ID IQG1_YEAST Reviewed; 1495 AA. AC Q12280; D6W3C9; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 31-MAY-2011, entry version 92. DE RecName: Full=Ras GTPase-activating-like protein IQG1; DE AltName: Full=Cytokinesis protein 1; DE AltName: Full=IQGAP-related protein 1; GN Name=IQG1; Synonyms=CYK1; OrderedLocusNames=YPL242C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH AFR1; AKR1 AND RP CDC42. RC STRAIN=CUY30; RX PubMed=9679143; DOI=10.1083/jcb.142.2.443; RA Osman M.A., Cerione R.A.; RT "Iqg1p, a yeast homologue of the mammalian IQGAPs, mediates cdc42p RT effects on the actin cytoskeleton."; RL J. Cell Biol. 142:443-455(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204511 / S288c / AB972; RX MEDLINE=97313271; PubMed=9169875; RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., RA Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., RA Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., RA Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., RA Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., RA Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., RA Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., RA Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., RA Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., RA Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., RA Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., RA Zollner A., Vo D.H., Hani J.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; RL Nature 387:103-105(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [4] RP FUNCTION. RX PubMed=9382845; DOI=10.1016/S0960-9822(06)00411-8; RA Epp J.A., Chant J.; RT "An IQGAP-related protein controls actin-ring formation and RT cytokinesis in yeast."; RL Curr. Biol. 7:921-929(1997). RN [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9442111; DOI=10.1083/jcb.140.2.355; RA Lippincott J., Li R.; RT "Sequential assembly of myosin II, an IQGAP-like protein, and RT filamentous actin to a ring structure involved in budding yeast RT cytokinesis."; RL J. Cell Biol. 140:355-366(1998). RN [6] RP FUNCTION, AND INTERACTION WITH CMD1 AND TEM1. RX PubMed=9950677; RA Shannon K.B., Li R.; RT "The multiple roles of Cyk1p in the assembly and function of the RT actomyosin ring in budding yeast."; RL Mol. Biol. Cell 10:283-296(1999). RN [7] RP INTERACTION WITH MLC1 AND MYO1, AND MUTAGENESIS OF LEU-457. RX PubMed=11082046; RA Boyne J.R., Yosuf H.M., Bieganowski P., Brenner C., Price C.; RT "Yeast myosin light chain, Mlc1p, interacts with both IQGAP and class RT II myosin to effect cytokinesis."; RL J. Cell Sci. 113:4533-4543(2000). RN [8] RP INTERACTION WITH BUD4 AND SEC3. RX PubMed=12446742; DOI=10.1083/jcb.200205084; RA Osman M.A., Konopka J.B., Cerione R.A.; RT "Iqg1p links spatial and secretion landmarks to polarity and RT cytokinesis."; RL J. Cell Biol. 159:601-611(2002). