RHG17_MOUSE
ID RHG17_MOUSE Reviewed; 846 AA.
AC Q3UIA2; Q3UDP7; Q8BGD1; Q99LH3; Q99N39; Q99N40;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Rho GTPase-activating protein 17;
DE AltName: Full=Neuron-associated developmentally-regulated protein;
DE Short=Nadrin;
DE AltName: Full=Rho-type GTPase-activating protein 17;
GN Name=Arhgap17;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10967100; DOI=10.1074/jbc.m004069200;
RA Harada A., Furuta B., Takeuchi K., Itakura M., Takahashi M., Umeda M.;
RT "Nadrin, a novel neuron-specific GTPase-activating protein involved in
RT regulated exocytosis.";
RL J. Biol. Chem. 275:36885-36891(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-575; SER-698;
RP SER-700; THR-730; THR-734; THR-736; SER-739 AND THR-740, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the maintenance of
CC tight junction by regulating the activity of CDC42, thereby playing a
CC central role in apical polarity of epithelial cells. Specifically acts
CC as a GTPase activator for the CDC42 GTPase by converting it to an
CC inactive GDP-bound state. The complex formed with AMOT acts by
CC regulating the uptake of polarity proteins at tight junctions, possibly
CC by deciding whether tight junction transmembrane proteins are recycled
CC back to the plasma membrane or sent elsewhere. Participates in the
CC Ca(2+)-dependent regulation of exocytosis, possibly by catalyzing
CC GTPase activity of Rho family proteins and by inducing the
CC reorganization of the cortical actin filaments. Acts as a GTPase
CC activator in vitro for RAC1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex whose core is composed of ARHGAP17,
CC AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1,
CC TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and
CC SH3KBP1/CIN85 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Cell junction, tight
CC junction {ECO:0000250}. Note=Associates with membranes and concentrates
CC at sites of cell-cell contact. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Nadrin-1;
CC IsoId=Q3UIA2-1; Sequence=Displayed;
CC Name=2; Synonyms=Nadrin-2;
CC IsoId=Q3UIA2-2; Sequence=VSP_023690;
CC Name=3;
CC IsoId=Q3UIA2-3; Sequence=VSP_023690, VSP_023691;
CC Name=4;
CC IsoId=Q3UIA2-4; Sequence=VSP_023690, VSP_023692;
CC -!- DOMAIN: The BAR domain mediates the interaction with the coiled coil
CC domain of AMOT, leading to its recruitment to tight junctions.
CC {ECO:0000250}.
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DR EMBL; AB060553; BAB43862.1; -; mRNA.
DR EMBL; AB060554; BAB43863.1; -; mRNA.
DR EMBL; AK036468; BAC29443.1; -; mRNA.
DR EMBL; AK036617; BAC29508.1; -; mRNA.
DR EMBL; AK147010; BAE27604.1; -; mRNA.
DR EMBL; AK149986; BAE29214.1; -; mRNA.
DR EMBL; AK152266; BAE31084.1; -; mRNA.
DR EMBL; BC003259; AAH03259.1; -; mRNA.
DR CCDS; CCDS52388.1; -. [Q3UIA2-4]
DR CCDS; CCDS52389.1; -. [Q3UIA2-1]
DR CCDS; CCDS85404.1; -. [Q3UIA2-2]
DR CCDS; CCDS85405.1; -. [Q3UIA2-3]
DR RefSeq; NP_001116112.1; NM_001122640.1.
DR RefSeq; NP_001116113.1; NM_001122641.1. [Q3UIA2-2]
DR RefSeq; NP_001116114.1; NM_001122642.1. [Q3UIA2-3]
DR RefSeq; NP_001116115.1; NM_001122643.1. [Q3UIA2-4]
DR RefSeq; NP_001303642.1; NM_001316713.1.
DR RefSeq; NP_653112.2; NM_144529.2. [Q3UIA2-1]
DR AlphaFoldDB; Q3UIA2; -.
DR SMR; Q3UIA2; -.
DR BioGRID; 214096; 2.
DR STRING; 10090.ENSMUSP00000102050; -.
DR iPTMnet; Q3UIA2; -.
DR PhosphoSitePlus; Q3UIA2; -.
DR EPD; Q3UIA2; -.
DR jPOST; Q3UIA2; -.
DR MaxQB; Q3UIA2; -.
DR PaxDb; Q3UIA2; -.
DR PeptideAtlas; Q3UIA2; -.
DR PRIDE; Q3UIA2; -.
