RGA3_SCHPO
ID RGA3_SCHPO Reviewed; 969 AA.
AC O14014; Q9USB8;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable Rho-type GTPase-activating protein 3;
GN Name=rga3; ORFNames=SPAC29A4.11;
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 [LARGE SCALE GENOMIC DNA] OF 461-692, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP GENE NAME.
RX PubMed=11737264; DOI=10.1046/j.1365-2443.2001.00485.x;
RA Nakano K., Mutoh T., Mabuchi I.;
RT "Characterization of GTPase-activating proteins for the function of the
RT Rho-family small GTPases in the fission yeast Schizosaccharomyces pombe.";
RL Genes Cells 6:1031-1042(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIL1.
RX PubMed=20404563; DOI=10.4161/cc.9.9.11526;
RA Rumpf C., Cipak L., Novatchkova M., Li Z., Polakova S., Dudas A.,
RA Kovacikova I., Miadokova E., Ammerer G., Gregan J.;
RT "High-throughput knockout screen in Schizosaccharomyces pombe identifies a
RT novel gene required for efficient homolog disjunction during meiosis I.";
RL Cell Cycle 9:1802-1808(2010).
CC -!- FUNCTION: GTPase-activating protein for Rho-type proteins.
CC {ECO:0000305}.
CC -!- SUBUNIT: Interacts with dil1. {ECO:0000269|PubMed:20404563}.
CC -!- SUBCELLULAR LOCATION: Cell septum {ECO:0000269|PubMed:10759889}.
CC Note=Cell poles and septum.
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DR EMBL; CU329670; CAB10138.1; -; Genomic_DNA.
DR EMBL; AB027887; BAA87191.1; -; Genomic_DNA.
DR PIR; T38478; T38478.
DR RefSeq; NP_594871.1; NM_001020300.2.
DR AlphaFoldDB; O14014; -.
DR SMR; O14014; -.
DR BioGRID; 278773; 60.
DR STRING; 4896.SPAC29A4.11.1; -.
DR iPTMnet; O14014; -.
DR MaxQB; O14014; -.
DR PaxDb; O14014; -.
DR PRIDE; O14014; -.
DR EnsemblFungi; SPAC29A4.11.1; SPAC29A4.11.1:pep; SPAC29A4.11.
DR GeneID; 2542306; -.
DR KEGG; spo:SPAC29A4.11; -.
DR PomBase; SPAC29A4.11; rga3.
DR VEuPathDB; FungiDB:SPAC29A4.11; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG1704; Eukaryota.
DR HOGENOM; CLU_309526_0_0_1; -.
DR InParanoid; O14014; -.
DR OMA; TGHAYEL; -.
DR PhylomeDB; O14014; -.
DR PRO; PR:O14014; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; HDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0090726; C:cortical dynamic polarity patch; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:PomBase.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00029; C1; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00132; LIM; 2.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW GTPase activation; LIM domain; Metal-binding; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..969
FT /note="Probable Rho-type GTPase-activating protein 3"
FT /id="PRO_0000075901"
FT DOMAIN 17..81
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 76..135
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 780..966
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 697..744
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 170..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 108649 MW; 7BC27BD909076F0B CRC64;
MIFRKSISKS PSSKGSTVCF RCGQAFQRRE TPISFGGHMW HKDCFCCTKC DKGLEHSDQM
LVQTSDGRPV CSSCAHTCTA CRMRIKDYAL MSGYDSYHRE CFRCHDCRKQ IIDSNFKRDN
RTIFCNDCKQ VRHPSRSSDE SADYHNFEVD VTIKPTETKS SVESNKSLSI EIMSPQKPPL
SPFGGSRDRL VSETPTNMSQ AEGGNVPNDG QDSNLASNSA DSLLPSAKNR SFSSFTSFES
PMKYDDSFFP ISPSISPLQK VNKQQQIESP TATFPLSKNT WKNRFHTFHK QSFTPVNDSS
SSDSLKPTIN EEALDDFAGS ASPYKTMSLT DRAEPIVMNG HMRSLHNATS PFRPFSPSYR
SSDTHSPRTR SPNVQTHKKT SSQPSDLSSF AQLLSPPQVL SPKPNGGGHK SFRHSHSLSE
TSQQTLVPSL GSNGEYHLPT NDHSSTPAQS ERDSDVEELR EQLENLTALT KKLSERLSSS
TFDNSKFIRT EDKDTVRSAK LEICEKFFSF ADVTDDPTLK DPKHQDLVAA ANAYMAMLRE
SYGTEINNLL ERRNELLDDY NNVQKILNES LEASVHLNTK NLELADLNNN LVKQIQHRVP
PENQSNLEHT ITTSSKNTTS SINPLTAVSS NSGQSSGRPG PLSPNLNVTT RIDIKGKKGS
MHLQPRDVNR KVPFKSMHTK SKSADPVVGN EDRTQCDHVF HVNAIFKPSR CYICSESVWG
SELRCFHCSI SCHSRCLKRL FAESEHEKTM SETVSENSKW MPEMPTRMPP PGPSPTMFGR
SLENQLKIEG SVLPQVIAMC VSCVDAHGLE VEGIYRISGS ASQVRVLVDE FENGSIRMEH
LTSDLFACTS VLKTYLHRLP EPVIPGTQYE ELLEAEKIEK EEEKIERVVE VMKTLHPAHL
SVFRFLIAHL GRVCKHAEKN LMNSKNVSTV FAPTLMRDKV NRFDLQHATK KSTALQFMLD
NVDKILHNL
