Full text data of ARHGAP17
ARHGAP17
(RICH1)
[Confidence: low (only semi-automatic identification from reviews)]
Rho GTPase-activating protein 17 (Rho-type GTPase-activating protein 17; RhoGAP interacting with CIP4 homologs protein 1; RICH-1)
Rho GTPase-activating protein 17 (Rho-type GTPase-activating protein 17; RhoGAP interacting with CIP4 homologs protein 1; RICH-1)
UniProt
Q68EM7
ID RHG17_HUMAN Reviewed; 881 AA.
AC Q68EM7; A8K6M6; Q6ZUS4; Q7Z2F2; Q8NDG2; Q96KS2; Q96KS3; Q96SS8;
read moreAC Q9BVF6; Q9H8U5; Q9NW54;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Rho GTPase-activating protein 17;
DE AltName: Full=Rho-type GTPase-activating protein 17;
DE AltName: Full=RhoGAP interacting with CIP4 homologs protein 1;
DE Short=RICH-1;
GN Name=ARHGAP17; Synonyms=RICH1; ORFNames=MSTP066, MSTP110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, AND
RP MUTAGENESIS OF ARG-288.
RX PubMed=11431473; DOI=10.1074/jbc.M103540200;
RA Richnau N., Aspenstroem P.;
RT "Rich, a rho GTPase-activating protein domain-containing protein
RT involved in signaling by Cdc42 and Rac1.";
RL J. Biol. Chem. 276:35060-35070(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5).
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6).
RC TISSUE=Cervix, and Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881.
RC TISSUE=Aorta;
RA Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y.,
RA Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=11285285; DOI=10.1083/jcb.153.1.191;
RA Reczek D., Bretscher A.;
RT "Identification of EPI64, a TBC/rabGAP domain-containing microvillar
RT protein that binds to the first PDZ domain of EBP50 and E3KARP.";
RL J. Cell Biol. 153:191-206(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, AND INTERACTION WITH AMOT;
RP MPP5; INADL; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the
CC maintenance of tight junction by regulating the activity of CDC42,
CC thereby playing a central role in apical polarity of epithelial
CC cells. Specifically acts as a GTPase activator for the CDC42
CC GTPase by converting it to an inactive GDP-bound state. The
CC complex formed with AMOT acts by regulating the uptake of polarity
CC proteins at tight junctions, possibly by deciding whether tight
CC junction transmembrane proteins are recycled back to the plasma
CC membrane or sent elsewhere. Participates in the Ca(2+)-dependent
CC regulation of exocytosis, possibly by catalyzing GTPase activity
CC of Rho family proteins and by inducing the reorganization of the
CC cortical actin filaments. Acts as a GTPase activator in vitro for
CC RAC1.
CC -!- SUBUNIT: Component of a complex whose core is composed of
CC ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts
CC with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3),
CC CAPZB, CD2AP and SH3KBP1/CIN85.
CC -!- INTERACTION:
CC Q4VCS5:AMOT; NbExp=2; IntAct=EBI-1642807, EBI-2511319;
CC Q4VCS5-2:AMOT; NbExp=4; IntAct=EBI-1642807, EBI-3891843;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC Cytoplasm. Cell junction, tight junction. Note=Associates with
CC membranes and concentrates at sites of cell-cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q68EM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68EM7-2; Sequence=VSP_023687;
CC Name=3;
CC IsoId=Q68EM7-3; Sequence=VSP_023683;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=RICH1B;
CC IsoId=Q68EM7-4; Sequence=VSP_023684, VSP_023685;
CC Name=5;
CC IsoId=Q68EM7-5; Sequence=VSP_023688;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q68EM7-6; Sequence=VSP_023689;
CC Name=7;
CC IsoId=Q68EM7-7; Sequence=VSP_023682, VSP_023686;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher
CC level in heart and placenta.
CC -!- DOMAIN: The BAR domain mediates the interaction with the coiled
CC coil domain of AMOT, leading to its recruitment to tight
CC junctions.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01241.1; Type=Erroneous initiation;
CC Sequence=AAQ13586.1; Type=Erroneous initiation;
CC Sequence=AAQ13632.1; Type=Erroneous initiation;
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DR EMBL; AJ306731; CAC37948.1; -; mRNA.
