YPT3_SCHPO
ID YPT3_SCHPO Reviewed; 214 AA.
AC P17610;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=GTP-binding protein ypt3;
DE AltName: Full=RAB;
GN Name=ypt3; Synonyms=its5; ORFNames=SPAC18G6.03;
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].
RX PubMed=2328721; DOI=10.1002/j.1460-2075.1990.tb08257.x;
RA Miyake S., Yamamoto M.;
RT "Identification of ras-related, YPT family genes in Schizosaccharomyces
RT pombe.";
RL EMBO J. 9:1417-1422(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF SER-24 AND ARG-29.
RX PubMed=12181359; DOI=10.1091/mbc.01-09-0463;
RA Cheng H., Sugiura R., Wu W., Fujita M., Lu Y., Sio S.O., Kawai R.,
RA Takegawa K., Shuntoh H., Kuno T.;
RT "Role of the Rab GTP-binding protein Ypt3 in the fission yeast exocytic
RT pathway and its connection to calcineurin function.";
RL Mol. Biol. Cell 13:2963-2976(2002).
RN [4]
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 [5]
RP ISOPRENYLATION AT CYS-213 AND CYS-214.
RX PubMed=1597466; DOI=10.1016/s0021-9258(19)49914-6;
RA Newman C.M., Giannakouros T., Hancock J.F., Fawell E.H., Armstrong J.,
RA Magee A.I.;
RT "Post-translational processing of Schizosaccharomyces pombe YPT proteins.";
RL J. Biol. Chem. 267:11329-11336(1992).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16483310; DOI=10.1111/j.1365-2443.2006.00935.x;
RA He Y., Sugiura R., Ma Y., Kita A., Deng L., Takegawa K., Matsuoka K.,
RA Shuntoh H., Kuno T.;
RT "Genetic and functional interaction between Ryh1 and Ypt3: two Rab GTPases
RT that function in S. pombe secretory pathway.";
RL Genes Cells 11:207-221(2006).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in retrograde traffricking of proteins from the
CC endosome to the Golgi. Involved in the secretory pathway where it has a
CC role in acid phosphatase secretion. {ECO:0000269|PubMed:12181359,
CC ECO:0000269|PubMed:16483310}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305|PubMed:1597466}; Cytoplasmic side {ECO:0000305}. Endosome
CC membrane {ECO:0000269|PubMed:12181359, ECO:0000269|PubMed:16483310};
CC Lipid-anchor {ECO:0000305|PubMed:1597466}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:12181359, ECO:0000269|PubMed:16483310}; Lipid-
CC anchor {ECO:0000305|PubMed:1597466}. Cytoplasm
CC {ECO:0000269|PubMed:12181359}. Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X52100; CAA36320.1; -; Genomic_DNA.
DR EMBL; X52732; CAA36946.1; -; mRNA.
DR EMBL; CU329670; CAA92383.1; -; Genomic_DNA.
DR PIR; S10026; S10026.
DR RefSeq; NP_593667.1; NM_001019099.2.
DR AlphaFoldDB; P17610; -.
DR SMR; P17610; -.
DR BioGRID; 278693; 12.
DR STRING; 4896.SPAC18G6.03.1; -.
DR iPTMnet; P17610; -.
DR SwissPalm; P17610; -.
DR MaxQB; P17610; -.
DR PaxDb; P17610; -.
DR PRIDE; P17610; -.
DR EnsemblFungi; SPAC18G6.03.1; SPAC18G6.03.1:pep; SPAC18G6.03.
DR PomBase; SPAC18G6.03; ypt3.
DR VEuPathDB; FungiDB:SPAC18G6.03; -.
DR eggNOG; KOG0087; Eukaryota.
DR HOGENOM; CLU_041217_23_0_1; -.
DR InParanoid; P17610; -.
DR OMA; PSSYENC; -.
DR PhylomeDB; P17610; -.
DR Reactome; R-SPO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-SPO-8854214; TBC/RABGAPs.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR PRO; PR:P17610; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0090689; C:cleavage furrow leading edge; IDA:PomBase.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035838; C:growing cell tip; IDA:CACAO.
DR GO; GO:0090619; C:meiotic spindle pole; IDA:PomBase.
DR GO; GO:0035974; C:meiotic spindle pole body; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005628; C:prospore membrane; IDA:PomBase.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISS:PomBase.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; TAS:PomBase.
DR GO; GO:0061796; P:membrane addition at site of mitotic cytokinesis; EXP:PomBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:PomBase.
DR GO; GO:1903024; P:positive regulation of ascospore-type prospore membrane formation; IMP:PomBase.
DR GO; GO:0045921; P:positive regulation of exocytosis; IMP:PomBase.
DR GO; GO:1990896; P:protein localization to cell cortex of cell tip; IMP:PomBase.
DR GO; GO:1902441; P:protein localization to meiotic spindle pole body; IMP:PomBase.
DR GO; GO:0042144; P:vacuole fusion, non-autophagic; IMP:PomBase.
DR GO; GO:0016192; P:vesicle-mediated transport; 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 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Endosome; Golgi apparatus; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..214
FT /note="GTP-binding protein ypt3"
FT /id="PRO_0000121310"
FT MOTIF 39..47
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 65..69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 123..126
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 214
FT /note="Not methylated"
FT /evidence="ECO:0000269|PubMed:1597466"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT LIPID 213
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1597466"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000269|PubMed:1597466"
FT MUTAGEN 24
FT /note="S->N: Growth inhibited."
FT /evidence="ECO:0000269|PubMed:12181359"
FT MUTAGEN 29
FT /note="R->H: Localizes to cytoplasm and nucleus."
FT /evidence="ECO:0000269|PubMed:12181359"
SQ SEQUENCE 214 AA; 23861 MW; BBE084B6A05DC6EE CRC64;
MCQEDEYDYL FKTVLIGDSG VGKSNLLMRF TRNEFNIESK STIGVEFATR NIVLDNKKIK
AQIWDTAGQE RYRAITSAYY RGAVGALIVY DITKQSSFDN VGRWLKELRE HADSNIVIML
VGNKTDLLHL RAVSTEEAQA FAAENNLSFI ETSAMDASNV EEAFQTVLTE IFRIVSNRSL
EAGDDGVHPT AGQTLNIAPT MNDLNKKKSS SQCC
