RNG2_SCHPO
ID RNG2_SCHPO Reviewed; 1489 AA.
AC O14188; Q9USG0;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ras GTPase-activating-like protein rng2;
DE AltName: Full=Ring assembly protein 2;
GN Name=rng2; ORFNames=SPAC4F8.13c;
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] {ECO:0000305}
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 354-531, 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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CAM1, AND SUBCELLULAR LOCATION.
RX PubMed=9635188; DOI=10.1016/s0960-9822(98)70248-9;
RA Eng K., Naqvi N.I., Wong K.C.Y., Balasubramanian M.K.;
RT "Rng2p, a protein required for cytokinesis in fission yeast, is a component
RT of the actomyosin ring and the spindle pole body.";
RL Curr. Biol. 8:611-621(1998).
CC -!- FUNCTION: Required for cytokinesis. Component of the contractile F-
CC actin ring; required for its construction following assembly of F-actin
CC at the division site. {ECO:0000269|PubMed:9635188}.
CC -!- SUBUNIT: Interacts with calmodulin (cam1).
CC {ECO:0000269|PubMed:9635188}.
CC -!- INTERACTION:
CC O14188; P10989: act1; NbExp=3; IntAct=EBI-1152490, EBI-617028;
CC O14188; P05933: cam1; NbExp=2; IntAct=EBI-1152490, EBI-1152513;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus envelope.
CC Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole
CC body. Note=Localized to the F-actin ring and spindle pole body during
CC interphase and mitosis. Also found in septum.
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DR EMBL; CU329670; CAB11059.1; -; Genomic_DNA.
DR EMBL; AB027779; BAA87083.1; -; Genomic_DNA.
DR PIR; T38842; T38842.
DR RefSeq; NP_593860.1; NM_001019289.2.
DR PDB; 1P2X; X-ray; 2.21 A; A=32-190.
DR PDB; 1P5S; X-ray; 2.22 A; A=1-190.
DR PDBsum; 1P2X; -.
DR PDBsum; 1P5S; -.
DR AlphaFoldDB; O14188; -.
DR SMR; O14188; -.
DR BioGRID; 279561; 48.
DR IntAct; O14188; 2.
DR MINT; O14188; -.
DR STRING; 4896.SPAC4F8.13c.1; -.
DR iPTMnet; O14188; -.
DR MaxQB; O14188; -.
DR PaxDb; O14188; -.
DR PRIDE; O14188; -.
DR EnsemblFungi; SPAC4F8.13c.1; SPAC4F8.13c.1:pep; SPAC4F8.13c.
DR GeneID; 2543129; -.
DR KEGG; spo:SPAC4F8.13c; -.
DR PomBase; SPAC4F8.13c; rng2.
DR VEuPathDB; FungiDB:SPAC4F8.13c; -.
DR eggNOG; KOG2128; Eukaryota.
DR HOGENOM; CLU_000972_1_0_1; -.
DR InParanoid; O14188; -.
DR OMA; HQKHFGG; -.
DR PhylomeDB; O14188; -.
DR Reactome; R-SPO-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR Reactome; R-SPO-9013026; RHOB GTPase cycle.
DR Reactome; R-SPO-9013106; RHOC GTPase cycle.
DR Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR Reactome; R-SPO-9013424; RHOV GTPase cycle.
DR EvolutionaryTrace; O14188; -.
DR PRO; PR:O14188; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120104; C:mitotic actomyosin contractile ring, proximal layer; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005816; C:spindle pole body; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:PomBase.
DR GO; GO:0008093; F:cytoskeletal anchor activity; EXP:PomBase.
DR GO; GO:0005096; F:GTPase activator activity; ISM:PomBase.
DR GO; GO:1903478; P:actin filament bundle convergence involved in mitotic contractile ring assembly; IMP:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:1903486; P:establishment of mitotic actomyosin contractile ring localization; IMP:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:PomBase.
DR GO; GO:1903479; P:mitotic actomyosin contractile ring assembly actin filament organization; IBA:GO_Central.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; EXP:PomBase.
DR GO; GO:1902406; P:mitotic actomyosin contractile ring maintenance; EXP:PomBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR000593; RasGAP_C.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF03836; RasGAP_C; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00015; IQ; 8.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Nucleus; Reference proteome; Repeat; Septation.
