YPT7_SCHPO
ID YPT7_SCHPO Reviewed; 205 AA.
AC O94655;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ypt/Rab-type GTPase ypt7;
GN Name=ypt7; ORFNames=SPBC405.04c;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-190, AND FUNCTION.
RX PubMed=9443913; DOI=10.1016/s0960-9822(98)00060-8;
RA Bone N., Millar J.B.A., Toda T., Armstrong J.;
RT "Regulated vacuole fusion and fission in Schizosaccharomyces pombe: an
RT osmotic response dependent on MAP kinases.";
RL Curr. Biol. 8:135-144(1998).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16357443; DOI=10.1247/csf.30.43;
RA Kashiwazaki J., Nakamura T., Iwaki T., Takegawa K., Shimoda C.;
RT "A role for fission yeast Rab GTPase Ypt7p in sporulation.";
RL Cell Struct. Funct. 30:43-49(2005).
RN [4]
RP FUNCTION.
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). Ypt7 is necessary for trafficking from the endosome to the
CC vacuole and for homotypic vacuole fusion (PubMed:9443913,
CC PubMed:19453973). Plays an important role in sporulation
CC (PubMed:16357443). {ECO:0000250|UniProtKB:P32939,
CC ECO:0000269|PubMed:16357443, ECO:0000269|PubMed:19453973,
CC ECO:0000269|PubMed:9443913}.
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:0000250|UniProtKB:P32939}.
CC -!- DISRUPTION PHENOTYPE: Asci produce less than 4 spores, which are
CC immature and germinate at low frequency. Cells are defective in
CC development of the forespore membranes. {ECO:0000269|PubMed:16357443}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB38603.1; -; Genomic_DNA.
DR PIR; T40425; T40425.
DR RefSeq; NP_596307.1; NM_001022229.2.
DR AlphaFoldDB; O94655; -.
DR SMR; O94655; -.
DR BioGRID; 277283; 4.
DR STRING; 4896.SPBC405.04c.1; -.
DR iPTMnet; O94655; -.
DR MaxQB; O94655; -.
DR PaxDb; O94655; -.
DR PRIDE; O94655; -.
DR EnsemblFungi; SPBC405.04c.1; SPBC405.04c.1:pep; SPBC405.04c.
DR GeneID; 2540763; -.
DR KEGG; spo:SPBC405.04c; -.
DR PomBase; SPBC405.04c; ypt7.
DR VEuPathDB; FungiDB:SPBC405.04c; -.
DR eggNOG; KOG0394; Eukaryota.
DR HOGENOM; CLU_041217_10_6_1; -.
DR InParanoid; O94655; -.
DR OMA; IQACPRD; -.
DR PhylomeDB; O94655; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8854214; TBC/RABGAPs.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR Reactome; R-SPO-9013405; RHOD GTPase cycle.
DR PRO; PR:O94655; -.
DR Proteomes; UP000002485; Chromosome II.
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: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; TAS:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0006896; P:Golgi to vacuole transport; ISS:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0061191; P:positive regulation of vacuole fusion, non-autophagic; IMP:PomBase.
DR GO; GO:0032889; P:regulation of vacuole fusion, non-autophagic; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:PomBase.
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..205
FT /note="Ypt/Rab-type GTPase ypt7"
FT /id="PRO_0000121313"
FT MOTIF 37..45
FT /note="Effector region"
FT /evidence="ECO:0000305"
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; 22994 MW; B63D9B5A019FBA32 CRC64;
MAGKKKHLLK VIILGESGVG KTSIMNQYVN RKFSKDYKAT IGADFLTKEV LVDDKVVTLQ
LWDTAGQERF QSLGVAFYRG ADCCVLVYDV NNSKSFETLD SWRDEFLIQA SPSNPETFPF
ILLGNKVDVE EQKRMVSKSK ALAFCQARGE IPYFETSAKE AINVQEAFET VAKLALENMD
SDDIAADFTD PIHLDMESQK TSCYC
