ID   HYP2_HYPJE              Reviewed;          86 AA.
AC   P79073;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Hydrophobin-2;
DE   AltName: Full=Hydrophobin II;
DE            Short=HFBII;
DE   Flags: Precursor;
GN   Name=hfb2;
OS   Hypocrea jecorina (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 16-35.
RC   STRAIN=ATCC 56765 / Rut C-30;
RX   PubMed=9346297; DOI=10.1111/j.1432-1033.1997.00415.x;
RA   Nakari-Setaelae T., Aro N., Ilmen M., Munoz G., Kalkkinen N., Penttilae M.;
RT   "Differential expression of the vegetative and spore-bound hydrophobins of
RT   Trichoderma reesei: cloning and characterization of the hfb2 gene.";
RL   Eur. J. Biochem. 248:415-423(1997).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 16-86, AND DISULFIDE BONDS.
RX   PubMed=14555650; DOI=10.1074/jbc.m309650200;
RA   Hakanpaa J., Paananen A., Askolin S., Nakari-Setaelae T., Parkkinen T.,
RA   Penttilae M., Linder M.B., Rouvinen J.;
RT   "Atomic resolution structure of the HFBII hydrophobin, a self-assembling
RT   amphiphile.";
RL   J. Biol. Chem. 279:534-539(2004).
CC   -!- FUNCTION: Responsible for spore hydrophobicity and protection.
CC   -!- SUBCELLULAR LOCATION: Spore wall. Secreted, cell wall.
CC   -!- DEVELOPMENTAL STAGE: Expressed during conidiation. No expression in
CC       vegetative or sporulating aerial hyphae.
CC   -!- INDUCTION: By C and N starvation, and by light.
CC   -!- PTM: Four disulfide bonds may be present.
CC   -!- SIMILARITY: Belongs to the cerato-ulmin hydrophobin family.
CC       {ECO:0000305}.
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DR   EMBL; Y11894; CAA72636.1; -; Genomic_DNA.
DR   PDB; 1R2M; X-ray; 1.00 A; A/B=16-86.
DR   PDB; 2B97; X-ray; 0.75 A; A/B=16-86.
DR   PDB; 2PL6; X-ray; 2.20 A; A/B/C/D/E/F/G/H=16-86.
DR   PDB; 2PL7; X-ray; 1.00 A; A/B=16-86.
DR   PDB; 3QQT; X-ray; 1.90 A; A/B=16-86.
DR   PDBsum; 1R2M; -.
DR   PDBsum; 2B97; -.
DR   PDBsum; 2PL6; -.
DR   PDBsum; 2PL7; -.
DR   PDBsum; 3QQT; -.
DR   AlphaFoldDB; P79073; -.
DR   SMR; P79073; -.
DR   VEuPathDB; FungiDB:TrQ_004956; -.
DR   OMA; PLCCATN; -.
DR   EvolutionaryTrace; P79073; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0031160; C:spore wall; 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   3D-structure; Cell wall; Direct protein sequencing; Disulfide bond;
KW   Secreted; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000269|PubMed:9346297"
FT   CHAIN           16..86
FT                   /note="Hydrophobin-2"
FT                   /id="PRO_0000013521"
FT   DISULFID        18..67
FT                   /evidence="ECO:0000269|PubMed:14555650"
FT   DISULFID        28..58
FT                   /evidence="ECO:0000269|PubMed:14555650"
FT   DISULFID        29..41
FT                   /evidence="ECO:0000269|PubMed:14555650"
FT   DISULFID        68..79
FT                   /evidence="ECO:0000269|PubMed:14555650"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:3QQT"
FT   STRAND          25..33
FT                   /evidence="ECO:0007829|PDB:2B97"
FT   TURN            34..36
FT                   /evidence="ECO:0007829|PDB:2B97"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:2B97"
FT   HELIX           51..60
FT                   /evidence="ECO:0007829|PDB:2B97"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:2B97"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:2B97"
SQ   SEQUENCE   86 AA;  8766 MW;  39EAD7D4E02698AB CRC64;
     MQFFAVALFA TSALAAVCPT GLFSNPLCCA TNVLDLIGVD CKTPTIAVDT GAIFQAHCAS
     KGSKPLCCVA PVADQALLCQ KAIGTF