IQG1_YEAST
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 03-AUG-2022, entry version 176.
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; DOI=10.1242/jcs.113.24.4533;
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}.
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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 AlphaFoldDB; Q12280; -.
DR SMR; Q12280; -.
DR BioGRID; 35921; 101.
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 SGD; S000006163; IQG1.
DR VEuPathDB; FungiDB:YPL242C; -.
DR eggNOG; KOG2128; Eukaryota.
DR GeneTree; ENSGT00950000183076; -.
DR HOGENOM; CLU_000972_1_0_1; -.
DR InParanoid; Q12280; -.
DR OMA; HQKHFGG; -.
DR BioCyc; YEAST:G3O-34128-MON; -.
DR Reactome; R-SCE-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8980692; RHOA GTPase cycle.
DR Reactome; R-SCE-9013026; RHOB GTPase cycle.
DR Reactome; R-SCE-9013106; RHOC GTPase cycle.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR Reactome; R-SCE-9013424; RHOV GTPase cycle.
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:0110085; C:mitotic actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0005516; F:calmodulin binding; IPI:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
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: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:0031991; P:regulation of actomyosin contractile ring contraction; IC:ComplexPortal.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IC:ComplexPortal.
DR GO; GO:0032465; P:regulation of cytokinesis; IC:ComplexPortal.
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 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; 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 MOD_RES 264
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 299
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|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
