RHG29_RAT
ID RHG29_RAT Reviewed; 1266 AA.
AC Q5PQJ5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Rho GTPase-activating protein 29;
DE AltName: Full=Rho-type GTPase-activating protein 29;
GN Name=Arhgap29;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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-166; SER-171; SER-174;
RP SER-185; SER-549 AND SER-915, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: 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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5PQJ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5PQJ5-2; Sequence=VSP_031061;
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DR EMBL; AABR03012575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC087167; AAH87167.1; -; mRNA.
DR RefSeq; NP_001009405.1; NM_001009405.1. [Q5PQJ5-2]
DR AlphaFoldDB; Q5PQJ5; -.
DR SMR; Q5PQJ5; -.
DR BioGRID; 259768; 1.
DR STRING; 10116.ENSRNOP00000017076; -.
DR iPTMnet; Q5PQJ5; -.
DR PhosphoSitePlus; Q5PQJ5; -.
DR PaxDb; Q5PQJ5; -.
DR PRIDE; Q5PQJ5; -.
DR Ensembl; ENSRNOT00000066486; ENSRNOP00000062636; ENSRNOG00000012563. [Q5PQJ5-2]
DR GeneID; 310833; -.
DR KEGG; rno:310833; -.
DR UCSC; RGD:1306185; rat. [Q5PQJ5-1]
DR CTD; 9411; -.
DR RGD; 1306185; Arhgap29.
DR VEuPathDB; HostDB:ENSRNOG00000012563; -.
DR eggNOG; KOG1453; Eukaryota.
DR GeneTree; ENSGT00950000183110; -.
DR InParanoid; Q5PQJ5; -.
DR PhylomeDB; Q5PQJ5; -.
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:Q5PQJ5; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012563; Expressed in lung and 20 other tissues.
DR ExpressionAtlas; Q5PQJ5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; GTPase activation; Metal-binding;
KW Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1266
FT /note="Rho GTPase-activating protein 29"
FT /id="PRO_0000317584"
FT DOMAIN 187..457
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 668..883
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 609..654
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 538..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1266
FT /note="Interaction with PTPN13/PTPL1"
FT /evidence="ECO:0000250"
FT COILED 291..413
FT /evidence="ECO:0000255"
FT COMPBIAS 538..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGF1"
FT MOD_RES 1151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q52LW3"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031061"
SQ SEQUENCE 1266 AA; 141943 MW; D08AB730726E94D1 CRC64;
MIAHKQKKAK KKRVWASGQL SAAITTSEMG LKSVSSNSIF DPEYIKELVN DIRKFSHVLL
YLKEAILSDC FKEVIHIRLD ELLHMSKHQN LNSVDLQNAA ETLASKVKAV NFTEVNDENK
NDLFREVFSS IETLAFTFGN ILTNFLMGDV GNDSILRLPI SRESKSFENI SMDSVDLPHE
KGNFSPIELD NLLLKNSDSI ELALSYAKTW SKYTKNIVSW VEKKLNLELE STRNIVKLAE
ATRSSIGIQE FMPLQSLFTN ALLNDIHSSH LLQQTIAALQ ANKFVQPLLG RKNEMEKQRK
EIKELWKQQQ NKLLETETAL KKAKLLCMQR QDEYEKAKSS MFRAEEEQLS SSVGLGKNLN
KLLEKRRRLE EEALQKVEEA NEHYKVCVTN VEERRNDLEN TKREILTQLR TLVFQCDLTL
KAVTVNLFHM QQLQAASLAN SLQSLCDSAK LYDPGQEYSE FVKATSSSEL EEKVDGNVNK
QIASSPQTSG YEPADSLEDV ARLPDSCHKL EEDRCSNSAD MTGPSFIRSW KFGMFSDSES
TGGSSESRSL DSESISPGDF HRKLPRTPSS GTMSSADDLD EREPPSPSEA GPNSLGTFKK
TLMSKAALTH KFRKLRSPTK CRDCEGIVMF PGVECEECLL VCHRKCLENL VIVCGHQKLQ
GKMHIFGAEF IQVAKKEPDG IPFVLKICAS EIESRALCLQ GIYRVCGNKI KTEKLCQALE
NGMHLVDISE FSSHDICDVL KLYLRQLPEP FILFRLYKEF IDLAKEIQHV NEEQEAKKDS
PEDKKHPHVS IEINRILLRS KDLLRQLPAS NFNSLHYLIV HLKRVVDHAE ENKMNSKNLG
VIFGPTLIRP RPTTAPVTIS SLAEYSSQAR VVEFLITYAQ KIFDGSLQPQ AGVIANTGAI
APQVDHGCHP KPLLSPDERD SDHSLKQLFF SSKEDIRTMD CESKTFELTT SFEESERKQN
ALGKCDAPIL DNKVHLLFDQ ELESASHKTE DTCKSPKLLL LRSDRVANSV QRPTPRTRLR
PVSLPVDRLL LLAGSPTERS SRNTGNTDSD KFGKNAAFEG LHRKDNSNTT CSKVNGFDQQ
NVQKSWDKQN ERNSFTAKTT VIIPSAYAEK GLAVSTGNNR GHSSGAAQPS KAHADPARSA
RDTSEHSSSD SCPVAAVRAP RTLQPQHWTT FYKPPNPTFN VRGTEEKTAF PSAAVPPVLV
HAPQSHVAKS DPDLEATLAC PVQTSGQPKE SSEEPGLPEG TPTCQRPRLK RMQQFEDLED
EIPQFV