DR EMBL; AJ306732; CAC37949.1; -; mRNA.
DR EMBL; AK001170; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK023281; BAB14506.1; -; mRNA.
DR EMBL; AK027567; BAB55203.1; -; mRNA.
DR EMBL; AK125358; BAC86144.1; -; mRNA.
DR EMBL; AK291691; BAF84380.1; -; mRNA.
DR EMBL; AL833975; CAD38819.1; -; mRNA.
DR EMBL; BC001241; AAH01241.1; ALT_INIT; mRNA.
DR EMBL; BC080195; AAH80195.1; -; mRNA.
DR EMBL; AF163257; AAQ13586.1; ALT_INIT; mRNA.
DR EMBL; AF173885; AAQ13632.1; ALT_INIT; mRNA.
DR PIR; F59433; F59433.
DR RefSeq; NP_001006635.1; NM_001006634.1.
DR RefSeq; NP_060524.4; NM_018054.4.
DR RefSeq; XP_005255471.1; XM_005255414.1.
DR UniGene; Hs.373793; -.
DR ProteinModelPortal; Q68EM7; -.
DR SMR; Q68EM7; 25-232, 246-442.
DR IntAct; Q68EM7; 7.
DR MINT; MINT-195688; -.
DR PhosphoSite; Q68EM7; -.
DR DMDM; 74736331; -.
DR PaxDb; Q68EM7; -.
DR PRIDE; Q68EM7; -.
DR Ensembl; ENST00000289968; ENSP00000289968; ENSG00000140750.
DR Ensembl; ENST00000303665; ENSP00000303130; ENSG00000140750.
DR Ensembl; ENST00000441763; ENSP00000406950; ENSG00000140750.
DR GeneID; 55114; -.
DR KEGG; hsa:55114; -.
DR UCSC; uc002dna.3; human.
DR CTD; 55114; -.
DR GeneCards; GC16M024931; -.
DR HGNC; HGNC:18239; ARHGAP17.
DR HPA; HPA041703; -.
DR MIM; 608293; gene.
DR neXtProt; NX_Q68EM7; -.
DR PharmGKB; PA134908575; -.
DR eggNOG; NOG329716; -.
DR HOVERGEN; HBG000015; -.
DR InParanoid; Q68EM7; -.
DR OMA; SICHHSH; -.
DR OrthoDB; EOG7MKW5G; -.
DR Reactome; REACT_111102; Signal Transduction.
DR ChiTaRS; ARHGAP17; human.
DR GenomeRNAi; 55114; -.
DR NextBio; 58744; -.
DR PRO; PR:Q68EM7; -.
DR ArrayExpress; Q68EM7; -.
DR Bgee; Q68EM7; -.
DR Genevestigator; Q68EM7; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
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; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Complete proteome; Cytoplasm;
KW GTPase activation; Membrane; Phosphoprotein; Reference proteome;
KW SH3-binding; Tight junction.
FT CHAIN 1 881 Rho GTPase-activating protein 17.
FT /FTId=PRO_0000280462.
FT DOMAIN 14 246 BAR.
FT DOMAIN 252 442 Rho-GAP.
FT MOTIF 753 766 SH3-binding (Potential).
FT COMPBIAS 521 816 Pro-rich.
FT MOD_RES 575 575 Phosphoserine.
FT MOD_RES 679 679 Phosphothreonine.
FT VAR_SEQ 1 467 Missing (in isoform 7).
FT /FTId=VSP_023682.
FT VAR_SEQ 1 273 Missing (in isoform 3).
FT /FTId=VSP_023683.
FT VAR_SEQ 215 226 LLEAQADYHRKA -> ISGRKNQPLGLP (in isoform
FT 4).
FT /FTId=VSP_023684.
FT VAR_SEQ 227 881 Missing (in isoform 4).
FT /FTId=VSP_023685.
FT VAR_SEQ 468 496 TGNDSDSGTLERKRPASMAVMEGDLVKKE -> MCGFNTCG
FT PMGFCLSSLLAWCVDCFFSLC (in isoform 7).
FT /FTId=VSP_023686.
