YPT71_SCHPO
ID YPT71_SCHPO Reviewed; 208 AA.
AC Q9HDY0;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ypt/Rab-type GTPase ypt71;
GN Name=ypt71; ORFNames=SPAPB1A10.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19453973; DOI=10.1111/j.1600-0854.2009.00907.x;
RA Kashiwazaki J., Iwaki T., Takegawa K., Shimoda C., Nakamura T.;
RT "Two fission yeast rab7 homologs, ypt7 and ypt71, play antagonistic roles
RT in the regulation of vacuolar morphology.";
RL Traffic 10:912-924(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). Act antagonistically to ypt7 in regulating vacuolar
CC morphology, promoting vacuolar fission (PubMed:19453973).
CC {ECO:0000250|UniProtKB:P32939, ECO:0000269|PubMed:19453973}.
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 -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:19453973}.
CC -!- DISRUPTION PHENOTYPE: Contains large vacuoles.
CC {ECO:0000269|PubMed:19453973}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAC21483.1; -; Genomic_DNA.
DR RefSeq; NP_593524.1; NM_001018958.2.
DR AlphaFoldDB; Q9HDY0; -.
DR SMR; Q9HDY0; -.
DR BioGRID; 279833; 7.
DR STRING; 4896.SPAPB1A10.10c.1; -.
DR MaxQB; Q9HDY0; -.
DR PaxDb; Q9HDY0; -.
DR PRIDE; Q9HDY0; -.
DR EnsemblFungi; SPAPB1A10.10c.1; SPAPB1A10.10c.1:pep; SPAPB1A10.10c.
DR GeneID; 2543411; -.
DR KEGG; spo:SPAPB1A10.10c; -.
DR PomBase; SPAPB1A10.10c; ypt71.
DR VEuPathDB; FungiDB:SPAPB1A10.10c; -.
DR eggNOG; KOG0394; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; Q9HDY0; -.
DR OMA; FESVENW; -.
DR PhylomeDB; Q9HDY0; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8854214; TBC/RABGAPs.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR PRO; PR:Q9HDY0; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:PomBase.
DR GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central.
DR GO; GO:0005774; C:vacuolar membrane; EXP:PomBase.
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; ISO:PomBase.
DR GO; GO:0006897; P:endocytosis; ISO:PomBase.
DR GO; GO:0006896; P:Golgi to vacuole transport; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0061192; P:negative regulation of vacuole fusion, non-autophagic; IMP:PomBase.
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 GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport; Vacuole.
FT CHAIN 1..208
FT /note="Ypt/Rab-type GTPase ypt71"
FT /id="PRO_0000121314"
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 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT BINDING 158..160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32939"
FT MOD_RES 208
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT LIPID 206
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P36586"
FT LIPID 208
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P36586"
SQ SEQUENCE 208 AA; 23474 MW; 9B76A6881BC4F389 CRC64;
MSAQKRVFLK VVILGDSGVG KTCLMNQFVN QKFSREYKAT IGADFLTKDV VVDDKLVTLQ
LWDTAGQERF QSLGMAFYRG ADCCVIVYNV NNSKSFDSVE NWRQEFLYQT SQDECAFPFI
IVGNQIDKDA SKRAVSLHRA LDYCKSKHGS NMIHFEASAK ENTNVTDLFE TVSRLALENE
SSRDDFVNDF SEPLLLSKPL NNTSSCNC
