IQG1_CANAL
ID IQG1_CANAL Reviewed; 1647 AA.
AC Q5AH02; A0A1D8PQY8; Q3MPF8;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 116.
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; OrderedLocusNames=CAALFM_C701840WA;
GN ORFNames=CaO19.13889, CaO19.6536;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION AT SER-48; THR-66;
RP THR-72; THR-82; SER-83; SER-91; SER-139; SER-165; SER-167; SER-169;
RP THR-367; SER-369; SER-433; SER-440; SER-1064; SER-1068; SER-1088; SER-1383
RP AND SER-1385, AND INTERACTION WITH BNI1; BNR1; CLB2; CLB4 AND CDC28.
RX PubMed=18923418; DOI=10.1038/emboj.2008.219;
RA Li C.R., Wang Y.M., Wang Y.;
RT "The IQGAP Iqg1 is a regulatory target of CDK for cytokinesis in Candida
RT albicans.";
RL EMBO J. 27:2998-3010(2008).
RN [5]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
CC -!- FUNCTION: Required for the assembly and the contraction of the
CC actomyosin ring at the bud neck during cytokinesis.
CC {ECO:0000269|PubMed:18923418}.
CC -!- SUBUNIT: Interacts with myosin MYO1 and its light chain MLC1 (By
CC similarity). Interacts with BNI1, BNR1, CLB2, CLB4, and CDC28.
CC {ECO:0000250, ECO:0000269|PubMed:18923418}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:18923418}.
CC Note=Forms a ring at the bud neck in a MLC1-dependent manner, which
CC contracts at the end of cytokinesis.
CC -!- INDUCTION: Rat catheter biofilm repressed.
CC {ECO:0000269|PubMed:19527170}.
CC -!- DOMAIN: The calponin homology (CH) domain binds to actin filaments and
CC is required for their recruitment to the bud neck.
CC {ECO:0000269|PubMed:18923418}.
CC -!- DOMAIN: The IQ domains provide the interaction surface for the myosin
CC light chain MLC1. {ECO:0000250}.
CC -!- DOMAIN: The Ras-GAP domain is required for contraction of the
CC actomyosin ring. It probably does not stimulate GTPase activity (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Hyperphosphorylated. Phosphorylation is cell cycle-dependent and
CC peaks at the time of cytokinesis. Contains 21 consensus sites for
CC cyclin-dependent kinases (CDKs). At least some of them are
CC phosphorylated by the CLB2-CDC28 kinase complex. Mutation of 15 of the
CC phosphorylation sites to Ala caused both premature assembly and delayed
CC disassembly of the actomyosin ring, blocked interaction with the actin-
CC nucleating proteins BNI1 and BNR1, and resulted in defects in
CC cytokinesis. {ECO:0000269|PubMed:18923418}.
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DR EMBL; CP017629; AOW30549.1; -; Genomic_DNA.
DR RefSeq; XP_721374.2; XM_716281.2.
DR AlphaFoldDB; Q5AH02; -.
DR SMR; Q5AH02; -.
DR BioGRID; 1220146; 6.
DR IntAct; Q5AH02; 5.
DR MINT; Q5AH02; -.
DR STRING; 237561.Q5AH02; -.
DR iPTMnet; Q5AH02; -.
DR PRIDE; Q5AH02; -.
DR GeneID; 3637052; -.
DR KEGG; cal:CAALFM_C701840WA; -.
DR CGD; CAL0000175167; IQG1.
DR VEuPathDB; FungiDB:C7_01840W_A; -.
DR eggNOG; KOG2128; Eukaryota.
DR HOGENOM; CLU_000972_1_0_1; -.
DR InParanoid; Q5AH02; -.
DR OrthoDB; 674320at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:1903479; P:mitotic actomyosin contractile ring assembly actin filament organization; IBA:GO_Central.