FT VAR_SEQ 497 574 Missing (in isoform 2).
FT /FTId=VSP_023687.
FT VAR_SEQ 839 881 DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTEST
FT AL -> GFQNRIAASFLKCTQTQPAKTCLAASCWI (in
FT isoform 5).
FT /FTId=VSP_023688.
FT VAR_SEQ 840 881 SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTA
FT L -> V (in isoform 6).
FT /FTId=VSP_023689.
FT MUTAGEN 288 288 R->A: Loss of function; leading to
FT defects in tight junction maintenance.
FT CONFLICT 139 139 K -> E (in Ref. 2; BAB55203).
FT CONFLICT 167 167 Q -> R (in Ref. 1; CAC37948).
FT CONFLICT 186 186 K -> R (in Ref. 1; CAC37948).
FT CONFLICT 255 255 E -> A (in Ref. 2; BAB14506).
FT CONFLICT 404 404 G -> A (in Ref. 2; BAB55203).
FT CONFLICT 575 575 S -> C (in Ref. 2; BAC86144).
FT CONFLICT 855 855 M -> V (in Ref. 2; BAB55203).
SQ SEQUENCE 881 AA; 95437 MW; 92029DBFFEAD1001 CRC64;
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT
DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV
DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM
DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH
QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL
WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA
AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK
RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP
EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG
QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS
QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT
QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA
GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS
NSRVSEPHRS IFPEMHSDSA SKDVPGRILL DIDNDTESTA L
//
ID RHG17_HUMAN Reviewed; 881 AA.
AC Q68EM7; A8K6M6; Q6ZUS4; Q7Z2F2; Q8NDG2; Q96KS2; Q96KS3; Q96SS8;
read moreAC Q9BVF6; Q9H8U5; Q9NW54;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 22-JAN-2014, entry version 91.
DE RecName: Full=Rho GTPase-activating protein 17;
DE AltName: Full=Rho-type GTPase-activating protein 17;
DE AltName: Full=RhoGAP interacting with CIP4 homologs protein 1;
DE Short=RICH-1;
GN Name=ARHGAP17; Synonyms=RICH1; ORFNames=MSTP066, MSTP110;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, INTERACTION WITH FNBP1 AND TRIP10, AND
RP MUTAGENESIS OF ARG-288.
RX PubMed=11431473; DOI=10.1074/jbc.M103540200;
RA Richnau N., Aspenstroem P.;
RT "Rich, a rho GTPase-activating protein domain-containing protein
RT involved in signaling by Cdc42 and Rac1.";
RL J. Biol. Chem. 276:35060-35070(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 634-881 (ISOFORM 5).
RC TISSUE=Placenta, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 714-881 (ISOFORM 6).
RC TISSUE=Cervix, and Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-881.
RC TISSUE=Aorta;
RA Liu Y.Q., Zhao B., Xu Y.Y., Wang X.Y., Liu B., Ye J., Song L., Gao Y.,
RA Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH SLC9A3R1.
RX PubMed=11285285; DOI=10.1083/jcb.153.1.191;
RA Reczek D., Bretscher A.;
RT "Identification of EPI64, a TBC/rabGAP domain-containing microvillar
RT protein that binds to the first PDZ domain of EBP50 and E3KARP.";
RL J. Cell Biol. 153:191-206(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN BAR, AND INTERACTION WITH AMOT;
RP MPP5; INADL; PARD3; CAPZA; CAPZB; CD2AP AND SH3KBP1.
RX PubMed=16678097; DOI=10.1016/j.cell.2006.02.045;
RA Wells C.D., Fawcett J.P., Traweger A., Yamanaka Y., Goudreault M.,
RA Elder K., Kulkarni S., Gish G., Virag C., Lim C., Colwill K.,
RA Starostine A., Metalnikov P., Pawson T.;
RT "A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity
RT proteins in epithelial cells.";
RL Cell 125:535-548(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Rho GTPase-activating protein involved in the
CC maintenance of tight junction by regulating the activity of CDC42,
CC thereby playing a central role in apical polarity of epithelial
CC cells. Specifically acts as a GTPase activator for the CDC42
CC GTPase by converting it to an inactive GDP-bound state. The
CC complex formed with AMOT acts by regulating the uptake of polarity
CC proteins at tight junctions, possibly by deciding whether tight
CC junction transmembrane proteins are recycled back to the plasma
CC membrane or sent elsewhere. Participates in the Ca(2+)-dependent
CC regulation of exocytosis, possibly by catalyzing GTPase activity
CC of Rho family proteins and by inducing the reorganization of the
CC cortical actin filaments. Acts as a GTPase activator in vitro for
CC RAC1.
