SC4_SCHCO
ID SC4_SCHCO Reviewed; 111 AA.
AC P16934;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Fruiting body protein SC4;
DE AltName: Full=Hydrophobin SC4;
DE Flags: Precursor;
GN Name=SC4;
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).
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: In solution, the protein monomers form rodlet-like and
CC insoluble aggregates.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall. Secreted. Note=Abundantly
CC secreted in aqueous environment.
CC -!- DEVELOPMENTAL STAGE: Is abundantly expressed and accumulates in the
CC walls of developing fruiting bodies (only in fruiting dikaryons).
CC -!- SIMILARITY: Belongs to the fungal hydrophobin family. {ECO:0000305}.
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DR EMBL; M32330; AAA33927.1; -; Genomic_DNA.
DR PIR; JH0183; JH0183.
DR AlphaFoldDB; P16934; -.
DR SMR; P16934; -.
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 2: Evidence at transcript level;
KW Cell wall; Disulfide bond; Fruiting body; Glycoprotein; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..111
FT /note="Fruiting body protein SC4"
FT /id="PRO_0000013514"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..37
FT /evidence="ECO:0000250"
FT DISULFID 38..72
FT /evidence="ECO:0000250"
FT DISULFID 86..92
FT /evidence="ECO:0000250"
FT DISULFID 93..106
FT /evidence="ECO:0000250"
SQ SEQUENCE 111 AA; 10730 MW; FEBEB2B2CAA846DF CRC64;
MRFSLALLAL PALAAAAPVP GGGKGAGQAC NSGPVQCCNE TTTVANAQKQ GLLGGLLGVV
VGPITGLVGL NCSPISVVGV LTGNSCTAQT VCCDHVTQNG LVNVGCTPIS L