RODL_EMENI
ID RODL_EMENI Reviewed; 157 AA.
AC P28346; C8V9N5; Q5ASC7;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Rodlet protein;
DE Flags: Precursor;
GN Name=rodA; ORFNames=AN8803;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2065971; DOI=10.1101/gad.5.7.1161;
RA Stringer M.A., Dean R.A., Sewall T.C., Timberlake W.E.;
RT "Rodletless, a new Aspergillus developmental mutant induced by directed
RT gene inactivation.";
RL Genes Dev. 5:1161-1171(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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 at about the time sterigmata appear
CC and remains at high levels throughout the final stages of conidiophore
CC formation and during spore differentiation and maturation.
CC -!- INDUCTION: By brlA.
CC -!- SIMILARITY: Belongs to the fungal hydrophobin family. {ECO:0000305}.
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DR EMBL; M61113; AAA33321.1; -; Genomic_DNA.
DR EMBL; AACD01000161; EAA60596.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF77990.1; -; Genomic_DNA.
DR PIR; A40323; A40323.
DR RefSeq; XP_682072.1; XM_676980.1.
DR AlphaFoldDB; P28346; -.
DR SMR; P28346; -.
DR STRING; 162425.CADANIAP00006259; -.
DR PRIDE; P28346; -.
DR EnsemblFungi; CBF77990; CBF77990; ANIA_08803.
DR EnsemblFungi; EAA60596; EAA60596; AN8803.2.
DR GeneID; 2868430; -.
DR KEGG; ani:AN8803.2; -.
DR VEuPathDB; FungiDB:AN8803; -.
DR eggNOG; ENOG502T10M; Eukaryota.
DR HOGENOM; CLU_106380_1_0_1; -.
DR InParanoid; P28346; -.
DR OMA; MTVKQAQ; -.
DR OrthoDB; 1513191at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IEA:InterPro.
DR GO; GO:0031160; C:spore wall; IDA:AspGD.
DR GO; GO:0005199; F:structural constituent of cell wall; IEA:InterPro.
DR GO; GO:0042243; P:asexual spore wall assembly; IMP:AspGD.
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; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..157
FT /note="Rodlet protein"
FT /id="PRO_0000013508"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..131
FT /evidence="ECO:0000250"
FT DISULFID 65..125
FT /evidence="ECO:0000250"
FT DISULFID 66..106
FT /evidence="ECO:0000250"
FT DISULFID 132..150
FT /evidence="ECO:0000250"
SQ SEQUENCE 157 AA; 15643 MW; 69F08B2C7ED28277 CRC64;
MKFSIAAAVV AFAASVAALP PAHDSQFAGN GVGNKGNSNV KFPVPENVTV KQASDKCGDQ
AQLSCCNKAT YAGDTTTVDE GLLSGALSGL IGAGSGAEGL GLFDQCSKLD VAVLIGIQDL
VNQKCKQNIA CCQNSPSSAD GNLIGVGLPC VALGSIL