RHG24_RAT
ID RHG24_RAT Reviewed; 748 AA.
AC Q5U2Z7; Q6I7R2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Rho GTPase-activating protein 24;
DE AltName: Full=Down-regulated in nephrectomized rat kidney #2;
DE AltName: Full=Rho-type GTPase-activating protein 24;
GN Name=Arhgap24; ORFNames=DR-NR#2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND INDUCTION.
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=15200410; DOI=10.1111/j.1523-1755.2004.00704.x;
RA Horiba N., Masuda S., Takeuchi A., Saito H., Okuda M., Inui K.;
RT "Gene expression variance based on random sequencing in rat remnant
RT kidney.";
RL Kidney Int. 66:29-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-159 (ISOFORM 1).
RG Amgen EST program;
RT "Amgen rat EST program.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369; SER-391; SER-398 AND
RP SER-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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=Q5U2Z7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U2Z7-2; Sequence=VSP_023723, VSP_023724;
CC Name=3;
CC IsoId=Q5U2Z7-3; Sequence=VSP_023722;
CC -!- INDUCTION: Down-regulated after nephrectomy.
CC {ECO:0000269|PubMed:15200410}.
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}.
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DR EMBL; AB108670; BAD23895.1; -; mRNA.
DR EMBL; BC085797; AAH85797.1; -; mRNA.
DR EMBL; CB609913; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001012032.1; NM_001012032.1. [Q5U2Z7-2]
DR AlphaFoldDB; Q5U2Z7; -.
DR SMR; Q5U2Z7; -.
DR STRING; 10116.ENSRNOP00000002857; -.
DR iPTMnet; Q5U2Z7; -.
DR PhosphoSitePlus; Q5U2Z7; -.
DR PaxDb; Q5U2Z7; -.
DR PRIDE; Q5U2Z7; -.
DR Ensembl; ENSRNOT00000080758; ENSRNOP00000072212; ENSRNOG00000056944. [Q5U2Z7-1]
DR GeneID; 305156; -.
DR KEGG; rno:305156; -.
DR CTD; 83478; -.
DR RGD; 1306669; Arhgap24.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00950000183015; -.
DR InParanoid; Q5U2Z7; -.
DR OMA; ELLYYYK; -.
DR OrthoDB; 917149at2759; -.
DR PhylomeDB; Q5U2Z7; -.
DR TreeFam; TF323577; -.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q5U2Z7; -.
DR Proteomes; UP000002494; Chromosome 14.
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; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; ISO:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1900028; P:negative regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISO:RGD.
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..748
FT /note="Rho GTPase-activating protein 24"
FT /id="PRO_0000280475"
FT DOMAIN 18..124
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 134..328
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 328..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 649..729
FT /evidence="ECO:0000255"
FT COMPBIAS 336..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..640
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4V1"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 452
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N264"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C4V1"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15200410"
FT /id="VSP_023722"
FT VAR_SEQ 1..91
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023723"
FT VAR_SEQ 92..129
FT /note="RDRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG -> MPEDRNSGGR
FT PSGALASTPFIPKTTYRRIKRCFSFRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023724"
FT CONFLICT 355
FT /note="M -> I (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="S -> R (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="A -> G (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="T -> S (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="K -> E (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="M -> W (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="I -> Y (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="A -> G (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="G -> S (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="S -> R (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="E -> D (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="V -> F (in Ref. 1; BAD23895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 84144 MW; CEEC20AD771784A7 CRC64;
MEENCDSTEN PHSQGRQNAT KCGWLRKQGG FVKTWHTRWF VLKGDQLHYF KDEDETKPLG
TIFLPGNKVI EHPCNEESPG KFLFEVVPGG ERDRMTANHE SYLLMASTQN DMEDWVKSIR
RVIWGPFGGG IFGQKLEDTV RYEKRYGNRL APMLVEQCVD FIRQRGLKEE GLFRLPGQAN
LVKELQDAFD CGEKPSFDSN TDVHTVASLL KLYLRELPEP VVPYAKYEDF LSCATLLSKE
EEAGVKELTK QVKSLPVVNY NLLKYICRFL DEVQSYSGVN KMSAQNLATV FGPNILRPKV
EDPLTIMEGT VVVQQLMSVM ISKHDRLFPK DTEPQSKPQE GPNSNNNDGH KKVTMGQLQN
KENNNTKESP VRRCSWDKPE SPQRSSMDNG SPTALSGSKT NSPRNSIHKL DVSRSPPLTV
KKNPAFNKGS GIVTNGSFSS SNAEGVEKTQ TTPNGSLQAR RTSSLKSSGT KMGTHSVQNG
TVRMGILNTD TLGNSLNGRS MSWLPNGYVT LRDNKQKEPA GESGQHNRLS TYDNVHQQFS
LMNLDDKHSV DSATWSTSSC EISLPENSNS CRSSTTTCPE QDFYGGNFED PVLDGPPQDD
LSHPGDYENK SDRRSVGGRS SRATSSSDNS ETFVGNTSSN HSALHSLVSS LKQEMTKQKI
EYESRIKSLE QRNLTLETEM LNLHDELDQE RKKFTMIEIK MRNAERAKED AEKRNDMLQK
EMEQFFSTFG DLTVEPRRSE RGNTIWIQ
