RHG29_BOVIN
ID RHG29_BOVIN Reviewed; 1269 AA.
AC A7YY57;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Rho GTPase-activating protein 29;
DE AltName: Full=Rho-type GTPase-activating protein 29;
GN Name=ARHGAP29;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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. May act as a specific effector
CC of RAP2A to regulate Rho (By similarity). In concert with RASIP1,
CC suppresses RhoA signaling and dampens ROCK and MYH9 activities in
CC endothelial cells and plays an essential role in blood vessel
CC tubulogenesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTPN13/PTPL1. Interacts with RAP2A via its
CC coiled coil domain (By similarity). Interacts with RASIP1 (By
CC similarity). {ECO:0000250}.
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DR EMBL; BC151351; AAI51352.1; -; mRNA.
DR RefSeq; NP_001095955.1; NM_001102485.1.
DR RefSeq; XP_005204323.1; XM_005204266.2.
DR RefSeq; XP_010801599.1; XM_010803297.2.
DR AlphaFoldDB; A7YY57; -.
DR SMR; A7YY57; -.
DR STRING; 9913.ENSBTAP00000005488; -.
DR iPTMnet; A7YY57; -.
DR PaxDb; A7YY57; -.
DR PRIDE; A7YY57; -.
DR Ensembl; ENSBTAT00000005488; ENSBTAP00000005488; ENSBTAG00000004190.
DR Ensembl; ENSBTAT00000071067; ENSBTAP00000069642; ENSBTAG00000004190.
DR Ensembl; ENSBTAT00000071906; ENSBTAP00000072902; ENSBTAG00000004190.
DR GeneID; 504657; -.
DR KEGG; bta:504657; -.
DR CTD; 9411; -.
DR VEuPathDB; HostDB:ENSBTAG00000004190; -.
DR VGNC; VGNC:26087; ARHGAP29.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR HOGENOM; CLU_006236_2_0_1; -.
DR InParanoid; A7YY57; -.
DR OMA; QMIFDTP; -.
DR OrthoDB; 1300981at2759; -.
DR TreeFam; TF351450; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000004190; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; A7YY57; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:0030165; F:PDZ domain binding; IEA:Ensembl.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
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; 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; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1269
FT /note="Rho GTPase-activating protein 29"
FT /id="PRO_0000317581"
FT DOMAIN 192..462
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 671..886
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 612..657
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 472..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1269
FT /note="Interaction with PTPN13/PTPL1"
FT /evidence="ECO:0000250"
FT COILED 296..418
FT /evidence="ECO:0000255"
FT COMPBIAS 505..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 499
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQJ5"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5PQJ5"
FT MOD_RES 954
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 1152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 1154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
SQ SEQUENCE 1269 AA; 142971 MW; E31B8B0B1A492CF6 CRC64;
MIAYKQKKTK KKRVLSTGQL STDVTTSEMG LKSINSNAIL DPDYIKELVN DIRKFSHMLL
YLKEAILSEC FKEVIHIRLD ELLRVLKSVM NKHQNLNSVD LQNAAEMLIA KVKAVNFTEV
NEENKNDLFR EVFSSIETLA FTFGNILTNF LMGDVGNDSL LRLPVSQESK SFESVSVESV
DSSNEKGSFS PIELDSMLLK NTNSVELALS YAKTWSKYTK NIVSWVEKKL NLELESTRNI
VKLAEATRTN IGLQEFMPLQ SLFTNALLND IESSHLLQQT IAALQANKFV QPLLGRKNEM
EKQRKEIKEL WKQEQNKMLE TETALKKAKL LCMQRQDEYE KAKSSMFRAE EEHLSSSSGL
VKNLNRQLEK KRRLEEEALQ KVEEANELYK VCVTNVEERR NDLENTKREI LTQLRKLVFQ
CDLTLKAVTV NLFQMQQLQA ASLSSNLQSL CDSAKLYDPG QEYSEFVRAT NSAEEEKVDG
NVNKQLSSPP ISGYGPSDSL EDVVRLPDSS NKMEEDRCSN SADITGPSFL RSWTFGMFSD
SESTGGSSES RSLDSESISP GDFHRKLPRT PSSGTMSSAD DLDEREPPSP SEAGPNSLGT
FKKTLMSKAA LTHKFRKLRS PTKCRDCEGI VVFHGVECEE CLLVCHRKCL ENLVIICGHQ
KLMGKIHLFG AEFTQVAKKE PDGIPFVLKM CASEIENRAL SLQGIYRVCG NKIKTEKLCQ
ALENGMHLVD ISEFSSHDIC DVLKLYLRQL PEPFILFRLY KEFIDLAVEI QHVNEEQEMK
KDNPEDKKWP SSSIEISRIL LKSKDLLRQL PASNFNSLHY LIVHLKRVVD HSEENKMNSR
NLGVIFGPSL LRPRPTTAPI TISSLADYSN QARLVEFLIT YSQKIFDGSL QPQDSAVGSA
GGIAPQVDPG YLPKSLLSPE ERDPERSMKS LFFSSKEDIQ TTDSECKSFE STPSFEESER
KQNALEKCDA YLIDNKGRLL VDQELESASR KTEDACKTSK LPTLKSDREI NGVERHLPRT
RIRPVSLPID RLLLLASSPT ERNGRNMGNV NSDKLCKNPV FEGVNRKDSP TVVCSKFDGF
DQQTLQKTRE KQYEQNDHTA KTGMIVPSAF QERGVALNIR SSGDHPVSIT QPSKPYTEPV
RSTRQVSERR SSDSCPPASV RTPRTLQPQH WTTFYKPPAP AASGRGDEEK PVTPSVAVPP
GTTHAPQEHV LKSVPGSENA SAGPVHPVSR PEEKAEERDQ PDVPTACQRP RLKRMQQFED
LEDEIPQFV
