ARHG9_MOUSE
ID ARHG9_MOUSE Reviewed; 516 AA.
AC Q3UTH8; B1AXI3; B1AXI5; B9EJ88; Q3TQ60; Q80U06; Q8CAF9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Rho guanine nucleotide exchange factor 9;
DE AltName: Full=Collybistin;
DE AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 9;
GN Name=Arhgef9; Synonyms=Kiaa0424;
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] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, and Hypothalamus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=11168555; DOI=10.1046/j.0953-816x.2000.01411.x;
RA Kneussel M., Engelkamp D., Betz H.;
RT "Distribution of transcripts for the brain-specific GDP/GTP exchange factor
RT collybistin in the developing mouse brain.";
RL Eur. J. Neurosci. 13:487-492(2001).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=27609886; DOI=10.1126/science.aag0821;
RA Uezu A., Kanak D.J., Bradshaw T.W., Soderblom E.J., Catavero C.M.,
RA Burette A.C., Weinberg R.J., Soderling S.H.;
RT "Identification of an elaborate complex mediating postsynaptic
RT inhibition.";
RL Science 353:1123-1129(2016).
CC -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for CDC42.
CC Promotes formation of GPHN clusters (By similarity).
CC {ECO:0000250|UniProtKB:Q9QX73}.
CC -!- SUBUNIT: Interacts with GPHN. {ECO:0000250|UniProtKB:Q9QX73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QX73}.
CC Postsynaptic density {ECO:0000269|PubMed:27609886}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3UTH8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UTH8-2; Sequence=VSP_021143;
CC Name=3;
CC IsoId=Q3UTH8-3; Sequence=VSP_021144, VSP_021146;
CC Name=4;
CC IsoId=Q3UTH8-4; Sequence=VSP_021145;
CC -!- TISSUE SPECIFICITY: Detected in embryonic and adult brain.
CC {ECO:0000269|PubMed:11168555}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65562.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122280; BAC65562.1; ALT_INIT; mRNA.
DR EMBL; AK038840; BAC30147.2; ALT_TERM; mRNA.
DR EMBL; AK163874; BAE37525.1; -; mRNA.
DR EMBL; AK139416; BAE24002.1; -; mRNA.
DR EMBL; AL807821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX470092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141385; AAI41386.1; -; mRNA.
DR CCDS; CCDS53137.1; -. [Q3UTH8-1]
DR CCDS; CCDS72409.1; -. [Q3UTH8-2]
DR RefSeq; NP_001028501.1; NM_001033329.3. [Q3UTH8-1]
DR RefSeq; NP_001277313.1; NM_001290384.1. [Q3UTH8-2]
DR RefSeq; NP_001277314.1; NM_001290385.1. [Q3UTH8-2]
DR RefSeq; XP_011245884.1; XM_011247582.2. [Q3UTH8-4]
DR RefSeq; XP_011245885.1; XM_011247583.2. [Q3UTH8-1]
DR RefSeq; XP_017173962.1; XM_017318473.1. [Q3UTH8-2]
DR AlphaFoldDB; Q3UTH8; -.
DR BMRB; Q3UTH8; -.
DR SMR; Q3UTH8; -.
DR IntAct; Q3UTH8; 1.
DR MINT; Q3UTH8; -.
DR STRING; 10090.ENSMUSP00000109516; -.
DR iPTMnet; Q3UTH8; -.
DR PhosphoSitePlus; Q3UTH8; -.
DR MaxQB; Q3UTH8; -.
DR PaxDb; Q3UTH8; -.
DR PeptideAtlas; Q3UTH8; -.
DR PRIDE; Q3UTH8; -.
DR ProteomicsDB; 273926; -. [Q3UTH8-1]
DR ProteomicsDB; 273927; -. [Q3UTH8-2]
DR ProteomicsDB; 273928; -. [Q3UTH8-3]
DR ProteomicsDB; 273929; -. [Q3UTH8-4]
DR ABCD; Q3UTH8; 2 sequenced antibodies.
DR Antibodypedia; 27024; 188 antibodies from 30 providers.
