RYH1_SCHPO
ID RYH1_SCHPO Reviewed; 201 AA.
AC P17608;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=GTP-binding protein ryh1;
GN Name=ryh1; Synonyms=hos1, its6; ORFNames=SPAC4C5.02c;
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=2112088; DOI=10.1002/j.1460-2075.1990.tb08322.x;
RA Hengst L., Lehmeier T., Gallwitz D.;
RT "The ryh1 gene in the fission yeast Schizosaccharomyces pombe encoding a
RT GTP-binding protein related to ras, rho and ypt: structure, expression and
RT identification of its human homologue.";
RL EMBO J. 9:1949-1955(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF THR-25 AND GLN-70.
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 [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).
RN [4]
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).
CC -!- FUNCTION: Has a role in retrograde traffricking of proteins from the
CC endosome to the Golgi. Involved in protein transport to the plasma
CC membrane. Involved in the secretory pathway where it has a role in acid
CC phosphatase secretion. Required also in normal glycosylation
CC trafficking pathways. {ECO:0000269|PubMed:16483310}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2112088};
CC Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endosome
CC membrane {ECO:0000269|PubMed:2112088}; Lipid-anchor {ECO:0000305}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:2112088}; Lipid-anchor
CC {ECO:0000305}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; X52475; CAA36715.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11173.1; -; Genomic_DNA.
DR PIR; S12789; S12789.
DR RefSeq; NP_593249.1; NM_001018646.2.
DR AlphaFoldDB; P17608; -.
DR SMR; P17608; -.
DR BioGRID; 279947; 166.
DR STRING; 4896.SPAC4C5.02c.1; -.
DR iPTMnet; P17608; -.
DR MaxQB; P17608; -.
DR PaxDb; P17608; -.
DR PRIDE; P17608; -.
DR EnsemblFungi; SPAC4C5.02c.1; SPAC4C5.02c.1:pep; SPAC4C5.02c.
DR GeneID; 2543529; -.
DR KEGG; spo:SPAC4C5.02c; -.
DR PomBase; SPAC4C5.02c; ryh1.
DR VEuPathDB; FungiDB:SPAC4C5.02c; -.
DR eggNOG; KOG0094; Eukaryota.
DR HOGENOM; CLU_041217_10_2_1; -.
DR InParanoid; P17608; -.
DR OMA; PVSNDGC; -.
DR PhylomeDB; P17608; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR Reactome; R-SPO-8873719; RAB geranylgeranylation.
DR Reactome; R-SPO-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR PRO; PR:P17608; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:1904515; P:positive regulation of TORC2 signaling; IMP:PomBase.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; 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; Methylation; Nucleotide-binding; Nucleus;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..201
FT /note="GTP-binding protein ryh1"
FT /id="PRO_0000121307"
FT MOTIF 40..48
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 18..25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 66..70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 199
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 201
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 25
FT /note="T->N: Growth inhibited in ypt3-i5 mutant cells; no
FT effect on wild-type cells."
FT /evidence="ECO:0000269|PubMed:16483310"
FT MUTAGEN 70
FT /note="Q->L: Growth inhibited in wild-type cells; localizes
FT to the plasma membrane."
FT /evidence="ECO:0000269|PubMed:16483310"
SQ SEQUENCE 201 AA; 23136 MW; 353493CBF987D1E5 CRC64;
MSENYSFSLR KFKLVFLGEQ SVGKTSLITR FMYDQFDNTY QATIGIDFLS KTMYLEDRTV
RLQLWDTAGQ ERFRSLIPSY IRDSSVAIIV YDITNHNSFV NTEKWIEDVR AERGDDVIIV
LVGNKTDLAD KRQVTQEEGE KKAKELKIMH METSAKAGHN VKLLFRKIAQ MLPGMENVET
QSTQMIDVSI QPNENESSCN C