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [10] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS RP SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354 AND SER-365, AND RP MASS SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [13] RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH INN1. RX PubMed=18344988; DOI=10.1038/ncb1701; RA Sanchez-Diaz A., Marchesi V., Murray S., Jones R., Pereira G., RA Edmondson R., Allen T., Labib K.; RT "Inn1 couples contraction of the actomyosin ring to membrane RT ingression during cytokinesis in budding yeast."; RL Nat. Cell Biol. 10:395-406(2008). CC -!- FUNCTION: Required for the assembly and the contraction of the CC actomyosin ring at the bud neck during cytokinesis. Seems to be CC involved in additional tasks during cell division like axial bud- CC site selection and targeted secretion by recruiting the spatial CC landmark BUD4, the septin CDC12 and the secretion landmark SEC3 to CC the bud neck. May be regulated by calcium ions. CC -!- SUBUNIT: Interacts with AFR1, AKR1, activated CDC42, calmodulin CC (CMD1), myosin MYO1 and its light chain MLC1, BUD4, INN1, SEC3 and CC TEM1. CC -!- INTERACTION: CC P47136:BUD4; NbExp=4; IntAct=EBI-35351, EBI-3848; CC P53141:MLC1; NbExp=3; IntAct=EBI-35351, EBI-10988; CC P08964:MYO1; NbExp=1; IntAct=EBI-35351, EBI-11650; CC P33332:SEC3; NbExp=1; IntAct=EBI-35351, EBI-16850; CC -!- SUBCELLULAR LOCATION: Bud neck. Note=Forms a ring at the bud neck CC in a MLC1-dependent manner, which contracts at the end of CC cytokinesis. CC -!- DOMAIN: The calponin homology (CH) domain binds to actin filaments CC and is required for their recruitment to the bud neck. CC -!- DOMAIN: The IQ domains serve as interaction surface for the myosin CC light chain MLC1. CC -!- DOMAIN: The Ras-GAP domain is required for contraction of the CC actomyosin ring and is needed for the interaction with TEM1. It CC probably does not stimulate GTPase activity. CC -!- MISCELLANEOUS: Present with 279 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Contains 1 CH (calponin-homology) domain. CC -!- SIMILARITY: Contains 7 IQ domains. CC -!- SIMILARITY: Contains 1 Ras-GAP domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF019644; AAB70827.1; -; Genomic_DNA. DR EMBL; Z73598; CAA97963.1; -; Genomic_DNA. DR EMBL; Z67751; CAA91603.1; -; Genomic_DNA. DR EMBL; BK006949; DAA11195.1; -; Genomic_DNA. DR PIR; S61023; S61023. DR RefSeq; NP_015082.1; NM_001184056.1. DR ProteinModelPortal; Q12280; -. DR SMR; Q12280; 99-258, 1369-1494. DR DIP; DIP-1144N; -. DR IntAct; Q12280; 27. DR MINT; MINT-1578204; -. DR STRING; Q12280; -. DR PeptideAtlas; Q12280; -. DR EnsemblFungi; YPL242C; YPL242C; YPL242C. DR GeneID; 855834; -. DR KEGG; sce:YPL242C; -. DR NMPDR; fig|4932.3.peg.6209; -. DR CYGD; YPL242c; -. DR SGD; S000006163; IQG1. DR eggNOG; fuNOG04232; -. DR GeneTree; EFGT00050000002498; -. DR HOGENOM; HBG204004; -. DR OMA; PDLFRFE; -. DR OrthoDB; EOG4XH378; -. DR PhylomeDB; Q12280; -. DR NextBio; 980401; -. DR ArrayExpress; Q12280; -. DR Genevestigator; Q12280; -. DR GermOnline; YPL242C; Saccharomyces cerevisiae. DR GO; GO:0000142; C:cellular bud neck contractile ring; TAS:SGD. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005099; F:Ras GTPase activator activity; IEA:InterPro. DR GO; GO:0007015; P:actin filament organization; IPI:SGD. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0000910; P:cytokinesis; IMP:SGD. DR GO; GO:0006970; P:response to osmotic stress; TAS:SGD. DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR001936; RasGAP. DR InterPro; IPR000593; RasGAP_C. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1. DR Gene3D; G3DSA:1.10.506.10; RasGAP; 1. DR Pfam; PF00307; CH; 1. DR Pfam; PF00612; IQ; 1. DR Pfam; PF00616; RasGAP; 1. DR Pfam; PF03836; RasGAP_C; 1. DR SMART; SM00033; CH; 1. DR SMART; SM00015; IQ; 3. DR SUPFAM; SSF47576; Calponin-homology; 1. DR SUPFAM; SSF48350; Rho_GAP; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS50096; IQ; FALSE_NEG. DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; FALSE_NEG. DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; FALSE_NEG. PE 1: Evidence at protein level; KW Actin-binding; Cell cycle; Cell division; Coiled coil; KW Complete proteome; Phosphoprotein; Repeat. FT CHAIN 1 1495 Ras GTPase-activating-like protein IQG1. FT /FTId=PRO_0000056652. FT DOMAIN 108 217 CH. FT DOMAIN 447 467 IQ 1. FT DOMAIN 538 567 IQ 2. FT DOMAIN 568 597 IQ 3. FT DOMAIN 599 628 IQ 4. FT DOMAIN 629 658 IQ 5. FT DOMAIN 687 716 IQ 6. FT DOMAIN 717 746 IQ 7. FT DOMAIN 860 1071 Ras-GAP. FT COILED 759 798 Potential. FT COMPBIAS 37 76 Ser-rich. FT MOD_RES 354 354 Phosphoserine. FT MOD_RES 365 365 Phosphoserine. FT MUTAGEN 457 457 L->P: In IQG1-1; causes a defect in FT cytokinesis at 37 degrees Celsius. SQ SEQUENCE 1495 AA; 172830 MW; C0C7582808154DCC CRC64; MTAYSGSPSK PGNNNSYLNR YVENLGTNVT PPLRPQSSSK INSSLNIASP SHLKTKTSAS NSSATILSKK VESSVSKLKP SLPNKLVGKY TVDLSNYSKI ELRYYEFLCR VSEVKIWIEA VIEEALPSEI ELCVGDSLRN GVFLAKLTQR INPDLTTVIF PAGDKLQFKH TQNINAFFGL VEHVGVPDSF RFELQDLYNK KNIPQVFETL HILISMINKK WPGKTPALTN VSGQISFTKE EIAACKKAWP RIRDFKSLGT NINTAPASPE EPKEKRSGLI KDFNKFERPN IPVEEILITP RKNITDANCS DFSNTPSPYN EAPKMSNLDV VVEKRKFTPI EPSLLGPTPS LEYSPIKNKS LSYYSPTISK YLTYDTEFYT RRSRAREEDL NYYQTFKYSP SHYSPMRRER MTEEQFLEKV VQLQNICRGV NTRFNLYIQK RLLNLFEQDI LRFQACLRGN KFRVLSSMYL PIRRAKIDVP HVEAIQSRIK GSRIRYKYDK LKFTLSRFSC TVELLQAYCR SKLLKTTVNT KLNDIEISHY PLTKLQSYMR ASYVRKKVMS LNTKLNDERE SIMKFSAIIR GNVVRCSEDA ILSAVHDVHK ENISKLQSLI RGIFTRSCLA SIIYSLGKEN CNIIQLSACI RGNAVRHKVQ SLFAPENNLS ETVHDLQGLV RGILVRYTLD LVDDIVEYNN LALFQAFSRG ALVRESLDQK SSFYKRNVRS VIMIQSWIRK SLQRSAYLEL LDCPNPSLWA VKKFVHLLNG TATIEEVQNQ LESCQASLDS ENMKKERLLK SIRQQLNING VLDKFGLLKD KDHELGISDS TIPKSKYQKY EKLFYMLQVD PSYWKLLYLK EPEFVAKNVY MTFGTVNQRM NDRERSYFTR FVCEMLQNAI NEAPSIESFL DNRSQFWQTI LQDFLRRESP EFFSIIVPVL DYLSDPVVDF ESDPYKIYQE IHGFSSPQHC SPVDDASTKN KFIDNLRCLW HAIEMVAEIY TRKVHTIPVE IRYLCTKIFC YAADKNIEEI DSLRAISSIL VNVFVSEYLV NREYYGYKDS NVQKNNQKID ILMKSLATVF EIKNFDGFLD PLNQYANEIK PHIKDVLYNV LVDPEYEQEG DRLIYLDMVS PSPKLELLTE KVLEISGKFE EYLNEFPEAD ILHDILEKNL DNSSFPRSGR VTLELDASAY RFLVSDDKMR KIYDQVKRAF VYMMQIEDVD TNLYDLSIST ILPQDEPNFA NFLEQNPKIR DDPMIQKLKP LKYFTLKNVT LKKIHELEST GTFCSSDNKL QNFLNDIANT IKNPNYAIDY VTQEIYITKE TLTKISEMNH SLDIELSRLK KHVDHTIKDF QKAKDFSPVH KSKFGNFKNA VKKVQGRERS ELQGMKFKWN TKQLYERGVL KTIRGEKLAE LTVKVFGSSG PKFPDIIFKI STSDGSRFGI QMIDKRKGPD KRYSDDVDSF SFKDLIKTQV EPKIETWKLF HSNVVVNNSQ LLHLIVSFFY KRNAL //