CC -!- SUBUNIT: Component of a complex whose core is composed of
CC ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts
CC with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3),
CC CAPZB, CD2AP and SH3KBP1/CIN85.
CC -!- INTERACTION:
CC Q4VCS5:AMOT; NbExp=2; IntAct=EBI-1642807, EBI-2511319;
CC Q4VCS5-2:AMOT; NbExp=4; IntAct=EBI-1642807, EBI-3891843;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC Cytoplasm. Cell junction, tight junction. Note=Associates with
CC membranes and concentrates at sites of cell-cell contact.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q68EM7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68EM7-2; Sequence=VSP_023687;
CC Name=3;
CC IsoId=Q68EM7-3; Sequence=VSP_023683;
CC Note=No experimental confirmation available;
CC Name=4; Synonyms=RICH1B;
CC IsoId=Q68EM7-4; Sequence=VSP_023684, VSP_023685;
CC Name=5;
CC IsoId=Q68EM7-5; Sequence=VSP_023688;
CC Note=No experimental confirmation available;
CC Name=6;
CC IsoId=Q68EM7-6; Sequence=VSP_023689;
CC Name=7;
CC IsoId=Q68EM7-7; Sequence=VSP_023682, VSP_023686;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher
CC level in heart and placenta.
CC -!- DOMAIN: The BAR domain mediates the interaction with the coiled
CC coil domain of AMOT, leading to its recruitment to tight
CC junctions.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01241.1; Type=Erroneous initiation;
CC Sequence=AAQ13586.1; Type=Erroneous initiation;
CC Sequence=AAQ13632.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AJ306731; CAC37948.1; -; mRNA.
DR EMBL; AJ306732; CAC37949.1; -; mRNA.
DR EMBL; AK001170; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK023281; BAB14506.1; -; mRNA.
DR EMBL; AK027567; BAB55203.1; -; mRNA.
DR EMBL; AK125358; BAC86144.1; -; mRNA.
DR EMBL; AK291691; BAF84380.1; -; mRNA.
DR EMBL; AL833975; CAD38819.1; -; mRNA.
DR EMBL; BC001241; AAH01241.1; ALT_INIT; mRNA.
DR EMBL; BC080195; AAH80195.1; -; mRNA.
DR EMBL; AF163257; AAQ13586.1; ALT_INIT; mRNA.
DR EMBL; AF173885; AAQ13632.1; ALT_INIT; mRNA.
DR PIR; F59433; F59433.
DR RefSeq; NP_001006635.1; NM_001006634.1.
DR RefSeq; NP_060524.4; NM_018054.4.
DR RefSeq; XP_005255471.1; XM_005255414.1.
DR UniGene; Hs.373793; -.
DR ProteinModelPortal; Q68EM7; -.
DR SMR; Q68EM7; 25-232, 246-442.
DR IntAct; Q68EM7; 7.
DR MINT; MINT-195688; -.
DR PhosphoSite; Q68EM7; -.
DR DMDM; 74736331; -.
DR PaxDb; Q68EM7; -.
DR PRIDE; Q68EM7; -.
DR Ensembl; ENST00000289968; ENSP00000289968; ENSG00000140750.
DR Ensembl; ENST00000303665; ENSP00000303130; ENSG00000140750.
DR Ensembl; ENST00000441763; ENSP00000406950; ENSG00000140750.
DR GeneID; 55114; -.
DR KEGG; hsa:55114; -.
DR UCSC; uc002dna.3; human.
DR CTD; 55114; -.
DR GeneCards; GC16M024931; -.
DR HGNC; HGNC:18239; ARHGAP17.
DR HPA; HPA041703; -.
DR MIM; 608293; gene.
DR neXtProt; NX_Q68EM7; -.
