REP1_USTMA
ID REP1_USTMA Reviewed; 652 AA.
AC Q99109; A0A0D1CMC1; Q4P7I9;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Repellent protein 1;
DE Contains:
DE RecName: Full=Rep1-1;
DE Contains:
DE RecName: Full=Rep1-2;
DE Contains:
DE RecName: Full=Rep1-3;
DE Contains:
DE RecName: Full=Rep1-4;
DE Contains:
DE RecName: Full=Rep1-5;
DE Contains:
DE RecName: Full=Rep1-6;
DE Contains:
DE RecName: Full=Rep1-7;
DE Contains:
DE RecName: Full=Rep1-8;
DE Contains:
DE RecName: Full=Rep1-9;
DE Contains:
DE RecName: Full=Rep1-10;
DE Contains:
DE RecName: Full=Rep1-C;
DE Flags: Precursor;
GN Name=REP1; ORFNames=UMAG_03924;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC49419.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MASS SPECTROMETRY.
RC STRAIN=FBD11 {ECO:0000312|EMBL:AAC49419.1};
RX PubMed=8861956; DOI=10.1002/j.1460-2075.1996.tb00802.x;
RA Woesten H.A.B., Bohlmann R., Eckerskorn C., Lottspeich F., Boelker M.,
RA Kahmann R.;
RT "A novel class of small amphipathic peptides affect aerial hyphal growth
RT and surface hydrophobicity in Ustilago maydis.";
RL EMBO J. 15:4274-4281(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Water-repellent structural protein required for surface
CC hydrophobicity and formation of aerial hyphae during filamentous
CC growth. {ECO:0000269|PubMed:8861956}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:8861956}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in filamentous form.
CC {ECO:0000269|PubMed:8861956}.
CC -!- MASS SPECTROMETRY: [Rep1-1]: Mass=3794.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8861956};
CC -!- MASS SPECTROMETRY: [Rep1-5]: Mass=3767.8; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8861956};
CC -!- MASS SPECTROMETRY: [Rep1-7]: Mass=4920.0; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8861956};
CC -!- MASS SPECTROMETRY: [Rep1-8]: Mass=3857.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8861956};
CC -!- MASS SPECTROMETRY: [Rep1-9]: Mass=3851.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8861956};
CC -!- MASS SPECTROMETRY: [Rep1-10]: Mass=3888.6; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8861956};
CC -!- MISCELLANEOUS: Regulated by the mating type loci.
CC {ECO:0000269|PubMed:8861956}.
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DR EMBL; U56826; AAC49419.1; -; Genomic_DNA.
DR EMBL; CM003150; KIS67868.1; -; Genomic_DNA.
DR PIR; S71753; S71753.
DR RefSeq; XP_011390397.1; XM_011392095.1.
DR AlphaFoldDB; Q99109; -.
DR STRING; 237631.Q99109; -.
DR EnsemblFungi; KIS67868; KIS67868; UMAG_03924.
DR GeneID; 23564245; -.
DR KEGG; uma:UMAG_03924; -.
DR VEuPathDB; FungiDB:UMAG_03924; -.
DR eggNOG; KOG1170; Eukaryota.
DR HOGENOM; CLU_483294_0_0_1; -.
DR InParanoid; Q99109; -.
DR OMA; SYYNGGH; -.
DR OrthoDB; 849227at2759; -.
DR Proteomes; UP000000561; Chromosome 11.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030446; C:hyphal cell wall; IDA:UniProtKB.
DR GO; GO:0005199; F:structural constituent of cell wall; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030448; P:hyphal growth; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..23
FT /evidence="ECO:0000255, ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022207"
FT PEPTIDE 24..57
FT /note="Rep1-1"
FT /evidence="ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022208"
FT PEPTIDE 60..113
FT /note="Rep1-2"
FT /evidence="ECO:0000269|PubMed:8861956,
FT ECO:0000303|PubMed:8861956"
FT /id="PRO_0000022209"
FT PEPTIDE 115..150
FT /note="Rep1-3"
FT /evidence="ECO:0000303|PubMed:8861956"
FT /id="PRO_0000022210"
FT PEPTIDE 154..188
FT /note="Rep1-4"
FT /evidence="ECO:0000269|PubMed:8861956,
FT ECO:0000303|PubMed:8861956"
FT /id="PRO_0000022211"
FT PEPTIDE 191..224
FT /note="Rep1-5"
FT /evidence="ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022212"
FT PEPTIDE 228..262
FT /note="Rep1-6"
FT /evidence="ECO:0000303|PubMed:8861956"
FT /id="PRO_0000022213"
FT PEPTIDE 266..310
FT /note="Rep1-7"
FT /evidence="ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022214"
FT PEPTIDE 313..346
FT /note="Rep1-8"
FT /evidence="ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022215"
FT PEPTIDE 350..384
FT /note="Rep1-9"
FT /evidence="ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022216"
FT PEPTIDE 387..421
FT /note="Rep1-10"
FT /evidence="ECO:0000269|PubMed:8861956"
FT /id="PRO_0000022217"
FT CHAIN 424..652
FT /note="Rep1-C"
FT /evidence="ECO:0000303|PubMed:8861956"
FT /id="PRO_0000022218"
FT REGION 452..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..504
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 652 AA; 71374 MW; 07B96277A2E496AB CRC64;
MPSKIALSIS VLTAALGMVS AAPHYEYKSY NAGHNVESVV ENKLVDASDL TLGVDILKRT
DYSACKKYVS SYNAGYNVYS INENKLIDLS DATVKLSLLT NNGRPVKTWN KAPRYCLEYI
KSYNGGHNVI IDNENKLIDL SGLNLGIDIL KRKAPEFSYY NPGHNVKSTT ENKLVDASDL
LANVNILSKR GDKYSYYNGG YNVESDTENK LIDLSGLLAN IDILKKRTGS QYSYYNGGHN
VESTNENKLV DASDLLANVD ILKKRGDKYT YYNGGHNIES TNENKLIDLS DLTANVGVLD
DVHVNIGLLD KRTDKYSYYD GGHNIELTNE NKLIDLSDLL ANVDVLKKRT DKFSYYNGGH
NVESDTQNKL IDVSHLTAIV NALSKRTDKY SYYNGGHNVE STNENKLIDL SDLTALVNVL
SKRSLKGYGS KIHARDISEE LYRRTNADED CTCVKKSKPT PPKQTVTKPS ADCDAPPAVT
PKPKPSTKPS PSPTTPPPSK DTSKPTTKPE PKPQPSDKPE PKPSDKPEPK PSDKPEPKPS
DKPEPTPSPK PTPPKVTCGT DEVYVDEGHN VVSKNSNKLL DLSNISINIG ILDGLFGGKK
SKEVAADSTC TSKQGCCVSK SVYYYNGGNN VQSSNENSGI DLSGLNLGLD IL
