ID   SC3_SCHCO               Reviewed;         136 AA.
AC   P16933;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Fruiting body protein SC3;
DE   AltName: Full=Hydrophobin SC3;
DE   Flags: Precursor;
GN   Name=SC3;
OS   Schizophyllum commune (Split gill fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX   NCBI_TaxID=5334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2401401; DOI=10.1016/0378-1119(90)90180-y;
RA   Schuren F.H.J., Wessels J.G.H.;
RT   "Two genes specifically expressed in fruiting dikaryons of Schizophyllum
RT   commune: homologies with a gene not regulated by mating-type genes.";
RL   Gene 90:199-205(1990).
RN   [2]
RP   SEQUENCE REVISION.
RA   Schuren F.H.J.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 25-33.
RC   STRAIN=ATCC 44200 / CBS 341.81 / 4-39;
RX   PubMed=1770359; DOI=10.1099/00221287-137-10-2439;
RA   Wessels J.G.H., de Vries O.M.H., Asgeirsdottir S.A., Springer J.;
RT   "The thn mutation of Schizophyllum commune, which suppresses formation of
RT   aerial hyphae, affects expression of the Sc3 hydrophobin gene.";
RL   J. Gen. Microbiol. 137:2439-2445(1991).
RN   [4]
RP   DISULFIDE BONDS.
RX   PubMed=10829014; DOI=10.1074/jbc.m000691200;
RA   de Vocht M.L., Reviakine I., Woesten H.A.B., Brisson A., Wessels J.G.H.,
RA   Robillard G.T.;
RT   "Structural and functional role of the disulfide bridges in the hydrophobin
RT   SC3.";
RL   J. Biol. Chem. 275:28428-28432(2000).
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.
CC   -!- SUBUNIT: Homodimer; in solution, the protein monomers form rodlet-like
CC       and insoluble aggregates.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted. Note=Cell wall of
CC       aerial hyphae. Abundantly secreted from the tips of submerged hyphae.
CC   -!- DEVELOPMENTAL STAGE: Abundantly expressed during formation of fruiting
CC       bodies (expressed in monokaryons and dikaryons). Accumulates in the
CC       walls of the individually growing aerial mycelium.
CC   -!- SIMILARITY: Belongs to the fungal hydrophobin family. {ECO:0000305}.
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DR   EMBL; M32329; AAA96324.1; -; Genomic_DNA.
DR   PIR; JH0184; JH0184.
DR   AlphaFoldDB; P16933; -.
DR   SMR; P16933; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:InterPro.
DR   GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR   InterPro; IPR001338; Hydrophobin.
DR   InterPro; IPR019778; Hydrophobin_CS.
DR   Pfam; PF01185; Hydrophobin; 1.
DR   SMART; SM00075; HYDRO; 1.
DR   PROSITE; PS00956; HYDROPHOBIN; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Direct protein sequencing; Disulfide bond; Fruiting body;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1770359"
FT   CHAIN           25..136
FT                   /note="Fruiting body protein SC3"
FT                   /id="PRO_0000013513"
FT   DISULFID        56..63
FT                   /evidence="ECO:0000269|PubMed:10829014"
FT   DISULFID        64..97
FT                   /evidence="ECO:0000269|PubMed:10829014"
FT   DISULFID        110..116
FT                   /evidence="ECO:0000269|PubMed:10829014"
FT   DISULFID        117..130
FT                   /evidence="ECO:0000269|PubMed:10829014"
SQ   SEQUENCE   136 AA;  13431 MW;  A8F24588EB216CF6 CRC64;
     MFARLPVVFL YAFVAFGALV AALPGGHPGT TTPPVTTTVT VTTPPSTTTI AAGGTCTTGS
     LSCCNQVQSA SSSPVTALLG LLGIVLSDLN VLVGISCSPL TVIGVGGSGC SAQTVCCENT
     QFNGLINIGC TPINIL