FT CHAIN 1..1489
FT /note="Ras GTPase-activating-like protein rng2"
FT /id="PRO_0000056665"
FT DOMAIN 41..147
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 359..388
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 389..418
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 418..449
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 535..564
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 565..594
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 655..684
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116,
FT ECO:0000305"
FT DOMAIN 854..1077
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT COILED 734..770
FT /evidence="ECO:0000255"
FT COILED 1330..1364
FT /evidence="ECO:0000255"
FT HELIX 33..55
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:1P2X"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:1P2X"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1P5S"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:1P2X"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:1P2X"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:1P2X"
SQ SEQUENCE 1489 AA; 171677 MW; 7D357FF9A7FED5EC CRC64;
MDVNVGLSRL QSQAGAPVGT KGSNTRLAAK QRETLQAYDY LCRVDEAKKW IEECLGTDLG
PTSTFEQSLR NGVVLALLVQ KFQPDKLIKI FYSNELQFRH SDNINKFLDF IHGIGLPEIF
HFELTDIYEG KNLPKVIYCI HALSYFLSMQ DLAPPLIKSD ENLSFTDEDV SIIVRRLRQS
NVILPNFKAL SADFMLRASP VSSRTPSPTR FPKHARFQTL NSSDSASIYS SPYTSPTLEF
SKKDASARSD ILKMHRRTKS ATPSLEQFNE PYKQTLPSHS IEFEDSFFQP PSQKGHMQRS
FLTTFSAPTR RREALFSTTS GLSQRSPVDE KIVNAIQACG RGVLVRLRLV DMLQSLVEQS
SSVVLLQAVI RGYISRNTYR IRKKAYDELV NWVTSIQSIS RAYLIRAQYR KVVLQEEATK
SIQTLQSIIR GGFYRRKYHS LIERLDLFTP SFVLIQSSAL GFLTRHAIVN MLDNLYNYIP
LFNRMQSILR ANMFRNEWSN FLDSVQSFPV SFHSICKGRL IRDSINRLNG SLLGELDNFI
KLQNLSRGFM IRRAFKEKLE KLKASTSSFI ALQAIVRAFL LRKNLESIYD SFQKSHLSVI
KAQSLYRGFI TRTKIDYCND YLLKRLPDIV FMQSAVRAIL LRDDVNYTEV QLDSFIPEIV
LLQSLIRGYL SRNKFSRKLQ NFHKNMENPI VAKSIFRGRQ EGLAYRELAT AKNPPVMTVK
NFVHLLDDTN FDFEEEVLLE KMRKEIVQQV RDNEEIEVHI NELDVKIALL VKNKISLDDV
LKHHNKYKFG KQSTEYLKIN TLSMKSLNNS SRKFLELYQC FFYVLQTNEM YLANYFQALK
TEGTSSVKIR HAVYLVLQIF GHGSNRREEV LLLRFISQVI KLEAALVNSS QDLLSDDCVW
KLLFTGYRGD VREVKLWKTI LGRIHKVLVA DNHLDFEINP LTLFKSFNPE VASQTDSPKL
TLSLAMQHPP TRNLYVSRLR ELRKLCQSFL VALSKNIENI PYALCYTAAQ LKNSLQRYFP
AAHKEEIFGV IGKFVYWAYV APVLVSPDNF KLVDGSITAL QRKNLYTLSS ILSEIFSIES
CDSKQLGFFR PLSEFIEVSK QDTMLMLERL VDVVDPEVYF EFDAFEDLVN TKRPVIYMKR
DDILGIYSSI AYVIDSIAPP DVNDPLRAVV NSLGPVSEQD NDFVQDETDV KLELNPKFCT
IENPVAQERT LIVQTKRYIL FIIRIQNGLN LLEILVKPVT DSDEAAWQNL LAEESEKNAR
NYDLFDDSIF SMSFAELKYT ALSNIVEMEK LGFANRRNNY QDMVNSIALD IRNKSRRRMQ
RQRELDAGHQ SLLNLREKRA FLDSQLKSYN EYIEQAMETL QSKKGKKKLI PFSKQYFHMR
DLRKSGRVPR FGSFKYPALK LYDRGVLVSI SHMPQKEKLY ITISADEVGK FILEATSPTV
KVSSPRCELH LDDLLSAQYN KVLTLDVLDG RLKLNTNMFL HLIFSKFYS