DR ProteomicsDB; 254869; -. [Q3UIA2-1]
DR ProteomicsDB; 254870; -. [Q3UIA2-2]
DR ProteomicsDB; 254871; -. [Q3UIA2-3]
DR ProteomicsDB; 254872; -. [Q3UIA2-4]
DR Antibodypedia; 52174; 182 antibodies from 27 providers.
DR DNASU; 70497; -.
DR Ensembl; ENSMUST00000098060; ENSMUSP00000095668; ENSMUSG00000030766. [Q3UIA2-2]
DR Ensembl; ENSMUST00000106442; ENSMUSP00000102050; ENSMUSG00000030766. [Q3UIA2-1]
DR Ensembl; ENSMUST00000205262; ENSMUSP00000146035; ENSMUSG00000030766. [Q3UIA2-4]
DR Ensembl; ENSMUST00000207010; ENSMUSP00000145628; ENSMUSG00000030766. [Q3UIA2-3]
DR GeneID; 70497; -.
DR KEGG; mmu:70497; -.
DR UCSC; uc009jpi.2; mouse. [Q3UIA2-1]
DR UCSC; uc009jpk.2; mouse. [Q3UIA2-4]
DR UCSC; uc009jpm.2; mouse. [Q3UIA2-3]
DR UCSC; uc009jpn.2; mouse. [Q3UIA2-2]
DR CTD; 55114; -.
DR MGI; MGI:1917747; Arhgap17.
DR VEuPathDB; HostDB:ENSMUSG00000030766; -.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000156201; -.
DR HOGENOM; CLU_013806_0_0_1; -.
DR InParanoid; Q3UIA2; -.
DR OMA; RLMGCFQ; -.
DR OrthoDB; 821331at2759; -.
DR PhylomeDB; Q3UIA2; -.
DR TreeFam; TF350627; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013405; RHOD GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 70497; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Arhgap17; mouse.
DR PRO; PR:Q3UIA2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UIA2; protein.
DR Bgee; ENSMUSG00000030766; Expressed in lymph node and 253 other tissues.
DR ExpressionAtlas; Q3UIA2; baseline and differential.
DR Genevisible; Q3UIA2; MM.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0035020; P:regulation of Rac protein signal transduction; 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; IPR004148; BAR_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cytoplasm; GTPase activation;
KW Membrane; Phosphoprotein; Reference proteome; SH3-binding; Tight junction.
FT CHAIN 1..846
FT /note="Rho GTPase-activating protein 17"
FT /id="PRO_0000280463"
FT DOMAIN 14..246
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 252..442
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 459..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 730..743
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 522..536
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..744
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 730
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 736
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 739
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 497..574
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10967100,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_023690"
FT VAR_SEQ 805..846
FT /note="TNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTAL -> ALPGAL
FT TGGEGFQN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023691"
FT VAR_SEQ 805..846
FT /note="TNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTAL -> V (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023692"
FT CONFLICT 207
FT /note="E -> K (in Ref. 1; BAB43862/BAB43863)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="F -> I (in Ref. 2; BAE29214)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="N -> D (in Ref. 1; BAB43862/BAB43863)"
FT /evidence="ECO:0000305"
FT CONFLICT 674..676
FT /note="Missing (in Ref. 3; AAH03259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 92202 MW; 3D12B030B41E6987 CRC64;
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SMCHHSHKRL IACFQGQHGT
DAERRHKKLP LTALAQNMQE ASAQLEESLL GKMLETCGDA ENQLALELSQ HEVFVEKEIM
DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM
DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKALPEMRAH
QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFSL YEEWTQVASV QDQDKKLQYL
WTTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA KQEGTLAEIA
AATSVHVVAV IEPIIQHADW FFPGEVEFNV SEAFVPLATP NSNHSSHTGN DSDSGTLERK
RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIA PAFQPPLPPT DGNALAPAGP
EPPSQSSRAD SSSGGGPVFS STGILEQGLS PGDSSPPKPK DSVSAAVPAA GRNSNQMTTV
PNQAQTGGNS HQLSVSTPHS AAGPSPHTLR RAVKKPAPAP PKPGNLPPGH PGGQSSPGTG
TSPKPSARSP SPPQQQQQQQ QQQQQQQQQQ TPGMRRCSSS LPPIQAPSHP PPQPPTQPRL
GEQGPEPGPT PPQTPTPPST PPLAKQNPSQ SETTQLHGTL PRPRPVPKPR NRPSVPPPPH
PPGTHTVDGG LTSSVPTASR IVTDTNSRVS ESLRSIFPEI HSDLASKEVP GHILLDIDND
TESTAL
