RGA5_SCHPO
ID RGA5_SCHPO Reviewed; 361 AA.
AC O74335; Q50JD6; Q9USS5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Rho-GTPase-activating protein 5;
GN Name=rga5; ORFNames=SPBC17F3.01c, SPBC557.01;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-343.
RX PubMed=12427731; DOI=10.1074/jbc.m208993200;
RA Huang T.Y., Markley N.A., Young D.;
RT "Nak1, an essential GC kinase regulates cell morphology and growth in
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 278:991-997(2003).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12519200; DOI=10.1046/j.1365-2958.2003.03312.x;
RA Calonge T.M., Arellano M., Coll P.M., Perez P.;
RT "Rga5p is a specific Rho1p GTPase-activating protein that regulates cell
RT integrity in Schizosaccharomyces pombe.";
RL Mol. Microbiol. 47:507-518(2003).
CC -!- FUNCTION: GTPase-activating protein for Rho1. Has a role in the
CC negative regulation of (1-3)beta-D-glucan synthase activity and cell
CC integrity. {ECO:0000269|PubMed:12519200}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12519200}.
CC Note=Membrane-associated. Localizes to the cell poles and septum.
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DR EMBL; CU329671; CAA20323.1; -; Genomic_DNA.
DR EMBL; AF091345; AAY18722.1; -; Genomic_DNA.
DR PIR; T39723; T39723.
DR RefSeq; NP_596024.2; NM_001021932.3.
DR AlphaFoldDB; O74335; -.
DR SMR; O74335; -.
DR BioGRID; 276260; 16.
DR STRING; 4896.SPBC17F3.01c.1; -.
DR iPTMnet; O74335; -.
DR MaxQB; O74335; -.
DR PaxDb; O74335; -.
DR PRIDE; O74335; -.
DR EnsemblFungi; SPBC17F3.01c.1; SPBC17F3.01c.1:pep; SPBC17F3.01c.
DR GeneID; 2539707; -.
DR KEGG; spo:SPBC17F3.01c; -.
DR PomBase; SPBC17F3.01c; rga5.
DR VEuPathDB; FungiDB:SPBC17F3.01c; -.
DR eggNOG; KOG2710; Eukaryota.
DR HOGENOM; CLU_025218_2_1_1; -.
DR InParanoid; O74335; -.
DR PhylomeDB; O74335; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR Reactome; R-SPO-9013148; CDC42 GTPase cycle.
DR PRO; PR:O74335; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IDA:PomBase.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IMP:PomBase.
DR GO; GO:0090334; P:regulation of cell wall (1->3)-beta-D-glucan biosynthetic process; IMP:PomBase.
DR GO; GO:0060237; P:regulation of fungal-type cell wall organization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 4: Predicted;
KW GTPase activation; Membrane; Reference proteome.
FT CHAIN 1..361
FT /note="Rho-GTPase-activating protein 5"
FT /id="PRO_0000097313"
FT DOMAIN 52..245
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 306..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 361 AA; 40976 MW; DA11FCFB006C46BF CRC64;
MTVVVGVLQI DDMGKKSSFA SWWKQLRVKK SDDNKLFGLS LTRALEVSKV AIFLTRRDGE
KVFYGYIPAV VAKCGFFLKQ NATQVKGIFR VNGSSKRIQI LQKAFSTGPD YGRSFDWEGY
TVHDAANVFR RFINLMPEHV IPLEYYERFR EPMTIPNLTD NERVEMYRRR IDELPIPNRQ
LLLYLLDLLS VFAMNSSKNL MTADNLAAIF QPGILSHPDH EVYSKDYQIS QTALLFLINH
QGSFIKTIPL SSLPPLVAAP TSPNTSSTLI TQSAAPTPIA STSIRINSFN PRNGSIKRWR
SFSRHSSATY SNSPSSNFSN MKSSEVDPGS PPRIKSRSYS LSRSSSMKLF HTLDRRRENR
M
