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   27-MAR-2024, entry version 144.
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; 284812.Q9HDY0; -.
DR   MaxQB; Q9HDY0; -.
DR   PaxDb; 4896-SPAPB1A10-10c-1; -.
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; DCCVIVY; -.
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:1904262; P:negative regulation of TORC1 signaling; IMP: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   CDD; cd01862; Rab7; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR47981; RAB FAMILY; 1.
DR   PANTHER; PTHR47981:SF38; YPT_RAB-TYPE GTPASE YPT71; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00176; RAN; 1.
DR   SMART; SM00173; RAS; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//