ID   RHG29_DANRE             Reviewed;        1337 AA.
AC   Q6PCS4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Rho GTPase-activating protein 29;
DE   AltName: Full=Rho-type GTPase-activating protein 29;
GN   Name=arhgap29; ORFNames=zgc:63950;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting them
CC       to an inactive GDP-bound state. Has strong activity toward RHOA, and
CC       weaker activity toward RAC1 and CDC42 (By similarity). {ECO:0000250}.
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DR   EMBL; BC059184; AAH59184.1; -; mRNA.
DR   RefSeq; NP_956405.1; NM_200111.1.
DR   AlphaFoldDB; Q6PCS4; -.
DR   SMR; Q6PCS4; -.
DR   STRING; 7955.ENSDARP00000115452; -.
DR   PaxDb; Q6PCS4; -.
DR   GeneID; 378998; -.
DR   KEGG; dre:378998; -.
DR   CTD; 378998; -.
DR   ZFIN; ZDB-GENE-031010-44; arhgap29b.
DR   eggNOG; KOG1453; Eukaryota.
DR   InParanoid; Q6PCS4; -.
DR   OrthoDB; 1300981at2759; -.
DR   PhylomeDB; Q6PCS4; -.
DR   PRO; PR:Q6PCS4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00029; C1; 1.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 1.20.1270.60; -; 1.
DR   InterPro; IPR027267; AH/BAR_dom_sf.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR031160; F_BAR.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF103657; SSF103657; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF57889; SSF57889; 1.
DR   PROSITE; PS51741; F_BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; GTPase activation; Metal-binding; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1337
FT                   /note="Rho GTPase-activating protein 29"
FT                   /id="PRO_0000317585"
FT   DOMAIN          225..488
FT                   /note="F-BAR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT   DOMAIN          737..950
FT                   /note="Rho-GAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT   ZN_FING         676..723
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          369..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..983
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1066
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1273..1337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          326..443
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        513..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        567..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..975
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1051
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1083..1105
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1291..1313
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1318..1337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1337 AA;  147666 MW;  2061AE2507489079 CRC64;
     MFRQGSNSGN KRMTSGARLS QPIIPLSLPT ASSKTLEMGR SSKTNPLNAM GLDHNIATSG
     GDPEYIMQLV NDVRKFSDVL LSLKEAFHSK ESQECSQHVV NERLGELVHV LKAVIGKHQA
     LNSSEILGAA GTVIAKVKGV NFKEVNNENK STIFGEIHTS IDTLAFTFGN VVSDFLMGDV
     DGGSRLGYPQ ARRSRSFENL SEDSRGCSQN DLADHSLSPE LSTVEQVDLL LLKNDSGVES
     ALLYAKAWSK YTKDVLAWVE KRLSLDMECA KSFAKMAESA KAVASQQDFM PFRDIYVSAF
     KNEIEYNHVL LQTAAALQTN KFTQPLLARK NDLDKQRKEI KEQWQRELKK MNESESALKK
     ARLLKMQKRE EYEKARSSTS RTEEEQPAAG GRTLEKKRRV EEEALQKAEE AQEQYKACVA
     DLEAKKVSLS NAKSEILAQI RKLVFQCDLT LKAVTVNWFQ MQQAQTMPLS VNYQALSEQA
     KKYEPGQRYS EFVRSLPKER VWLESLSQDI TASSKTGMSL HKRSQNSTRS SHGNLSQGSA
     TSMDNHSADE VEGNMQPCKA KIAERRSNSS IDMQVPRTQG SQRAWSSGSA GGGGMCSDSE
     SAGGSSESRS MDSPTASPGD FKRRLPRTPS TGTMSSADDL DEREPPSPSD TGLSEMVMET
     ASSPGPFRNA QMSKAAHTHK LRKLRAPSKC RECDSLVVFH GAECEECSLA CHKKCLETLA
     IQCGHKKLQG RLHLFGIDFA QVVKNSPDGI PFIIKKCTSE IESRALTIKG IYRVNGAKSR
     VEKLCQAFEN GKDLVELSDL HPHDISNVLK LYLRQLPEPL ILYRYYNDVI GLAKETQNMD
     KTDSAKEKSA GEQLGLSTEL KRVLFKVRDL LRQLPAPHYK TLQFLITHLH RVSEQAEENK
     MTASNLGIIF GPTLIKPRHL EAEVSLSSLV DYPHQARMVE LLIKHHQMIF DVPLSPMSPT
     SPTVSQASFG SSIQDKESKL SRHSRSLMDI KESAKLYKRH SSVIIPAQLM EEGKEMKTGD
     HRVQTSGEGS DVNGVGLTSV DSTSVFNRPG ASSRMVQLRP QRAKPVSRPI SMPIDRLLNE
     RNSRNTVEHD HSPAAIEETT EPEKPTTPRH TNFYRNPFID TQTLRRTWDR QYRHYDVTPR
     TAMIVANLPP SGVQKQPEIS MASQSSTSRK DGTSQSGVAP ISFRAARTLK PSSPGTFYRP
     PSGGQLKPSD LLAKSVSRAP TTTTGAIYTT AITVLTTAST SSVMTISTAV TTPPTTPTTS
     VTVALTSKPT FTTVSRSVSG GAGEGLSESD LLSPVTLSPP QSPGSSTEEL SPTDAKPLYQ
     RRSRRMQELE HREAHFV