RAB7_GIBZE
ID RAB7_GIBZE Reviewed; 205 AA.
AC I1RMF2;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Ypt/Rab-type GTPase Rab7;
GN Name=RAB7; ORFNames=FG05141.1, FGRAMPH1_01T17199;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26177389; DOI=10.1111/1462-2920.12982;
RA Zheng H., Zheng W., Wu C., Yang J., Xi Y., Xie Q., Zhao X., Deng X., Lu G.,
RA Li G., Ebbole D., Zhou J., Wang Z.;
RT "Rab GTPases are essential for membrane trafficking-dependent growth and
RT pathogenicity in Fusarium graminearum.";
RL Environ. Microbiol. 17:4580-4599(2015).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30044782; DOI=10.1371/journal.pgen.1007546;
RA Zheng H., Miao P., Lin X., Li L., Wu C., Chen X., Abubakar Y.S.,
RA Norvienyeku J., Li G., Zhou J., Wang Z., Zheng W.;
RT "Small GTPase Rab7-mediated FgAtg9 trafficking is essential for autophagy-
RT dependent development and pathogenicity in Fusarium graminearum.";
RL PLoS Genet. 14:E1007546-E1007546(2018).
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). RAB7 regulates the fusion of vacuoles and autophagosomes
CC (PubMed:26177389). Required for ATG9 trafficking (PubMed:30044782).
CC {ECO:0000250|UniProtKB:P32939, ECO:0000269|PubMed:26177389,
CC ECO:0000269|PubMed:30044782}.
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by guanine nucleotide-
CC exchange factors (GEFs), and inactivated by GTPase-activating proteins
CC (GAPs). {ECO:0000250|UniProtKB:P32939}.
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:30044782}; Lipid-anchor {ECO:0000305}. Vacuole
CC membrane {ECO:0000269|PubMed:26177389}; Lipid-anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; HG970334; CEF86602.1; -; Genomic_DNA.
DR RefSeq; XP_011323641.1; XM_011325339.1.
DR AlphaFoldDB; I1RMF2; -.
DR SMR; I1RMF2; -.
DR STRING; 5518.FGSG_05141P0; -.
DR GeneID; 23552334; -.
DR KEGG; fgr:FGSG_05141; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G17199; -.
DR eggNOG; KOG0394; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; I1RMF2; -.
DR Proteomes; UP000070720; Chromosome 3.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; 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 Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
PE 3: Inferred from homology;
KW Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Reference proteome; Vacuole.
FT CHAIN 1..205
FT /note="Ypt/Rab-type GTPase Rab7"
FT /id="PRO_0000451055"
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"
SQ SEQUENCE 205 AA; 23017 MW; 9B172F1BF136E537 CRC64;
MSSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSASYKAT IGADFLTREV LVDDRQVTMQ
LWDTAGQERF QSLGVAFYRG ADCCVLVYDV NNAKSFEALD SWRDEFLIQA SPRDPPNFPF
VVLGNKIDVE ESKRVISNKR AMTFCQSKGD IPYFETSAKE AINIDQAFEV IARNALAQEE
SEEFSGDFDD PINIHIENDR DGCAC
