RAS_SCHPO
ID RAS_SCHPO Reviewed; 219 AA.
AC P08647; O13806;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Ras-like protein 1;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01112};
DE Flags: Precursor;
GN Name=ras1; ORFNames=SPAC17H9.09c;
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=JY282;
RX PubMed=4006903; DOI=10.1002/j.1460-2075.1985.tb03684.x;
RA Fukui Y., Kaziro Y.;
RT "Molecular cloning and sequence analysis of a ras gene from
RT Schizosaccharomyces pombe.";
RL EMBO J. 4:687-691(1985).
RN [2]
RP SEQUENCE REVISION.
RA Kaziro Y.;
RL Submitted (AUG-1985) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3084798; DOI=10.1007/bf02100997;
RA Nadin-Davis S.A., Yang R.C.A., Narang S.A., Nasim A.;
RT "The cloning and characterization of a RAS gene from Schizosaccharomyces
RT pombe.";
RL J. Mol. Evol. 23:41-51(1986).
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 PALMITOYLATION.
RX PubMed=23843742; DOI=10.1371/journal.pbio.1001597;
RA Zhang M.M., Wu P.Y., Kelly F.D., Nurse P., Hang H.C.;
RT "Quantitative control of protein S-palmitoylation regulates meiotic entry
RT in fission yeast.";
RL PLoS Biol. 11:e1001597-e1001597(2013).
CC -!- FUNCTION: Participates in the process of sexual differentiation and the
CC determination of cell shape. Essential for mating and for recognition
CC of the mating pheromone, but not for vegetative growth. Does not
CC regulate the intracellular cAMP level. Regulates two downstream
CC pathways, namely the byr2/byr1/spk1 mitogen-activated protein kinase
CC cascade and the cdc42 small G protein pathway. The former is relevant
CC to mating and sporulation, whereas the latter is relevant to mating,
CC cell growth and cell morphology.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01112};
CC -!- ACTIVITY REGULATION: Alternates between an inactive form bound to GDP
CC and an active form bound to GTP. Activated by a guanine nucleotide-
CC exchange factor (GEF) and inactivated by a GTPase-activating protein
CC (GAP).
CC -!- SUBUNIT: Scd1, scd2, cdc42, and ras1, in its GTP-bound state, act
CC cooperatively to form a protein complex.
CC -!- INTERACTION:
CC P08647; P28829: byr2; NbExp=2; IntAct=EBI-15585264, EBI-1032333;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC -!- PTM: Palmitoylated by the erf2-erf4 complex.
CC {ECO:0000269|PubMed:23843742}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000305}.
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DR EMBL; X02331; CAA26191.1; -; Genomic_DNA.
DR EMBL; X03771; CAA27399.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11218.1; -; Genomic_DNA.
DR PIR; A22715; TVBYSR.
DR PIR; T37875; TVBYPR.
DR PIR; T45545; T45545.
DR RefSeq; NP_593579.1; NM_001019011.2.
DR AlphaFoldDB; P08647; -.
DR SMR; P08647; -.
DR BioGRID; 278753; 38.
DR DIP; DIP-61182N; -.
DR IntAct; P08647; 2.
DR STRING; 4896.SPAC17H9.09c.1; -.
DR iPTMnet; P08647; -.
DR SwissPalm; P08647; -.
DR MaxQB; P08647; -.
DR PaxDb; P08647; -.
DR PRIDE; P08647; -.
DR EnsemblFungi; SPAC17H9.09c.1; SPAC17H9.09c.1:pep; SPAC17H9.09c.
DR GeneID; 2542285; -.
DR KEGG; spo:SPAC17H9.09c; -.
DR PomBase; SPAC17H9.09c; ras1.
DR VEuPathDB; FungiDB:SPAC17H9.09c; -.
DR eggNOG; KOG0395; Eukaryota.
DR HOGENOM; CLU_041217_9_8_1; -.
DR InParanoid; P08647; -.
DR OMA; CCSGCVV; -.
DR PhylomeDB; P08647; -.
DR Reactome; R-SPO-9696273; RND1 GTPase cycle.
DR PRO; PR:P08647; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
DR GO; GO:0071521; C:Cdc42 GTPase complex; TAS:PomBase.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; 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:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IDA:PomBase.
DR GO; GO:0002135; F:CTP binding; IDA:PomBase.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0019003; F:GDP binding; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; IDA:PomBase.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; EXP:PomBase.
DR GO; GO:0002134; F:UTP binding; IDA:PomBase.
DR GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:1902917; P:positive regulation of mating projection assembly; IMP:PomBase.
DR GO; GO:0062038; P:positive regulation of pheromone response MAPK cascade; IMP:PomBase.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:PomBase.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:PomBase.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0031137; P:regulation of conjugation with cellular fusion; IMP:PomBase.
DR GO; GO:0032005; P:signal transduction involved in positive regulation of conjugation with cellular fusion; 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 InterPro; IPR020849; Small_GTPase_Ras-type.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell shape; GTP-binding; Hydrolase; Lipoprotein; Membrane;
KW Methylation; Nucleotide-binding; Prenylation; Reference proteome.
FT CHAIN 1..216
FT /note="Ras-like protein 1"
FT /id="PRO_0000082678"
FT PROPEP 217..219
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000281333"
FT MOTIF 37..45
FT /note="Effector region"
FT BINDING 15..22
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 121..124
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 216
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 216
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 6
FT /note="L -> M (in Ref. 3; CAA27399)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="L -> V (in Ref. 1; CAA26191)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> L (in Ref. 1; CAA26191)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="E -> Q (in Ref. 1; CAA26191)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..136
FT /note="AEG -> RER (in Ref. 1; CAA26191)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="Q -> H (in Ref. 1; CAA26191)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="T -> I (in Ref. 1; CAA26191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 219 AA; 24734 MW; 109A0C468663F535 CRC64;
MRSTYLREYK LVVVGDGGVG KSALTIQLIQ SHFVDEYDPT IEDSYRKKCE IDGEGALLDV
LDTAGQEEYS AMREQYMRTG EGFLLVYNIT SRSSFDEIST FYQQILRVKD KDTFPVVLVA
NKCDLEAERV VSRAEGEQLA KSMHCLYVET SAKLRLNVEE AFYSLVRTIR RYNKSEEKGF
QNKQAVQTAQ VPASTAKRAS AVNNSKTEDE VSTKCCVIC
