RHG24_MOUSE
ID RHG24_MOUSE Reviewed; 747 AA.
AC Q8C4V1; Q8CA50; Q8QZZ0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Rho GTPase-activating protein 24;
DE AltName: Full=Rho-type GTPase-activating protein 24;
GN Name=Arhgap24;
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 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-358 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Spinal cord;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Eye, Kidney, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-395; SER-397 AND
RP SER-494, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Pancreas;
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: Rho GTPase-activating protein involved in cell polarity, cell
CC morphology and cytoskeletal organization. Acts as a GTPase activator
CC for the Rac-type GTPase by converting it to an inactive GDP-bound
CC state. Controls actin remodeling by inactivating Rac downstream of Rho
CC leading to suppress leading edge protrusion and promotes cell
CC retraction to achieve cellular polarity. Able to suppress RAC1 and
CC CDC42 activity in vitro. Overexpression induces cell rounding with
CC partial or complete disruption of actin stress fibers and formation of
CC membrane ruffles, lamellipodia, and filopodia. Isoform 2 is a vascular
CC cell-specific GAP involved in modulation of angiogenesis (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FLNA. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction, adherens junction {ECO:0000250}. Cell junction, focal
CC adhesion {ECO:0000250}. Cell projection {ECO:0000250}. Note=Localizes
CC to actin stress fibers. In migrating cells, localizes to membrane
CC lamellae and protusions (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8C4V1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C4V1-2; Sequence=VSP_023720, VSP_023721;
CC Name=3;
CC IsoId=Q8C4V1-3; Sequence=VSP_023719;
CC -!- DOMAIN: The coiled coil domain mediates the interaction with FLNA
CC leading to its recruitment to lamellae. {ECO:0000250}.
CC -!- PTM: Phosphorylated by ROCK, leading to activate the RacGAP activity.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC30402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK039617; BAC30402.1; ALT_INIT; mRNA.
DR EMBL; AK080986; BAC38105.1; -; mRNA.
DR EMBL; BC023344; AAH23344.1; -; mRNA.
DR EMBL; BC025502; AAH25502.1; -; mRNA.
DR EMBL; BC027070; AAH27070.1; -; mRNA.
DR CCDS; CCDS19474.1; -. [Q8C4V1-1]
DR CCDS; CCDS19475.1; -. [Q8C4V1-3]
DR RefSeq; NP_001273397.1; NM_001286468.1. [Q8C4V1-3]
DR RefSeq; NP_083546.2; NM_029270.2.
DR RefSeq; NP_666273.1; NM_146161.3. [Q8C4V1-3]
DR RefSeq; XP_006534954.1; XM_006534891.3. [Q8C4V1-3]
DR RefSeq; XP_011247736.1; XM_011249434.2. [Q8C4V1-3]
DR AlphaFoldDB; Q8C4V1; -.
DR SMR; Q8C4V1; -.
DR BioGRID; 231132; 4.
DR IntAct; Q8C4V1; 1.
DR STRING; 10090.ENSMUSP00000092138; -.
DR iPTMnet; Q8C4V1; -.
DR PhosphoSitePlus; Q8C4V1; -.
DR jPOST; Q8C4V1; -.
DR MaxQB; Q8C4V1; -.
DR PaxDb; Q8C4V1; -.
DR PRIDE; Q8C4V1; -.
DR ProteomicsDB; 254962; -. [Q8C4V1-1]
DR ProteomicsDB; 254963; -. [Q8C4V1-2]
DR ProteomicsDB; 254964; -. [Q8C4V1-3]
DR Antibodypedia; 2133; 175 antibodies from 23 providers.
DR DNASU; 231532; -.
