YPT7_EMENI
ID YPT7_EMENI Reviewed; 205 AA.
AC C8VQY7; Q5BH91; Q8TGD9;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Ypt/Rab-type GTPase avaA {ECO:0000305};
DE AltName: Full=Aspergillus vacuolar morphology protein A {ECO:0000303|PubMed:12095681};
DE AltName: Full=YPT7 homolog avaA {ECO:0000303|PubMed:12095681};
GN Name=avaA {ECO:0000303|PubMed:12095681}; ORFNames=AN0089, ANIA_00089;
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, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF THR-22 AND GLN-67.
RC STRAIN=FGSC A26 / ATCC 24756 / JCM 19074 / M804;
RX PubMed=12095681; DOI=10.1016/s0378-1119(02)00626-1;
RA Ohsumi K., Arioka M., Nakajima H., Kitamoto K.;
RT "Cloning and characterization of a gene (avaA) from Aspergillus nidulans
RT encoding a small GTPase involved in vacuolar biogenesis.";
RL Gene 291:77-84(2002).
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: Ypt/Rab-type GTPases are key regulators of membrane
CC trafficking and intracellular vesicular transport. They act as
CC molecular switches that convert between GTP-bound and GDP-bound states,
CC and regulate virtually all steps of membrane traffic from the formation
CC of the transport vesicle at the donor membrane to its fusion at the
CC target membrane. In the GDP-bound state, Ypt proteins are predominantly
CC cytosolic, solubilized through the interaction with a GDP dissociation
CC inhibitor (GDI). In the GTP-bound state, the proteins are membrane
CC bound and interact with specific effector proteins that select cargo,
CC promote vesicle movement, or verify the correct site of fusion (By
CC similarity). AvaA functions in vacuolar biogenesis (PubMed:12095681).
CC {ECO:0000250|UniProtKB:P32939, ECO:0000269|PubMed:12095681}.
CC -!- ACTIVITY REGULATION: Rab activation is generally mediated by a guanine
CC exchange factor (GEF), while inactivation through hydrolysis of bound
CC GTP is catalyzed by a GTPase activating protein (GAP).
CC {ECO:0000250|UniProtKB:P32939}.
CC -!- DISRUPTION PHENOTYPE: Displays highly fragmented vacuoles.
CC {ECO:0000269|PubMed:12095681}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA65267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB072431; BAB88682.1; -; Genomic_DNA.
DR EMBL; BN001308; CBF90222.1; -; Genomic_DNA.
DR EMBL; AACD01000003; EAA65267.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_657693.1; XM_652601.1.
DR AlphaFoldDB; C8VQY7; -.
DR SMR; C8VQY7; -.
DR STRING; 162425.CADANIAP00002661; -.
DR EnsemblFungi; CBF90222; CBF90222; ANIA_00089.
DR EnsemblFungi; EAA65267; EAA65267; AN0089.2.
DR GeneID; 2875868; -.
DR KEGG; ani:AN0089.2; -.
DR VEuPathDB; FungiDB:AN0089; -.
DR eggNOG; KOG0394; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; C8VQY7; -.
DR OMA; IQACPRD; -.
DR OrthoDB; 1172019at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; IDA:AspGD.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007032; P:endosome organization; IMP:AspGD.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IBA:GO_Central.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:AspGD.
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 Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Lipoprotein; Methylation; Nucleotide-binding; Prenylation;
KW Reference proteome.
FT CHAIN 1..205
FT /note="Ypt/Rab-type GTPase avaA"
FT /id="PRO_0000451056"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT BINDING 17..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT BINDING 33..40
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT BINDING 66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT BINDING 125..128
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT BINDING 157..159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT MOD_RES 205
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT LIPID 203
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT LIPID 205
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT MUTAGEN 22
FT /note="T->N: Constitutively in the GDP-bound conformation.
FT Causes loss of function during vacuolar morphogenesis."
FT /evidence="ECO:0000269|PubMed:12095681"
FT MUTAGEN 67
FT /note="Q->L: Constitutively in the GTP-bound conformation.
FT Promotes vacuolar fusion resulting in large swollen
FT vacuoles."
FT /evidence="ECO:0000269|PubMed:12095681"
SQ SEQUENCE 205 AA; 22941 MW; 0E927E2D76F6BB32 CRC64;
MSSRKKVMLK VIILGDSGVG KTSLMNQYVN KKFSGSYKAT IGADFLTKEV LVDDRLVTMQ
IWDTAGQERF QSLGVAFYRG ADCCVLVYDV NNSKSFEALD SWRDEFLIQA SPRDPESFPF
VVIGNKIDME ESKRMISSKR AMTFCQSKGN IPYFETSAKE AVNVEQAFEV IARSALAQEE
AEEYGGDYTD PINIHDTTER DGCAC
