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Ras-like protein 1

 RAS_SCHPO               Reviewed;         219 AA.
P08647; O13806;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
05-DEC-2018, entry version 175.
RecName: Full=Ras-like protein 1;
Flags: Precursor;
Name=ras1; ORFNames=SPAC17H9.09c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=JY282;
PubMed=4006903;
Fukui Y., Kaziro Y.;
"Molecular cloning and sequence analysis of a ras gene from
Schizosaccharomyces pombe.";
EMBO J. 4:687-691(1985).
[2]
SEQUENCE REVISION.
Kaziro Y.;
Submitted (AUG-1985) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3084798; DOI=10.1007/BF02100997;
Nadin-Davis S.A., Yang R.C.A., Narang S.A., Nasim A.;
"The cloning and characterization of a RAS gene from
Schizosaccharomyces pombe.";
J. Mol. Evol. 23:41-51(1986).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
-!- FUNCTION: Participates in the process of sexual differentiation
and the determination of cell shape. Essential for mating and for
recognition of the mating pheromone, but not for vegetative
growth. Does not regulate the intracellular cAMP level. Regulates
two downstream pathways, namely the byr2/byr1/spk1 mitogen-
activated protein kinase cascade and the cdc42 small G protein
pathway. The former is relevant to mating and sporulation, whereas
the latter is relevant to mating, cell growth and cell morphology.
-!- ACTIVITY REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP).
-!- SUBUNIT: Scd1, scd2, cdc42, and ras1, in its GTP-bound state, act
cooperatively to form a protein complex.
-!- INTERACTION:
P28829:byr2; NbExp=2; IntAct=EBI-15585264, EBI-1032333;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X02331; CAA26191.1; -; Genomic_DNA.
EMBL; X03771; CAA27399.1; -; Genomic_DNA.
EMBL; CU329670; CAB11218.1; -; Genomic_DNA.
PIR; A22715; TVBYSR.
PIR; T37875; TVBYPR.
PIR; T45545; T45545.
RefSeq; NP_593579.1; NM_001019011.2.
ProteinModelPortal; P08647; -.
SMR; P08647; -.
BioGrid; 278753; 32.
DIP; DIP-61182N; -.
IntAct; P08647; 2.
STRING; 4896.SPAC17H9.09c.1; -.
iPTMnet; P08647; -.
SwissPalm; P08647; -.
MaxQB; P08647; -.
PaxDb; P08647; -.
PRIDE; P08647; -.
EnsemblFungi; SPAC17H9.09c.1; SPAC17H9.09c.1:pep; SPAC17H9.09c.
GeneID; 2542285; -.
KEGG; spo:SPAC17H9.09c; -.
EuPathDB; FungiDB:SPAC17H9.09c; -.
PomBase; SPAC17H9.09c; ras1.
HOGENOM; HOG000233973; -.
InParanoid; P08647; -.
KO; K07827; -.
OMA; QCVIDDI; -.
OrthoDB; EOG092C4VY0; -.
PhylomeDB; P08647; -.
PRO; PR:P08647; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:1990819; C:actin fusion focus; IDA:PomBase.
GO; GO:0071521; C:Cdc42 GTPase complex; TAS:PomBase.
GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
GO; GO:0032153; C:cell division site; IDA:PomBase.
GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0000935; C:division septum; IDA:PomBase.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0005886; C:plasma membrane; IDA:PomBase.
GO; GO:0002135; F:CTP binding; IDA:PomBase.
GO; GO:0019003; F:GDP binding; IDA:PomBase.
GO; GO:0005525; F:GTP binding; IDA:PomBase.
GO; GO:0003924; F:GTPase activity; IDA:PomBase.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; EXP:PomBase.
GO; GO:0002134; F:UTP binding; IDA:PomBase.
GO; GO:0032488; P:Cdc42 protein signal transduction; IC:PomBase.
GO; GO:0000753; P:cell morphogenesis involved in conjugation with cellular fusion; IMP:PomBase.
GO; GO:0000747; P:conjugation with cellular fusion; IMP:PomBase.
GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:PomBase.
GO; GO:0031139; P:positive regulation of conjugation with cellular fusion; IMP:PomBase.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:PomBase.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:PomBase.
GO; GO:0034307; P:regulation of ascospore formation; IMP:PomBase.
GO; GO:1905708; P:regulation of cell morphogenesis involved in conjugation with cellular fusion; EXP:PomBase.
GO; GO:0032005; P:signal transduction involved in positive regulation of conjugation with cellular fusion; IMP:PomBase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
Cell membrane; Cell shape; Complete proteome; GTP-binding;
Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
Reference proteome.
CHAIN 1 216 Ras-like protein 1.
/FTId=PRO_0000082678.
PROPEP 217 219 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281333.
NP_BIND 15 22 GTP. {ECO:0000250}.
NP_BIND 62 66 GTP. {ECO:0000250}.
NP_BIND 121 124 GTP. {ECO:0000250}.
MOTIF 37 45 Effector region.
MOD_RES 216 216 Cysteine methyl ester. {ECO:0000250}.
LIPID 216 216 S-farnesyl cysteine. {ECO:0000250}.
CONFLICT 6 6 L -> M (in Ref. 3; CAA27399).
{ECO:0000305}.
CONFLICT 57 57 L -> V (in Ref. 1; CAA26191).
{ECO:0000305}.
CONFLICT 60 60 V -> L (in Ref. 1; CAA26191).
{ECO:0000305}.
CONFLICT 81 81 E -> Q (in Ref. 1; CAA26191).
{ECO:0000305}.
CONFLICT 134 136 AEG -> RER (in Ref. 1; CAA26191).
{ECO:0000305}.
CONFLICT 181 181 Q -> H (in Ref. 1; CAA26191).
{ECO:0000305}.
CONFLICT 188 188 T -> I (in Ref. 1; CAA26191).
{ECO:0000305}.
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


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