RODL_NEUCR
ID RODL_NEUCR Reviewed; 108 AA.
AC Q04571; Q2XN72; Q7SC53;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Hydrophobin;
DE AltName: Full=Blue light-induced protein 7;
DE AltName: Full=Clock-controlled gene protein 2;
DE AltName: Full=Rodlet protein;
DE Flags: Precursor;
GN Name=eas; Synonyms=bli-7, ccg-2; ORFNames=NCU08457;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=1459459; DOI=10.1101/gad.6.12a.2373;
RA Lauter F.-R., Russo V.E.A., Yanofsky C.;
RT "Developmental and light regulation of eas, the structural gene for the
RT rodlet protein of Neurospora.";
RL Genes Dev. 6:2373-2381(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=1459460; DOI=10.1101/gad.6.12a.2382;
RA Bell-Pedersen D., Dunlap J.C., Loros J.J.;
RT "The Neurospora circadian clock-controlled gene, ccg-2, is allelic to eas
RT and encodes a fungal hydrophobin required for formation of the conidial
RT rodlet layer.";
RL Genes Dev. 6:2382-2394(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1472707; DOI=10.3109/10425179209034009;
RA Eberle J., Russo V.E.A.;
RT "Neurospora crassa blue-light-inducible gene bli-7 encodes a short
RT hydrophobic protein.";
RL DNA Seq. 3:131-141(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [5]
RP STRUCTURE BY NMR OF 27-108, AND DISULFIDE BONDS.
RX PubMed=16537446; DOI=10.1073/pnas.0505704103;
RA Kwan A.H., Winefield R.D., Sunde M., Matthews J.M., Haverkamp R.G.,
RA Templeton M.D., Mackay J.P.;
RT "Structural basis for rodlet assembly in fungal hydrophobins.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3621-3626(2006).
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. Important for the formation of hydrophobic rodlet layers of
CC asexually-produced spores.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC -!- DEVELOPMENTAL STAGE: Accumulates during conidiation but not during
CC germination.
CC -!- INDUCTION: Expression is controlled by blue light and by a circadian
CC clock. Also induced by glucose, nitrogen and carbon starvation.
CC -!- SIMILARITY: Belongs to the fungal hydrophobin family. {ECO:0000305}.
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DR EMBL; X67339; CAA47754.1; -; mRNA.
DR EMBL; S50953; AAA12691.1; -; Genomic_DNA.
DR EMBL; X62170; CAA44101.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA34064.1; -; Genomic_DNA.
DR PIR; A46222; A46222.
DR RefSeq; XP_963300.1; XM_958207.3.
DR PDB; 2FMC; NMR; -; A=27-108.
DR PDB; 2K6A; NMR; -; A=27-108.
DR PDB; 2LFN; NMR; -; A=27-108.
DR PDB; 4BWH; NMR; -; A=87-105.
DR PDBsum; 2FMC; -.
DR PDBsum; 2K6A; -.
DR PDBsum; 2LFN; -.
DR PDBsum; 4BWH; -.
DR AlphaFoldDB; Q04571; -.
DR SMR; Q04571; -.
DR STRING; 5141.EFNCRP00000008485; -.
DR EnsemblFungi; EAA34064; EAA34064; NCU08457.
DR GeneID; 3879448; -.
DR KEGG; ncr:NCU08457; -.
DR VEuPathDB; FungiDB:NCU08457; -.
DR HOGENOM; CLU_168414_0_0_1; -.
DR InParanoid; Q04571; -.
DR OMA; CCNSEPP; -.
DR EvolutionaryTrace; Q04571; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:InterPro.
DR GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.20.120.10; -; 1.
DR InterPro; IPR001338; Hydrophobin.
DR InterPro; IPR019778; Hydrophobin_CS.
DR InterPro; IPR036686; Hydrophobin_sf.
DR SMART; SM00075; HYDRO; 1.
DR PROSITE; PS00956; HYDROPHOBIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Cell wall biogenesis/degradation; Disulfide bond;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..108
FT /note="Hydrophobin"
FT /id="PRO_0000013509"
FT DISULFID 35..86
FT /evidence="ECO:0000269|PubMed:16537446"
FT DISULFID 44..80
FT /evidence="ECO:0000269|PubMed:16537446"
FT DISULFID 45..71
FT /evidence="ECO:0000269|PubMed:16537446"
FT DISULFID 87..106
FT /evidence="ECO:0000269|PubMed:16537446"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2K6A"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2FMC"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:2FMC"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:2K6A"
FT STRAND 79..88
FT /evidence="ECO:0007829|PDB:2FMC"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2FMC"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2FMC"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:2K6A"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2FMC"
SQ SEQUENCE 108 AA; 10876 MW; 7BB75992A9C173E9 CRC64;
MQFTSVFTIL AIAMTAAAAP AEVVPRATTI GPNTCSIDDY KPYCCQSMSG PAGSPGLLNL
IPVDLSASLG CVVGVIGSQC GASVKCCKDD VTNTGNSFLI INAANCVA
