GDS1_SCHPO
ID GDS1_SCHPO Reviewed; 492 AA.
AC O60077;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=GTPase-GDP dissociation stimulator arz1 {ECO:0000250|UniProtKB:P52306};
GN Name=arz1 {ECO:0000303|PubMed:18042546};
GN ORFNames=SPCC1494.03 {ECO:0000312|PomBase:SPCC1494.03};
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 [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 [2]
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 [3]
RP GENE NAME.
RX PubMed=18042546; DOI=10.1074/jbc.m707154200;
RA Cuthbertson B.J., Liao Y., Birnbaumer L., Blackshear P.J.;
RT "Characterization of zfs1 as an mRNA-binding and -destabilizing protein in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 283:2586-2594(2008).
CC -!- FUNCTION: Probably acts as a GEF (guanine nucleotide exchange factor)
CC for the Rho family of small GTP-binding proteins (G proteins) that
CC stimulates the dissociation of GDP to enable subsequent binding of GTP
CC (By similarity). May also chaperone the processing and/or trafficking
CC of small GTPases independently of GEF activity (By similarity). May be
CC involved in the control of polarized cell growth via CDC42-mediated
CC signaling (By similarity). May also be involved in the control of cell-
CC wall organization via RHO1-mediated signaling (By similarity).
CC {ECO:0000250|UniProtKB:P39011, ECO:0000250|UniProtKB:P52306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329672; CAA19301.1; -; Genomic_DNA.
DR PIR; T41004; T41004.
DR RefSeq; NP_588528.1; NM_001023516.2.
DR AlphaFoldDB; O60077; -.
DR SMR; O60077; -.
DR BioGRID; 275905; 10.
DR STRING; 4896.SPCC1494.03.1; -.
DR PaxDb; O60077; -.
DR EnsemblFungi; SPCC1494.03.1; SPCC1494.03.1:pep; SPCC1494.03.
DR GeneID; 2539339; -.
DR KEGG; spo:SPCC1494.03; -.
DR PomBase; SPCC1494.03; arz1.
DR VEuPathDB; FungiDB:SPCC1494.03; -.
DR eggNOG; KOG4500; Eukaryota.
DR HOGENOM; CLU_554504_0_0_1; -.
DR InParanoid; O60077; -.
DR OMA; VAILMIK; -.
DR PRO; PR:O60077; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:PomBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040144; RAP1GDS1.
DR PANTHER; PTHR10957; PTHR10957; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Guanine-nucleotide releasing factor; Nucleus;
KW Reference proteome.
FT CHAIN 1..492
FT /note="GTPase-GDP dissociation stimulator arz1"
FT /id="PRO_0000116890"
SQ SEQUENCE 492 AA; 56137 MW; 856A9798D09213C9 CRC64;
MTASDTVYLF QSLADRSKNP QERSLFRNYI SEALELLRET PSSPTVVHEQ CFRFLANSCS
DNNENRAAFF NLGGIDVLKP YCSKDNEYSA LAFAVIHNCI LDSREYRAQV ADAQILNLAI
TYWIDWQHKL KAPFFNMLSF VCEMLYPFCK DCSLVFMGLQ LLPSMVREGI DPFTIFAKAF
DNSLVCVSFA QNPSMLIDSI DLVRNMPDFT KKTDMLNLFP RIAEHDAVLS TSLHADPQFL
DFLESCFRSD DSNSITMASL FIGNLVRRDD IAKQLMQKDF LNMLISCIMQ EKDVDGNVER
VYACCAALRH FMIPVSSRAH FAPTAILLQE KLASSRFTQL HYISASMIRL SMPYILCELA
DHPERFYKLK DWSKSPDFNL ALESNRTLLG FVKHYLTVPK SKEKISAFFK NNINLFEESV
VTVLSTESKY PIVIGEAVFV AILMIKHGYA NVAQTIIASP VYEALKSYRD DPNLAYQLKQ
NVRSLLVLVE HR