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Rho GTPase-activating protein 24 (Down-regulated in nephrectomized rat kidney #2) (Rho-type GTPase-activating protein 24)

 RHG24_RAT               Reviewed;         748 AA.
Q5U2Z7; Q6I7R2;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
20-MAR-2007, sequence version 2.
23-MAY-2018, entry version 112.
RecName: Full=Rho GTPase-activating protein 24;
AltName: Full=Down-regulated in nephrectomized rat kidney #2;
AltName: Full=Rho-type GTPase-activating protein 24;
Name=Arhgap24; ORFNames=DR-NR#2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND INDUCTION.
STRAIN=Wistar; TISSUE=Kidney;
PubMed=15200410; DOI=10.1111/j.1523-1755.2004.00704.x;
Horiba N., Masuda S., Takeuchi A., Saito H., Okuda M., Inui K.;
"Gene expression variance based on random sequencing in rat remnant
kidney.";
Kidney Int. 66:29-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-159 (ISOFORM 1).
Amgen EST program;
"Amgen rat EST program.";
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369; SER-391; SER-398
AND SER-415, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Rho GTPase-activating protein involved in cell polarity,
cell morphology and cytoskeletal organization. Acts as a GTPase
activator for the Rac-type GTPase by converting it to an inactive
GDP-bound state. Controls actin remodeling by inactivating Rac
downstream of Rho leading to suppress leading edge protrusion and
promotes cell retraction to achieve cellular polarity. Able to
suppress RAC1 and CDC42 activity in vitro. Overexpression induces
cell rounding with partial or complete disruption of actin stress
fibers and formation of membrane ruffles, lamellipodia, and
filopodia. Isoform 2 is a vascular cell-specific GAP involved in
modulation of angiogenesis (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with FLNA. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
junction, adherens junction {ECO:0000250}. Cell junction, focal
adhesion {ECO:0000250}. Cell projection {ECO:0000250}.
Note=Localizes to actin stress fibers. In migrating cells,
localizes to membrane lamellae and protusions (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5U2Z7-1; Sequence=Displayed;
Name=2;
IsoId=Q5U2Z7-2; Sequence=VSP_023723, VSP_023724;
Name=3;
IsoId=Q5U2Z7-3; Sequence=VSP_023722;
Note=No experimental confirmation available.;
-!- INDUCTION: Down-regulated after nephrectomy.
{ECO:0000269|PubMed:15200410}.
-!- DOMAIN: The coiled coil domain mediates the interaction with FLNA
leading to its recruitment to lamellae. {ECO:0000250}.
-!- PTM: Phosphorylated by ROCK, leading to activate the RacGAP
activity. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AB108670; BAD23895.1; -; mRNA.
EMBL; BC085797; AAH85797.1; -; mRNA.
EMBL; CB609913; -; NOT_ANNOTATED_CDS; mRNA.
RefSeq; NP_001012032.1; NM_001012032.1. [Q5U2Z7-2]
UniGene; Rn.24657; -.
ProteinModelPortal; Q5U2Z7; -.
SMR; Q5U2Z7; -.
STRING; 10116.ENSRNOP00000002857; -.
iPTMnet; Q5U2Z7; -.
PhosphoSitePlus; Q5U2Z7; -.
PaxDb; Q5U2Z7; -.
PRIDE; Q5U2Z7; -.
GeneID; 305156; -.
KEGG; rno:305156; -.
CTD; 83478; -.
RGD; 1306669; Arhgap24.
eggNOG; KOG4270; Eukaryota.
eggNOG; ENOG410XRR2; LUCA.
HOGENOM; HOG000232151; -.
HOVERGEN; HBG058875; -.
InParanoid; Q5U2Z7; -.
KO; K20642; -.
OMA; LLKYICR; -.
PhylomeDB; Q5U2Z7; -.
TreeFam; TF323577; -.
PRO; PR:Q5U2Z7; -.
Proteomes; UP000002494; Unplaced.
Bgee; ENSRNOG00000056944; -.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
Pfam; PF00169; PH; 1.
Pfam; PF00620; RhoGAP; 1.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Cell junction; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; GTPase activation;
Phosphoprotein; Reference proteome.
CHAIN 1 748 Rho GTPase-activating protein 24.
/FTId=PRO_0000280475.
DOMAIN 18 124 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 134 328 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
COILED 649 729 {ECO:0000255}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C4V1}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N264}.
MOD_RES 413 413 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N264}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:Q8N264}.
MOD_RES 452 452 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8N264}.
MOD_RES 495 495 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C4V1}.
VAR_SEQ 1 152 Missing (in isoform 3).
{ECO:0000303|PubMed:15200410}.
/FTId=VSP_023722.
VAR_SEQ 1 91 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023723.
VAR_SEQ 92 129 RDRMTANHESYLLMASTQNDMEDWVKSIRRVIWGPFGG ->
MPEDRNSGGRPSGALASTPFIPKTTYRRIKRCFSFRK (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023724.
CONFLICT 355 355 M -> I (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 430 430 S -> R (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 443 443 A -> G (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 462 462 T -> S (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 466 466 K -> E (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 472 472 M -> W (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 486 486 I -> Y (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 520 520 A -> G (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 524 524 G -> S (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 549 549 S -> R (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 631 631 E -> D (in Ref. 1; BAD23895).
{ECO:0000305}.
CONFLICT 634 634 V -> F (in Ref. 1; BAD23895).
{ECO:0000305}.
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


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