RAB7_NEUCR
ID RAB7_NEUCR Reviewed; 205 AA.
AC Q9C2L8; Q7S7Y4;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ypt/Rab-type GTPase Rab7;
DE AltName: Full=Guanine triphosphate binding protein 14;
GN Name=gtp-14; ORFNames=17E5.300, NCU03711;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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.
CC {ECO:0000250|UniProtKB:P32939}.
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: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AL513467; CAC28856.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32251.1; -; Genomic_DNA.
DR RefSeq; XP_961487.1; XM_956394.2.
DR AlphaFoldDB; Q9C2L8; -.
DR SMR; Q9C2L8; -.
DR STRING; 5141.EFNCRP00000003431; -.
DR EnsemblFungi; EAA32251; EAA32251; NCU03711.
DR GeneID; 3877651; -.
DR KEGG; ncr:NCU03711; -.
DR VEuPathDB; FungiDB:NCU03711; -.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q9C2L8; -.
DR OMA; IQACPRD; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IBA:GO_Central.
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.
DR PROSITE; PS51419; RAB; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW Nucleotide-binding; Prenylation; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..205
FT /note="Ypt/Rab-type GTPase Rab7"
FT /id="PRO_0000121315"
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; 23128 MW; EFC8EBBAB6B89528 CRC64;
MSSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSASYKAT IGADFLTREV LVDDRQVTMQ
LWDTAGQERF QSLGVAFYRG ADCCVLVYDV NNSKSFDALD SWRDEFLIQA SPRDPDNFPF
VVLGNKIDME ESKRVISTKR AMTFCQSKGN IPYFETSAKE AINVEQAFEV IARNALMQEE
SEEFSGDFQD PINIHIENDR DGCAC
