YPT2_SCHPO
ID YPT2_SCHPO Reviewed; 200 AA.
AC P17609;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=GTP-binding protein ypt2;
DE AltName: Full=SEC4 homolog;
GN Name=ypt2; ORFNames=SPAC9E9.07c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=2112089; DOI=10.1002/j.1460-2075.1990.tb08323.x;
RA Hengst L., Lehmeier T., Gallwitz D.;
RT "Structural and functional analysis of ypt2, an essential ras-related gene
RT in the fission yeast Schizosaccharomyces pombe encoding a Sec4 protein
RT homologue.";
RL EMBO J. 9:1957-1962(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2115995; DOI=10.1093/nar/18.14.4264;
RA Fawell E., Hook S., Sweet D., Armstrong J.;
RT "Novel YPT1-related genes from Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 18:4264-4264(1990).
RN [3]
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).
CC -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- MISCELLANEOUS: This protein is essential for cell viability.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X52469; CAA36707.1; -; Genomic_DNA.
DR EMBL; X52864; CAA37045.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB16405.1; -; Genomic_DNA.
DR PIR; S12790; S12790.
DR RefSeq; NP_594580.1; NM_001020009.2.
DR AlphaFoldDB; P17609; -.
DR SMR; P17609; -.
DR BioGRID; 279707; 6.
DR STRING; 4896.SPAC9E9.07c.1; -.
DR iPTMnet; P17609; -.
DR MaxQB; P17609; -.
DR PaxDb; P17609; -.
DR PRIDE; P17609; -.
DR EnsemblFungi; SPAC9E9.07c.1; SPAC9E9.07c.1:pep; SPAC9E9.07c.
DR GeneID; 2543280; -.
DR KEGG; spo:SPAC9E9.07c; -.
DR PomBase; SPAC9E9.07c; ypt2.
DR VEuPathDB; FungiDB:SPAC9E9.07c; -.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P17609; -.
DR OMA; HKMLIGN; -.
DR PhylomeDB; P17609; -.
DR Reactome; R-SPO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR Reactome; R-SPO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P17609; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0006887; P:exocytosis; IMP:PomBase.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; ISO: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 Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..200
FT /note="GTP-binding protein ypt2"
FT /id="PRO_0000121309"
FT MOTIF 38..46
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 16..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 64..68
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 122..125
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 200
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 200 AA; 22755 MW; 2C658D153A290C30 CRC64;
MSTKSYDYLI KLLLIGDSGV GKSCLLLRFS EDSFTPSFIT TIGIDFKIRT IELDGKRIKL
QIWDTAGQER FRTITTAYYR GAMGILLLYD VTDKKSFDNV RTWFSNVEQH ASENVYKILI
GNKCDCEDQR QVSFEQGQAL ADELGVKFLE ASAKTNVNVD EAFFTLAREI KKQKIDAENE
FSNQANNVDL GNDRTVKRCC
