ID   MESA_EMENI              Reviewed;         791 AA.
AC   Q5BGR2; C8VUD7; Q870E3;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Protein mesA;
GN   Name=mesA; ORFNames=AN0268;
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], FUNCTION, MUTAGENESIS OF GLY-93, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=ACP21;
RX   PubMed=15155805; DOI=10.1091/mbc.e03-11-0803;
RA   Pearson C.L., Xu K., Sharpless K.E., Harris S.D.;
RT   "MesA, a novel fungal protein required for the stabilization of polarity
RT   axes in Aspergillus nidulans.";
RL   Mol. Biol. Cell 15:3658-3672(2004).
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: Required for the formation of actin cables at hyphal tips.
CC       Involved in establishment and maintenance of hyphal polarity axes.
CC       Stabilizes the localization of the formin sepA at sites of polarized
CC       growth. {ECO:0000269|PubMed:15155805}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:15155805}. Note=Localizes to hyphal tips and sites
CC       of branch emergence.
CC   -!- SIMILARITY: Belongs to the AFI1/mesA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CBF89848.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA66141.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY267354; AAP31022.1; -; Genomic_DNA.
DR   EMBL; AACD01000005; EAA66141.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF89848.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_657872.1; XM_652780.1.
DR   AlphaFoldDB; Q5BGR2; -.
DR   STRING; 162425.CADANIAP00002456; -.
DR   PRIDE; Q5BGR2; -.
DR   EnsemblFungi; EAA66141; EAA66141; AN0268.2.
DR   GeneID; 2876042; -.
DR   KEGG; ani:AN0268.2; -.
DR   VEuPathDB; FungiDB:AN0268; -.
DR   eggNOG; ENOG502QQUZ; Eukaryota.
DR   HOGENOM; CLU_009044_0_0_1; -.
DR   InParanoid; Q5BGR2; -.
DR   OrthoDB; 811536at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0051666; P:actin cortical patch localization; IBA:GO_Central.
DR   GO; GO:0030010; P:establishment of cell polarity; IMP:AspGD.
DR   GO; GO:0030448; P:hyphal growth; IMP:AspGD.
DR   InterPro; IPR012860; Afi1_N.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   Pfam; PF07792; Afi1; 1.
DR   PROSITE; PS50211; DENN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..791
FT                   /note="Protein mesA"
FT                   /id="PRO_0000373999"
FT   DOMAIN          81..321
FT                   /note="uDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          361..506
FT                   /note="cDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          508..613
FT                   /note="dDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..601
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..190
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         93
FT                   /note="G->R: In mesA1; reduced function."
FT                   /evidence="ECO:0000269|PubMed:15155805"
FT   CONFLICT        133..134
FT                   /note="PL -> HK (in Ref. 1; AAP31022)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        510
FT                   /note="S -> T (in Ref. 1; AAP31022)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   791 AA;  87985 MW;  C75724F25F3C031A CRC64;
     MSIPLPIRTS DGTGNLSSSP PKSNGLPRLS PSPSFVQKHS PRSSDTSGLR RSASHHNARQ
     TFKQRRCKSQ YPRDSPERHV EFILVASFHI DRGPIMEHQY PGPISSDEGM LAELMLPDQT
     HVRSQDWTIF FLPLDTGGEG EEDDLAGENN KRKGKRNRVR SSSGDEGTSA DTNNESEVTE
     EEESSDEEDG GEGPPLMYVL NLVNTKQDNT VKRGAVVKAM AICTRHSFLH IYKPILLLAL
     EDYFKNPYPE TLETLYNAVN AMDLSPMPKL NLLERQILQA TNSKDMFIEK FEQMVQQRAI
     EDGENDIDED NPPSPRRGTA PRYTLPRDTH EFESKIIYND IPIPVKVPTV IWPEIVGDFS
     LVKLIQIFSA PHAASPQPFP LHPHLTTSGP LTHPIIVLVN AMLTQKRVVF LGHNRPSGEV
     AEAVLAACAL ASGGILRGFT RHAFPYTDLT KIDDLLRVPG FIAGVTNPTF ANHPEWWDVL
     CDLPTGRIKI SNHIEPAPVT DGQLYFQQQS PVSASGPNAD PTGDNLFMED VLRSIANRYG
     ENAIRAKWRA YITKFTRVAA AFEETVYGAS NIYIIGPNEE LSPDSPSGLQ SDPGDPTTIR
     GHGYVWPDEA SKQRELMASV SRIEGWRTTR SYYSFIQDIA AMYWPSRPIQ KPDLHHHHDR
     LRTLKLSAYE AGAIYLAFAH AIKDYAGICQ LLTVTPESQA GLFYLSMGLL HPDRNVREAT
     ADLLERIALH PAGRHFWAQL NRFAKTAYFR IKREKEAAGN SSPIVKSPSD SFGPQQSLVG
     VAISGVHSQG S