DR Ensembl; ENSMUST00000113876; ENSMUSP00000109508; ENSMUSG00000025656. [Q3UTH8-2]
DR Ensembl; ENSMUST00000113878; ENSMUSP00000109510; ENSMUSG00000025656. [Q3UTH8-1]
DR Ensembl; ENSMUST00000113882; ENSMUSP00000109514; ENSMUSG00000025656. [Q3UTH8-4]
DR Ensembl; ENSMUST00000113883; ENSMUSP00000109515; ENSMUSG00000025656. [Q3UTH8-4]
DR Ensembl; ENSMUST00000181987; ENSMUSP00000138461; ENSMUSG00000025656. [Q3UTH8-3]
DR Ensembl; ENSMUST00000182001; ENSMUSP00000138668; ENSMUSG00000025656. [Q3UTH8-2]
DR Ensembl; ENSMUST00000199920; ENSMUSP00000143779; ENSMUSG00000025656. [Q3UTH8-2]
DR GeneID; 236915; -.
DR KEGG; mmu:236915; -.
DR UCSC; uc009ttt.2; mouse. [Q3UTH8-1]
DR UCSC; uc009ttv.1; mouse. [Q3UTH8-3]
DR CTD; 23229; -.
DR MGI; MGI:2442233; Arhgef9.
DR VEuPathDB; HostDB:ENSMUSG00000025656; -.
DR eggNOG; KOG3519; Eukaryota.
DR GeneTree; ENSGT00940000154103; -.
DR HOGENOM; CLU_008436_2_1_1; -.
DR InParanoid; Q3UTH8; -.
DR OMA; EXFEISE; -.
DR OrthoDB; 428887at2759; -.
DR PhylomeDB; Q3UTH8; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 236915; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Arhgef9; mouse.
DR PRO; PR:Q3UTH8; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q3UTH8; protein.
DR Bgee; ENSMUSG00000025656; Expressed in superior frontal gyrus and 145 other tissues.
DR ExpressionAtlas; Q3UTH8; baseline and differential.
DR Genevisible; Q3UTH8; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0099572; C:postsynaptic specialization; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0043113; P:receptor clustering; ISO:MGI.
DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; IDA:SynGO.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:MGI.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11975; SH3_ARHGEF9; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR035728; ARHGEF9_SH3.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..516
FT /note="Rho guanine nucleotide exchange factor 9"
FT /id="PRO_0000253896"
FT DOMAIN 8..67
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 103..287
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 318..425
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 100..110
FT /note="Interaction with GPHN"
FT /evidence="ECO:0000250"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12693553"
FT /id="VSP_021143"
FT VAR_SEQ 1..3
FT /note="MYD -> MQWIRGGTGM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021144"
FT VAR_SEQ 1..3
FT /note="MYD -> MTL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021145"
FT VAR_SEQ 458..516
FT /note="VNSARSVPPSYPPPQDPLNQGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFS
FT RLTPFKK -> TSAFTPPNPLTVCVGLGNHGVCVFTFLGSFLY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021146"
SQ SEQUENCE 516 AA; 60927 MW; A3372AA20B1B8F0B CRC64;
MYDLITGDSI VSAEAVWDHV TMANRELAFK AGDVIKVLDA SNKDWWWGQI DDEEGWFPAS
FVRLWVNQED GVEEGPSDVQ NGHLDPNSDC LCLGRPLQNR DQMRANVINE IMSTERHYIK
HLKDICEGYL KQCRKRRDMF SDEQLKVIFG NIEDIYRFQM GFVRDLEKQY NNDDPHLSEI
GPCFLEHQDG FWIYSEYCNN HLDACMELSK LMKDSRYQHF FEACRLLQQM IDIAIDGFLL
TPVQKICKYP LQLAELLKYT AQDHSDYRYV AAALAVMRNV TQQINERKRR LENIDKIAQW
QASVLDWEGE DILDRSSELI YTGEMAWIYQ PYGRNQQRVF FLFDHQMVLC KKDLIRRDIL
YYKGRIDMDK YEVIDIEDGR DDDFNVSMKN AFKLHNKETE EVHLFFAKKL EEKIRWLRAF
REERKMVQED EKIGFEISEN QKRQAAMTVR KASKQKGVNS ARSVPPSYPP PQDPLNQGQY
LVPDGIAQSQ VFEFTEPKRS QSPFWQNFSR LTPFKK
