RHG23_MOUSE
ID RHG23_MOUSE Reviewed; 1483 AA.
AC Q69ZH9; Q8BNY7; Q9JJD6;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Rho GTPase-activating protein 23;
DE AltName: Full=Rho-type GTPase-activating protein 23;
GN Name=Arhgap23; Synonyms=Kiaa1501; ORFNames=MNCb-1301;
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 STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1483 (ISOFORM 1).
RC TISSUE=Natural killer cell;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1107-1483.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-372; SER-515;
RP SER-579; SER-607; SER-619; THR-652; SER-655; SER-658 AND SER-673, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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: GTPase activator for the Rho-type GTPases by converting them
CC to an inactive GDP-bound state. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69ZH9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZH9-2; Sequence=VSP_023710;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC37556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB041572; BAA95056.1; -; mRNA.
DR EMBL; AL596088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK173187; BAD32465.1; -; mRNA.
DR EMBL; AK079135; BAC37556.1; ALT_INIT; mRNA.
DR RefSeq; NP_067468.2; NM_021493.2.
DR AlphaFoldDB; Q69ZH9; -.
DR SMR; Q69ZH9; -.
DR BioGRID; 208470; 14.
DR IntAct; Q69ZH9; 3.
DR MINT; Q69ZH9; -.
DR STRING; 10090.ENSMUSP00000112999; -.
DR iPTMnet; Q69ZH9; -.
DR PhosphoSitePlus; Q69ZH9; -.
DR jPOST; Q69ZH9; -.
DR MaxQB; Q69ZH9; -.
DR PaxDb; Q69ZH9; -.
DR PeptideAtlas; Q69ZH9; -.
DR PRIDE; Q69ZH9; -.
DR ProteomicsDB; 254960; -. [Q69ZH9-1]
DR ProteomicsDB; 254961; -. [Q69ZH9-2]
DR Antibodypedia; 73731; 36 antibodies from 16 providers.
DR DNASU; 58996; -.
DR Ensembl; ENSMUST00000093940; ENSMUSP00000091472; ENSMUSG00000049807. [Q69ZH9-2]
DR GeneID; 58996; -.
DR KEGG; mmu:58996; -.
DR UCSC; uc007lec.1; mouse. [Q69ZH9-1]
DR UCSC; uc007led.1; mouse. [Q69ZH9-2]
DR CTD; 57636; -.
DR MGI; MGI:3697726; Arhgap23.
DR VEuPathDB; HostDB:ENSMUSG00000049807; -.
DR eggNOG; KOG4407; Eukaryota.
DR GeneTree; ENSGT00940000157982; -.
DR HOGENOM; CLU_962967_0_0_1; -.
DR InParanoid; Q69ZH9; -.
DR OrthoDB; 142586at2759; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 58996; 4 hits in 58 CRISPR screens.
DR ChiTaRS; Arhgap23; mouse.
DR PRO; PR:Q69ZH9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q69ZH9; protein.
DR Bgee; ENSMUSG00000049807; Expressed in lumbar subsegment of spinal cord and 206 other tissues.
DR ExpressionAtlas; Q69ZH9; baseline and differential.
DR Genevisible; Q69ZH9; MM.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; GTPase activation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..1483
FT /note="Rho GTPase-activating protein 23"
FT /id="PRO_0000280472"
FT DOMAIN 71..155
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 684..804
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 901..1093
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1171..1361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P227"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 652
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 850
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9P227"
FT VAR_SEQ 1..1158
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_023710"
FT CONFLICT 1462..1464
FT /note="DLG -> EPR (in Ref. 4; BAC37556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1483 AA; 161832 MW; 652088C6725EC9BE CRC64;
MNGVAFCLVG IPPRPEPRPP QLPLGPRDGC SSGRPLPWPG PRTLLLRKSL QDGFGFTLRH
FIVYPPESAV HCILKEEENG GRGGGPSPRH RLEPMDTIFV KNVKDGGPAH RAGLRTGDRL
VKVNGESIIG KTYSQVIGLI QNSDDTLELS IMPKDEDILQ LAYSQDAYLK GNEPYSGEAR
SIPEPPPLCY PRKTYAPPTR APAWATMVPE PISALPPDPR SPAAWSDPGS RVPSATRAHL
DNSSLGMSQP RPSPGAFPHL PSESRTPRAF PEPGSRVLPS RLECQQALSH WLSNQIPRRA
GERRCPAMPP RARSASQDRL EDVTTHHPWP CSTSQDALSQ LGQEGWHRAR SDDYLSRATR
SAEALGPGAL VSPRLERCGW ASQRPSARTS ACPSRDLTQA PPPSGLQGLD DIGYIGYRSY
SPSFQRRTGL LHALSFRDSP FGGLPTFSLA QSPASFPPEA SEPPRVVRPD PSTRALEPPA
EDHRDEVVLR QKPPTGRKVQ LTPARQMNLG FGDESPEPEA RGERLGRKVA PLATTEDSLA
SIPFIDEPTS PSIDLQAKHV PASAVVSSAM NSAPVLGTSP SSPTFTFALS RHYSQDCSSI
KAGRRSSYLL AITTERSKSC DDGLNTFRDE GRVLRRLPSR VPSLRVLRSF FTDGSLDSWG
TSEDADAPSK RHSTSDLSDA TFSDIRREGW LYYKQILTKK GKKAGGGLRQ WKRVYAVLRA
RSLSLSKERR EPGPAAAGAA AAGAGEDEAA PVCIGSCLVD ISYSETKRRH VFRLTTADFC
EYLFQAEDRD DMLGWIRAIR ENSRAEGEDP GCANQALISK KLNDYRKVSH SSGPKADSSP
KGSRGLGGLK SEFLKQTAVR GLRTQEQPPG SKEDSVAAPK TPWGINIIKK NKKAAPRAFG
IRLEECQPAT ENQRVPLIVA ACCRIVEARG LESTGIYRVP GNNAVVSSLQ EQLNRGPSDI
NLQDERWQDL NVISSLLKAF FRKLPEPLFT DDKYNDFIEA NRIEDSRERM KTLRKLIRDL
PGHYYETLKF LVGHLKTIAD HSEKNKMEPR NLALVFGPTL VRTSEDNMTD MVTHMPDRYK
IVETLIQHSD WFFSDDEDKG ERTPVDDKEP QSVPNIEYLL PNIGRTVPPS DPGSDSTTCS
SAKSKGSWVP KKEPYAREML AISFISAVNR KRKKRREARG LGSSTDDDSE QEAHKAAVGT
QEPPEGQLPG PAAEEAPGRL SPPTAPDERP AADTRSIVSG YSTLSTMDRS VCSGTGGRRA
GAGDEADDER SELSHVETDT EGGAGPGGRL SRRPSFSSHH LMPCDTLARR RLSRSRAEAE
GPGAGTARAC PRGPEPPGSA SSSSQESLRP PAAAPALGSR PSRVEALRLR LRGTADDMLA
VRLRRPLSPE TRRRRSSWRR HTVVVQSPLT DLNFNEWKEL GGGGPQESVG VRPHSDNKDS
GLSSLESTKA RASSAASLPS GDLGALQGLP QRRSAAARLH QCL