DR Ensembl; ENSMUST00000073302; ENSMUSP00000073028; ENSMUSG00000057315. [Q8C4V1-3]
DR Ensembl; ENSMUST00000112852; ENSMUSP00000108473; ENSMUSG00000057315. [Q8C4V1-3]
DR Ensembl; ENSMUST00000112853; ENSMUSP00000108474; ENSMUSG00000057315. [Q8C4V1-3]
DR Ensembl; ENSMUST00000112854; ENSMUSP00000108475; ENSMUSG00000057315. [Q8C4V1-3]
DR GeneID; 231532; -.
DR KEGG; mmu:231532; -.
DR UCSC; uc008yix.2; mouse. [Q8C4V1-1]
DR UCSC; uc008yiz.1; mouse. [Q8C4V1-2]
DR CTD; 83478; -.
DR MGI; MGI:1922647; Arhgap24.
DR VEuPathDB; HostDB:ENSMUSG00000057315; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR HOGENOM; CLU_020795_0_0_1; -.
DR InParanoid; Q8C4V1; -.
DR OMA; ELLYYYK; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; Q8C4V1; -.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR BioGRID-ORCS; 231532; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Arhgap24; mouse.
DR PRO; PR:Q8C4V1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8C4V1; protein.
DR Bgee; ENSMUSG00000057315; Expressed in epithelium of lens and 240 other tissues.
DR ExpressionAtlas; Q8C4V1; baseline and differential.
DR Genevisible; Q8C4V1; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IMP:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IMP:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IMP:MGI.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; IMP:MGI.
DR GO; GO:0016601; P:Rac protein signal transduction; IMP:MGI.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:MGI.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; Cell junction; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..747
FT /note="Rho GTPase-activating protein 24"
FT /id="PRO_0000280474"
FT DOMAIN 17..123
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 133..327
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 648..728
FT /evidence="ECO:0000255"
FT COMPBIAS 335..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 617..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U2Z7"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 451
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023719"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023720"
FT VAR_SEQ 92..128
FT /note="DRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG -> MPEDRNSGGRP
FT SGALASTPFIPKTTYRRIKRCFSFRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023721"
FT CONFLICT 183
FT /note="E -> K (in Ref. 1; BAC38105)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 747 AA; 84100 MW; 769982BA6B90D425 CRC64;
MEERCESTES PQGQGRKNTK CGWLRKQGGF VKTWHTRWFV LKGDQLYYFK DEDETKPLGT
IFLHGNKVIE HPCNEENPGK FLFDVVPGGE RDRMTANHES YLLMASTQND MEDWVKSIRR
VIWGPFGGGI FGQKLEDTVR YEKRYGNRLA PMLVEQCVDF IRQRGLKEEG LFRLPGQANL
VKELQDAFDC GEKPSFDSNT DVHTVASLLK LYLRELPEPV VPYAKYEDFL SCATLLSKEE
EAGVKELMKQ VKSLPVVNYN LLKYICRFLD EVQSYSGVNK MSAQNLATVF GPNILRPKVE
DPLTIMEGTV VVQQLMSVMI SKHDRLFPKD TEPQSKPQDG PNSNNNDGHK KATMGQLQNK
ENNNTKESPV RRCSWDKPES PQRSSVDNGS PTALSGSKTN SPRNSIHKLD ISRSPPLMVK
KNPAFNKGSG IVTNGSFSSS NAEGVEKPQT TPNGSLQARR TSSLKSSGTK MGTHSVQNGT
VRMGILNTDT LGNSLNGRSM SWLPNGYVTL RDNKQKEPAG ESGQHNRLST YDNVHQQFSS
MSLDDKHSVD SATWSTSSCE ISLPENSNSC RSSTTTCPEQ DFYVGNFEDP VLDGPPQDDL
SHPGDYENKS DRRSVGGRSS RATSSSDNSE TFVGNTSSNH SALHSLVSSL KQEMTKQKIE
YESRIKSLEQ RNLTLETEML SLHDELDQER KKFTMIEIKM RNAERAKEDA EKRNDMLQKE
MEQFFSTFGD LTVEPRRSER GNTIWIQ
