IQGA2_MOUSE
ID IQGA2_MOUSE Reviewed; 1575 AA.
AC Q3UQ44;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ras GTPase-activating-like protein IQGAP2;
GN Name=Iqgap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-881, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Binds to activated CDC42 and RAC1 but does not seem to
CC stimulate their GTPase activity. Associates with calmodulin.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK147360; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK142813; BAE25199.1; -; mRNA.
DR EMBL; AK147360; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS36753.1; -.
DR RefSeq; NP_081987.1; NM_027711.1.
DR AlphaFoldDB; Q3UQ44; -.
DR SMR; Q3UQ44; -.
DR BioGRID; 243818; 11.
DR IntAct; Q3UQ44; 5.
DR MINT; Q3UQ44; -.
DR STRING; 10090.ENSMUSP00000067685; -.
DR iPTMnet; Q3UQ44; -.
DR PhosphoSitePlus; Q3UQ44; -.
DR SwissPalm; Q3UQ44; -.
DR EPD; Q3UQ44; -.
DR jPOST; Q3UQ44; -.
DR MaxQB; Q3UQ44; -.
DR PaxDb; Q3UQ44; -.
DR PeptideAtlas; Q3UQ44; -.
DR PRIDE; Q3UQ44; -.
DR ProteomicsDB; 269504; -.
DR Antibodypedia; 3789; 203 antibodies from 33 providers.
DR Ensembl; ENSMUST00000068603; ENSMUSP00000067685; ENSMUSG00000021676.
DR GeneID; 544963; -.
DR KEGG; mmu:544963; -.
DR UCSC; uc007rmo.1; mouse.
DR CTD; 10788; -.
DR MGI; MGI:2449975; Iqgap2.
DR VEuPathDB; HostDB:ENSMUSG00000021676; -.
DR eggNOG; KOG2128; Eukaryota.
DR GeneTree; ENSGT00950000183076; -.
DR HOGENOM; CLU_000972_2_1_1; -.
DR InParanoid; Q3UQ44; -.
DR OMA; PECANKY; -.
DR OrthoDB; 674320at2759; -.
DR PhylomeDB; Q3UQ44; -.
DR TreeFam; TF313078; -.
DR Reactome; R-MMU-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013408; RHOG GTPase cycle.
DR BioGRID-ORCS; 544963; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Iqgap2; mouse.
DR PRO; PR:Q3UQ44; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UQ44; protein.
DR Bgee; ENSMUSG00000021676; Expressed in ciliary body and 249 other tissues.
DR Genevisible; Q3UQ44; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0071933; F:Arp2/3 complex binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0070493; P:thrombin-activated receptor signaling pathway; ISO:MGI.
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; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001202; WW_dom.
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; 3.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1575
FT /note="Ras GTPase-activating-like protein IQGAP2"
FT /id="PRO_0000354074"
FT DOMAIN 41..156
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 594..627
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 690..719
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 720..749
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 750..779
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 917..1150
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 356
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 782
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 881
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1002
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 1269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 1279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT MOD_RES 1461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13576"
FT CONFLICT 1275
FT /note="K -> R (in Ref. 1; BAE25199)"
FT /evidence="ECO:0000305"
FT CONFLICT 1447
FT /note="K -> E (in Ref. 1; BAE25199)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1575 AA; 180528 MW; 5EF176042E4D158F CRC64;
MPHEELPSLQ RPRYGSIVDD ERLSAEEMDE RRRQNIAYEY LCHLEEAKRW MEVCLVEELP
PTTELEEGLR NGVYLAKLAK FFAPKMVSEK KIYDVEQTRY KKSGLHFRHT DNTVQWLRAM
EAIGLPKIFY PETTDVYDRK NIPRMIYCIH ALSLYLFKLG IAPQIQDLLG KVDFTEEEIS
NMRKELEKYG IQMPAFSKIG GILANELSVD EAALHAAVIA INEAIEKGVA KQTIITLRNP
NAVLTCVDDS LSQEYQKELW EAKKKKEESA KLKNSCISEE ERDAYEELLT QAEIQSNIST
VNRMAAVDHI NAVLQEGDPE NTLLALKKPE AQLPAVYPFA AVMYQNELFN LQKQNTSNYL
AHEELLIAVE MLSAVALLNQ ALESSDLVAV QNQLRSPTIG FNNLDEAHVD RYADALLSVK
QEALSQGQDT LSWNEIQNCI DMINNQIQEE NDRMVVLGYI NEAIDAGNPL KTLDTLLLPT
ANIRDVDPDC AQHYQDVLFY TKSQKLGDPK NVSKVLWLDE IQQAINEANV DENRAKQWVT
LVVDVNECLD RKQSDHILTA LKSSPSNIHN ILPECANKYY DTLVKAKESK TDNESSEGSW
VTLNVQEKYN YYYNTDSKEG SWVPPELCLS KESWLTGEEI EDIVEEVTSD YIREKLWSAS
EDLLVRFEAT TLGPALREEF EARKAFLYEQ TESVVKIQAF WKGFKQRQEY LHRQQVFAGN
VDSVVKIQSW FRMVTARKSY LSRLRYFEDH KNEIVKIQSL LRASKARDDY KALVGSENPP
LTVIRKFVYL LDQSDLDFQE ELEVARLREE VVTKIRANQQ LEKDLNLMDI KIGLLVKNRI
TLEDVISHRK KLNKKKGGEI EILNNTDNKG IKSLSKERRK TLETYQQLFY LLQTKPSYLA
KLIFQMPQNK STKFMDTVIF TLYNYASNQR EEYLLLKLFK TALEEEIKSK VDQVQDIVTG
NPTVIKMVVS FNRGARGQNT LRQLLAPVVK EIIEDKALVI NTNPVEVYKA WVNQLETQTG
EASKLPYDVT TEQALTYPEV KNKLEASIEN LRKVTDKVLG SIISSLDLLP YGLRYIAKVL
KNSIREKFPD ATEEELLKIV GNLLYYRYMN PAIVAPDGFD IIDMTAGGQI NSNQRRNLGS
VAKVLQHAAS NKLFEGENEH LSSMNNYLSE TYQEFRKYFQ EACDVPEPEE KFNMDKYTDL
VTVSKPVIYI SIEEIINTHL LLLEHQDAIA TEKSDLLNEL LESLGEVPTV ESFLGEGAVD
PNDPNKENTL NQLSKTEISL SLTSKYDVKD GEAVDGRSLM IKTKKLIIDV TRNQPGSTLT
EILETPATGQ QELEHAKDME SRAVVDSRTP EEGKQSQAVI EDARLPLEQK KRKIQRNLRT
LEQTGHVSSK NKYQDILNEI AKDIRNQRIH RKLRKAELSK LQQTLNALNK KAAFYEDQIN
YYDTYIKTCV DNLKRKNSRR SIKLDGKAEP KGTKRVKPVR YTAAKLHDKG VLLGIDDLQT
NQFKNVMFDI IATEDMGIFD VRSKFLGVEM EKVQLNIQDL LQMQYEGVAV MKMFDKVKVN
VNLLIYLLNK KFYGK
