesion of pathogens to host
CC       structures. Produced abundantly, except in the ds-RNA virus-infected
CC       strains, where the expression is much reduced.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted. Note=Cell wall of
CC       aerial hyphae and sporulation structures. Abundantly secreted.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed on day 2 and 3 after inoculation,
CC       a time when the fungus is in a rapid phase of growth. After a
CC       stationary phase on day 4, the expression decreases.
CC   -!- SIMILARITY: Belongs to the cerato-ulmin hydrophobin family.
CC       {ECO:0000305}.
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DR   EMBL; L09559; AAA19638.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P52753; -.
DR   SMR; P52753; -.
DR   OMA; LYTPQCC; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.20.120.10; -; 1.
DR   InterPro; IPR010636; Cerato-ulmin_hydrophobin.
DR   InterPro; IPR036686; Hydrophobin_sf.
DR   PANTHER; PTHR42341; PTHR42341; 1.
DR   Pfam; PF06766; Hydrophobin_2; 1.
DR   SUPFAM; SSF101751; SSF101751; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:8112589"
FT   CHAIN           23..118
FT                   /note="Cryparin"
FT                   /id="PRO_0000013518"
FT   REPEAT          29..30
FT                   /note="1"
FT   REPEAT          31..32
FT                   /note="2"
FT   REPEAT          33..34
FT                   /note="3"
FT   REPEAT          35..36
FT                   /note="4"
FT   REPEAT          37..38
FT                   /note="5"
FT   REPEAT          39..40
FT                   /note="6"
FT   REPEAT          41..42
FT                   /note="7"
FT   REGION          20..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          29..42
FT                   /note="7 X 2 AA tandem repeats of S-G"
FT   COMPBIAS        30..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   118 AA;  11387 MW;  F7C7CCEEA57D06A5 CRC64;
     MQFSIIAISF LASLAMASPA KRGGGGGGSG SGSGSGSGSG SGGGSTTYTA CSSTLYSEAQ
     CCATDVLGVA DLDCETVPET PTSASSFESI CATSGRDAKC CTIPLLGQAL LCQDPVGL