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; IPR000593; RasGAP_C.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR Pfam; PF00307; CH; 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.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell cycle; Cell division; Coiled coil; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1647
FT /note="Ras GTPase-activating-like protein IQG1"
FT /id="PRO_0000424604"
FT DOMAIN 184..291
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 467..478
FT /note="IQ 1"
FT DOMAIN 528..539
FT /note="IQ 2"
FT DOMAIN 556..567
FT /note="IQ 3"
FT DOMAIN 586..597
FT /note="IQ 4"
FT DOMAIN 616..627
FT /note="IQ 5"
FT DOMAIN 642..653
FT /note="IQ 6"
FT DOMAIN 672..683
FT /note="IQ 7"
FT DOMAIN 734..745
FT /note="IQ 8"
FT DOMAIN 764..775
FT /note="IQ 9"
FT DOMAIN 958..1193
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 18..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 841..919
FT /evidence="ECO:0000255"
FT COMPBIAS 326..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 66
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 82
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 1068
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 1383
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
FT MOD_RES 1385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18923418"
SQ SEQUENCE 1647 AA; 188768 MW; 2AD7E201C1586DAC CRC64;
MAIGNIAARY LSSLEETDTT ATTTTTTTSN VLQPSNRLNS PTKFNRKSLD NNSQDLDALA
RALNITPSKP ETPTSISKGS ATSLLRTKFE SPSATVSSFK STSSSNGVSP TKKNHFVEIT
SDETPSWANK NYKDILNKSP TKFNTQSNVH TPLKQLNQPI GTPSSSSLSP AKNASKSSPG
YEYLCRIEAI KQWLESVLQE QITQSASQLI SYIRNGIHLA KLANVVLPTS KPVFLNDSKL
QFKHTENINR FFQLLDFFNM PDLFRFELTD LYDAKNVPKV WFCLHALSYI LHKQDPSYPA
MNNLVGKVDF SADDIRTANR ALVNSPLPNF SSADTGEGKS DTSNNNSSTT SATAAFMDKV
TSPVKKTPSP LKRPQQLQKK QLELVEDNKP ELTQDSSGLS KISRDDPFTD RVDLAPPSTS
NAKLELHTPP SKSLEFKIKS PIIDLSHRDS DYYTPELESH LPNIIKFQSL ARGAVFRYLM
FVDRILLKSY QDEFTNLFAI IRGNKARRKT VHKHRDELRL YSFEIIELQS IIRKNFVINK
KPNFTSITND VETVELQSLI RGKLTRDWKK YVTNGLEKFT PQIIDFQSLV RMKSIYSKSN
KVISYKDEIL PSLIELQSIA RSQLYHRFSR SNAIDETEII KIQSIIRRNA VIEDLYTKLS
KVRSNKRRLI ELQSIARGGV ARTKLCNSVL VTLIYEDGIL NQLFAKIRGD NYRKKFNSQK
SELLKYEKSS IIPVQTLFRG VLSRYTKEVT LSDIFDQIDS VITLQSVARG KLMRGSIYEF
SDYYQKHIKQ VVKAQAILQR VFAQNAYKQL ITSKNPPLKV IRRFAPLLSN NDRDFQDEMT
LSDLKDLIIE KCKANEEYEN QIEQLDMKLG LLDKNKISIE EFLKPTKGKT FKPIVENVKN
LERLNKSLKK KIELWQTLFY FIQTNPIYLT KLFNSIPYTK NQTKSGQDLF QSVIQLFPVR
DSSITYHSRE EYFLVKLMIQ LMQNDTANSN NLGDITKLHL TNWIDFFTNF NNHTFQRQHL
KALLGKFVIR IVDNEQVDFE SDPIRIYNQI IDHEMKVYGR SEKSRDISPQ AAIQLPEVSN
KFVGNLMSLR ETCSDLLSML QKNASGNKAL LQIPDHVKLI CRQGYLCAQR KFPDKSDQQH
LAVAGVIFVK HYLGSILQVP ENYGILTGNN DTQKAKSKDN LRYLYRVMLQ LFSMKPFNDN
FLKPLNEYIM ASTDTVKSII SQAIINVGEI ETVYELHDYD DLVTHQRPKL TISVNSLIQL
EKSILQNVDI ITTGNDDQLY KTCVEVEKLL ISPQDMLTLT DLSSVTLNLN PTTQEESIVD
SKTKTLFTQA KRCLLYIIRV QEEDDSDDLL ELLISGIKPS HEQRFKEIVQ YEKAEQDISL
NNSKSVTANT VNKKKSTRPY SGTSLGDLSN LTYHELKKMC LEIILKLESM GELTRKNSFQ
TLLNQIAMDI KTKDSQRQCR WQQLQVSQKT IKKLSEKENY LKTQLHNYKK HVESVLLELQ
SKSKSNDKNW KRRLFNIMVI PVFSKQYFYH RELRKHNRLP KFGSYKYSAK KLIDQKVLID
FSTANNVATA SKLDFMFSCH QVGKFTIEVA SGTVNIPGAT NTITLDELLA LQYENKTKFE
LFDGMATFDS NNFMGLIFRK FYDLKKE
