RAL2_SCHPO
ID RAL2_SCHPO Reviewed; 611 AA.
AC P15258;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Protein ral2;
GN Name=ral2; ORFNames=SPBC21.05c;
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], AND FUNCTION.
RX PubMed=2586528; DOI=10.1128/mcb.9.12.5617-5622.1989;
RA Fukui Y., Miyake S., Satoh M., Yamamoto M.;
RT "Characterization of the Schizosaccharomyces pombe ral2 gene implicated in
RT activation of the ras1 gene product.";
RL Mol. Cell. Biol. 9:5617-5622(1989).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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: Essential for mating and for recognition of the mating
CC pheromone, and for the determination of cell shape. Implicated in
CC activation of the ras1 protein. {ECO:0000269|PubMed:2586528}.
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DR EMBL; M30827; AAA35331.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB36885.1; -; Genomic_DNA.
DR PIR; A33827; A33827.
DR RefSeq; NP_596339.1; NM_001022260.2.
DR AlphaFoldDB; P15258; -.
DR BioGRID; 277280; 7.
DR IntAct; P15258; 1.
DR MINT; P15258; -.
DR STRING; 4896.SPBC21.05c.1; -.
DR iPTMnet; P15258; -.
DR MaxQB; P15258; -.
DR PaxDb; P15258; -.
DR EnsemblFungi; SPBC21.05c.1; SPBC21.05c.1:pep; SPBC21.05c.
DR GeneID; 2540760; -.
DR KEGG; spo:SPBC21.05c; -.
DR PomBase; SPBC21.05c; ral2.
DR VEuPathDB; FungiDB:SPBC21.05c; -.
DR eggNOG; KOG0379; Eukaryota.
DR HOGENOM; CLU_041328_0_0_1; -.
DR InParanoid; P15258; -.
DR OMA; RNTMESQ; -.
DR PhylomeDB; P15258; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:P15258; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; 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; IGI:PomBase.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR SUPFAM; SSF117281; SSF117281; 1.
PE 1: Evidence at protein level;
KW Kelch repeat; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..611
FT /note="Protein ral2"
FT /id="PRO_0000119142"
FT REPEAT 43..91
FT /note="Kelch 1"
FT REPEAT 96..149
FT /note="Kelch 2"
FT REPEAT 175..224
FT /note="Kelch 3"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 611 AA; 69848 MW; 1C424B2D31F00AAB CRC64;
MSEVKRNISL RNSTNIFTST FSLSSNNVPK PLIGESVIKY GDEAFVYGGR DALNAQLVND
MYVVDLNTCS WKQVEYQGNQ KPIPRYFHSG DLWNNKLIFF GGMGFNDDTK CLYVLNDIDI
YDIETKQWSH IPGMITENQT NDDAKEVNGS DVDEKSKHLY PSARYGHLHC VLDHYLIIFC
GQDLSNSYIE EINIFDLDSG KWVFKSLFNH HCGIYRSNCV VINKDSEFLQ MCRPINTTQD
SNEHSIGSLF FYLNYNFVNV KRQVIYLELF ELDTAESEKK SAALAKDNNQ SFRFLELDVT
EKFLSSAMPP GLRFPAVNIL GDNLILSGIY LTSSRQAFVL WVYSLDKELW LQLDMLGVLN
HGSWFKCLVL DCTNRFVVFG NKTRKLTQDY NLRQSNYDHI VFIELEGYGV YRKPQMGRVT
ERSEQLGKLL LNGISDMEIL TIERMHIPCL SRMLYKRWPA FQKIMDRAVE KNQEAFQAEV
SQLGPQLTDL PFSSIHSTGS RALYMPYSFE TCSAFLHYIY CGTLNGSYCT AKNLCNLLIL
CKGFEGLETF FAYIVHLLHG VLNRNNVKLI YETAALTGAK GLQLRALRRI ARIEQGGTAI
SPTSPLPNLD D
