RGA8_SCHPO
ID RGA8_SCHPO Reviewed; 777 AA.
AC Q09697;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Rho-GTPase-activating protein 8;
GN Name=rga8; ORFNames=SPAC13A11.01c, SPAC2F7.18c;
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 [MRNA], FUNCTION, INTERACTION WITH PAK1, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RX PubMed=14506270; DOI=10.1074/jbc.m306819200;
RA Yang P., Qyang Y., Bartholomeusz G., Zhou X., Marcus S.;
RT "The novel Rho GTPase-activating protein family protein, Rga8, provides a
RT potential link between Cdc42/p21-activated kinase and Rho signaling
RT pathways in the fission yeast, Schizosaccharomyces pombe.";
RL J. Biol. Chem. 278:48821-48830(2003).
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-676; SER-680; THR-682;
RP SER-686; THR-694 AND SER-698, AND IDENTIFICATION BY 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: Acts in signal transduction. Negatively regulates the
CC pak1/shk1 control pathway. {ECO:0000269|PubMed:14506270}.
CC -!- SUBUNIT: Interacts with pak1/shk1. {ECO:0000269|PubMed:14506270}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14506270}.
CC Note=Localizes to the cell ends during interphase and to the septum-
CC forming region during cytokinesis.
CC -!- PTM: Phosphorylated by pak1/shk1. {ECO:0000269|PubMed:14506270,
CC ECO:0000269|PubMed:18257517}.
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DR EMBL; AY375444; AAR21285.1; -; mRNA.
DR EMBL; CU329670; CAA90505.1; -; Genomic_DNA.
DR PIR; T38566; S58162.
DR RefSeq; NP_592988.2; NM_001018388.2.
DR AlphaFoldDB; Q09697; -.
DR SMR; Q09697; -.
DR BioGRID; 279071; 61.
DR STRING; 4896.SPAC13A11.01c.1; -.
DR iPTMnet; Q09697; -.
DR MaxQB; Q09697; -.
DR PaxDb; Q09697; -.
DR PRIDE; Q09697; -.
DR EnsemblFungi; SPAC13A11.01c.1; SPAC13A11.01c.1:pep; SPAC13A11.01c.
DR GeneID; 2542617; -.
DR KEGG; spo:SPAC13A11.01c; -.
DR PomBase; SPAC13A11.01c; rga8.
DR VEuPathDB; FungiDB:SPAC13A11.01c; -.
DR eggNOG; ENOG502QQWB; Eukaryota.
DR HOGENOM; CLU_008201_1_0_1; -.
DR InParanoid; Q09697; -.
DR OMA; EYLQRHM; -.
DR PhylomeDB; Q09697; -.
DR Reactome; R-SPO-8856828; Clathrin-mediated endocytosis.
DR PRO; PR:Q09697; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IDA:PomBase.
DR GO; GO:0035838; C:growing cell tip; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IMP:PomBase.
DR GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IGI:PomBase.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 2.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR000591; DEP_dom.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00610; DEP; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00049; DEP; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50186; DEP; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..777
FT /note="Rho-GTPase-activating protein 8"
FT /id="PRO_0000097316"
FT DOMAIN 3..420
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 213..296
FT /note="DEP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00066"
FT DOMAIN 454..650
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 667..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 117..172
FT /evidence="ECO:0000255"
FT COMPBIAS 667..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 694
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 777 AA; 88208 MW; 707F64DCCADEDAE6 CRC64;
MISSFSNGFW SKDYATGVKK LFDCLDNGVE ENEQVKNLLK LYKEANEEFG EKLQEITKEC
LKGKKPENTE DGATSNKAFE GLRSEIANQG KQHIRIAKDL ETLIIAPFSK MSIDHSQKLQ
TSQQVLTNQI KSYEKKYYTL KKTKSAYYNK CRNLEDYEEE SKESNETTSE AITDLTTVSS
PQQQSLLEND DDLIQLGFME FRPEELKEVL AQVLQEIPLQ DYRVPILGTY PNTCSGNIIV
SWLQENLPVP TLVAAEAFGQ DLIAQGFLRH MGVGGSFVNS TNFHYQWKDK AFQFAGLNSV
DSLVENAKAL PLVGEYLSDY ISHRKLYSSE TQSQRLKREV LDANKIYSES VVDLDKCRTL
VEETIADHLQ FLQKCETDRV LYYKDFFMDL STIISNFLPS MKLLADQIVV YQEIIQPESD
IRYILESAAT GPFLPRVEIY EDYYNDIKDQ IFGVDVEFLS HRDKKRVPII VSTILSYLDL
LYPTLASDEV RQNIWLVNSP LSSVHQLREA LNHSSSVTKE VLSQYTPSVV IGVLKLYFLE
LPDSIVPSSA FELIRSIYMN HSNDTPYRLR LLQNLLSQLR RVNLATLSAI ITHLNRLITL
TPNKETFTIN LANSLSLCIS RPATWNLGIQ HDKHPTKFME DLLTYGPSIF EELRKLNSSK
RVSDRVLYQS SATPRSTDVS PTRPDSISSV RSHTAVESPR SSFEELQPSE IPAESEFTLE
NVPTSLIRSS YALNTRKTRR NFSHSSASNE SAAIFIDQDA KIVNEAVASR DSSLSGS
