RHOC_EMENI
ID RHOC_EMENI Reviewed; 280 AA.
AC Q96WY0; C8VKD2; Q5B9U3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=GTP-binding protein rhoC;
DE AltName: Full=Rho3 protein homolog;
DE Flags: Precursor;
GN Name=rhoC; ORFNames=AN2687;
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 [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 [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 51-280.
RA Guest G.M., Momany M.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC {ECO:0000305}.
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DR EMBL; AACD01000047; EAA63089.1; -; Genomic_DNA.
DR EMBL; AF379682; AAK55443.1; -; Genomic_DNA.
DR EMBL; BN001306; CBF84210.1; -; Genomic_DNA.
DR RefSeq; XP_660291.1; XM_655199.1.
DR AlphaFoldDB; Q96WY0; -.
DR SMR; Q96WY0; -.
DR STRING; 162425.CADANIAP00010429; -.
DR EnsemblFungi; CBF84210; CBF84210; ANIA_02687.
DR EnsemblFungi; EAA63089; EAA63089; AN2687.2.
DR GeneID; 2873818; -.
DR KEGG; ani:AN2687.2; -.
DR VEuPathDB; FungiDB:AN2687; -.
DR eggNOG; KOG0393; Eukaryota.
DR HOGENOM; CLU_041217_21_1_1; -.
DR InParanoid; Q96WY0; -.
DR OMA; NASYIEC; -.
DR OrthoDB; 1166960at2759; -.
DR Proteomes; UP000000560; Chromosome VI.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0000915; P:actomyosin contractile ring assembly; IMP:AspGD.
DR GO; GO:0030865; P:cortical cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:EnsemblFungi.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031991; P:regulation of actomyosin contractile ring contraction; IMP:AspGD.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0032955; P:regulation of division septum assembly; IEA:EnsemblFungi.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR003578; Small_GTPase_Rho.
DR PANTHER; PTHR24072; PTHR24072; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51420; RHO; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..277
FT /note="GTP-binding protein rhoC"
FT /id="PRO_0000198937"
FT PROPEP 278..280
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281267"
FT REGION 13..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 98..106
FT /note="Effector region"
FT /evidence="ECO:0000250"
FT BINDING 76..83
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 125..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183..186
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 277
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 277
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 280 AA; 31039 MW; 2AC4ACD4839B4FEC CRC64;
MSGSMYDDQY YATSRRHSLV TPPPSVAPRQ NRMRSQSVRV SNGTVSTDNS MSSGRVSEAT
NITQPPAYSK KFVVVGDGGC GKTCLLISYS QGYFPEKYVP TVFENYITQT LHRRSGKTVE
LALWDTAGQE EYDRLRPLSY PETDLLFVCF AIDCPASLEN VMDKWYPEVL HFCPTTPIIL
VGLKSDLRNK RTCIELLKTQ GLTPVTPEQG QAVAGRMNAS YVECSSKEMR GVDSVFQLAV
DTVVSLEEQN WDTRLPSSSG KPGGKPIGGK KIKKRSCKIL
