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 07-OCT-2020, entry version 168. 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; Saccharomycetes; OC 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 effects RT on the actin cytoskeleton."; RL J. Cell Biol. 142:443-455(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX 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., Botstein D., RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., RA Moestl D., 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., Wambutt R., RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., RA 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; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). 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 cytokinesis in RT 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 filamentous RT actin to a ring structure involved in budding yeast cytokinesis."; RL J. Cell Biol. 140:355-366(1998). RN [6] RP FUNCTION, AND INTERACTION WITH CMD1 AND TEM1. RX PubMed=9950677; DOI=10.1091/mbc.10.2.283; RA Shannon K.B., Li R.; RT "The multiple roles of Cyk1p in the assembly and function of the actomyosin RT 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 II RT 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 cytokinesis."; RL J. Cell Biol. 159:601-611(2002). RN [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX 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 PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [12] 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 ingression RT during cytokinesis in budding yeast."; RL Nat. Cell Biol. 10:395-406(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-264; SER-268 AND THR-299, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). 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-site CC selection and targeted secretion by recruiting the spatial landmark CC BUD4, the septin CDC12 and the secretion landmark SEC3 to the bud neck. CC May be regulated by calcium ions. {ECO:0000269|PubMed:18344988, CC ECO:0000269|PubMed:9382845, ECO:0000269|PubMed:9442111, CC ECO:0000269|PubMed:9950677}. CC -!- SUBUNIT: Interacts with AFR1, AKR1, activated CDC42, calmodulin (CMD1), CC myosin MYO1 and its light chain MLC1, BUD4, INN1, SEC3 and TEM1. CC {ECO:0000269|PubMed:11082046, ECO:0000269|PubMed:12446742, CC ECO:0000269|PubMed:18344988, ECO:0000269|PubMed:9679143, CC ECO:0000269|PubMed:9950677}. CC -!- INTERACTION: CC Q12280; P47136: BUD4; NbExp=4; IntAct=EBI-35351, EBI-3848; CC Q12280; P53141: MLC1; NbExp=12; IntAct=EBI-35351, EBI-10988; CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:18344988, ECO:0000269|PubMed:9442111}. Note=Forms a CC ring at the bud neck in a MLC1-dependent manner, which contracts at the CC end of cytokinesis. CC -!- DOMAIN: The calponin homology (CH) domain binds to actin filaments and CC is required for their recruitment to the bud neck. CC -!- DOMAIN: The IQ domains provide the 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 medium. CC {ECO:0000269|PubMed:14562106}. 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 SMR; Q12280; -. DR BioGRID; 35921; 98. DR ComplexPortal; CPX-3503; MIH complex. DR DIP; DIP-1144N; -. DR IntAct; Q12280; 12. DR MINT; Q12280; -. DR STRING; 4932.YPL242C; -. DR iPTMnet; Q12280; -. DR MaxQB; Q12280; -. DR PaxDb; Q12280; -. DR PRIDE; Q12280; -. DR TopDownProteomics; Q12280; -. DR EnsemblFungi; YPL242C_mRNA; YPL242C; YPL242C. DR GeneID; 855834; -. DR KEGG; sce:YPL242C; -. DR EuPathDB; FungiDB:YPL242C; -. DR SGD; S000006163; IQG1. DR eggNOG; KOG2128; Eukaryota. DR GeneTree; ENSGT00950000183076; -. DR HOGENOM; CLU_000972_1_0_1; -. DR InParanoid; Q12280; -. DR KO; K05767; -. DR OMA; PPMGVVR; -. DR Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs. DR Reactome; R-SCE-6798695; Neutrophil degranulation. DR PRO; PR:Q12280; -. DR Proteomes; UP000002311; Chromosome XVI. DR RNAct; Q12280; protein. DR GO; GO:0005935; C:cellular bud neck; IDA:SGD. DR GO; GO:0000142; C:cellular bud neck contractile ring; IDA:SGD. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0120155; C:MIH complex; IDA:SGD. DR GO; GO:0051015; F:actin filament binding; IDA:SGD. DR GO; GO:0005516; F:calmodulin binding; IPI:SGD. DR GO; GO:0032038; F:myosin II heavy chain binding; IPI:SGD. DR GO; GO:0032033; F:myosin II light chain binding; IPI:SGD. DR GO; GO:0032027; F:myosin light chain binding; IPI:SGD. DR GO; GO:0048365; F:Rac GTPase binding; IBA:GO_Central. DR GO; GO:0017016; F:Ras GTPase binding; IBA:GO_Central. DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:SGD. DR GO; GO:1903479; P:mitotic actomyosin contractile ring assembly actin filament organization; IMP:SGD. DR GO; GO:0072741; P:protein localization to cell division site; IMP:SGD. 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:1903471; P:regulation of mitotic actomyosin contractile ring contraction; IMP:SGD. DR GO; GO:0007165; P:signal transduction; IEA:InterPro. DR CDD; cd00014; CH; 1. DR Gene3D; 1.10.418.10; -; 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; 1. DR Pfam; PF00616; RasGAP; 1. DR Pfam; PF03836; RasGAP_C; 1. DR SMART; SM00033; CH; 1. DR SUPFAM; SSF47576; SSF47576; 1. DR SUPFAM; SSF48350; SSF48350; 1. DR PROSITE; PS50021; CH; 1. PE 1: Evidence at protein level; KW Actin-binding; Cell cycle; Cell division; Coiled coil; Phosphoprotein; KW Reference proteome; Repeat. FT CHAIN 1..1495 FT /note="Ras GTPase-activating-like protein IQG1" FT /id="PRO_0000056652" FT DOMAIN 108..221 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 447..467 FT /note="IQ 1" FT DOMAIN 538..567 FT /note="IQ 2" FT DOMAIN 568..597 FT /note="IQ 3" FT DOMAIN 599..628 FT /note="IQ 4" FT DOMAIN 629..658 FT /note="IQ 5" FT DOMAIN 687..716 FT /note="IQ 6" FT DOMAIN 717..746 FT /note="IQ 7" FT DOMAIN 860..1071 FT /note="Ras-GAP" FT COILED 759..798 FT /evidence="ECO:0000255" FT COMPBIAS 37..76 FT /note="Ser-rich" FT MOD_RES 264 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 299 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:19779198" FT MUTAGEN 457 FT /note="L->P: In IQG1-1; causes a defect in cytokinesis at FT 37 degrees Celsius." FT /evidence="ECO:0000269|PubMed:11082046" 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 //