DR PharmGKB; PA134908575; -.
DR eggNOG; NOG329716; -.
DR HOVERGEN; HBG000015; -.
DR InParanoid; Q68EM7; -.
DR OMA; SICHHSH; -.
DR OrthoDB; EOG7MKW5G; -.
DR Reactome; REACT_111102; Signal Transduction.
DR ChiTaRS; ARHGAP17; human.
DR GenomeRNAi; 55114; -.
DR NextBio; 58744; -.
DR PRO; PR:Q68EM7; -.
DR ArrayExpress; Q68EM7; -.
DR Bgee; Q68EM7; -.
DR Genevestigator; Q68EM7; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
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; SSF48350; SSF48350; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Complete proteome; Cytoplasm;
KW GTPase activation; Membrane; Phosphoprotein; Reference proteome;
KW SH3-binding; Tight junction.
FT CHAIN 1 881 Rho GTPase-activating protein 17.
FT /FTId=PRO_0000280462.
FT DOMAIN 14 246 BAR.
FT DOMAIN 252 442 Rho-GAP.
FT MOTIF 753 766 SH3-binding (Potential).
FT COMPBIAS 521 816 Pro-rich.
FT MOD_RES 575 575 Phosphoserine.
FT MOD_RES 679 679 Phosphothreonine.
FT VAR_SEQ 1 467 Missing (in isoform 7).
FT /FTId=VSP_023682.
FT VAR_SEQ 1 273 Missing (in isoform 3).
FT /FTId=VSP_023683.
FT VAR_SEQ 215 226 LLEAQADYHRKA -> ISGRKNQPLGLP (in isoform
FT 4).
FT /FTId=VSP_023684.
FT VAR_SEQ 227 881 Missing (in isoform 4).
FT /FTId=VSP_023685.
FT VAR_SEQ 468 496 TGNDSDSGTLERKRPASMAVMEGDLVKKE -> MCGFNTCG
FT PMGFCLSSLLAWCVDCFFSLC (in isoform 7).
FT /FTId=VSP_023686.
FT VAR_SEQ 497 574 Missing (in isoform 2).
FT /FTId=VSP_023687.
FT VAR_SEQ 839 881 DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTEST
FT AL -> GFQNRIAASFLKCTQTQPAKTCLAASCWI (in
FT isoform 5).
FT /FTId=VSP_023688.
FT VAR_SEQ 840 881 SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTA
FT L -> V (in isoform 6).
FT /FTId=VSP_023689.
FT MUTAGEN 288 288 R->A: Loss of function; leading to
FT defects in tight junction maintenance.
FT CONFLICT 139 139 K -> E (in Ref. 2; BAB55203).
FT CONFLICT 167 167 Q -> R (in Ref. 1; CAC37948).
FT CONFLICT 186 186 K -> R (in Ref. 1; CAC37948).
FT CONFLICT 255 255 E -> A (in Ref. 2; BAB14506).
FT CONFLICT 404 404 G -> A (in Ref. 2; BAB55203).
FT CONFLICT 575 575 S -> C (in Ref. 2; BAC86144).
FT CONFLICT 855 855 M -> V (in Ref. 2; BAB55203).
SQ SEQUENCE 881 AA; 95437 MW; 92029DBFFEAD1001 CRC64;
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SICHHSHKRL VACFQGQHGT
DAERRHKKLP LTALAQNMQE ASTQLEDSLL GKMLETCGDA ENQLALELSQ HEVFVEKEIV
DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM
DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKTLPEMRAH
QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFNL YEEWTQVASV QDQDKKLQDL
WRTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA RNEGTLAEMA
AATSVHVVAV IEPIIQHADW FFPEEVEFNV SEAFVPLTTP SSNHSFHTGN DSDSGTLERK
RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIS PAFQPPLPPT DGSTVVPAGP
EPPPQSSRAE SSSGGGTVPS SAGILEQGPS PGDGSPPKPK DPVSAAVPAP GRNNSQIASG
QNQPQAAAGS HQLSMGQPHN AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSSGTS
QHPPSLSPKP PTRSPSPPTQ HTGQPPGQPS APSQLSAPRR YSSSLSPIQA PNHPPPQPPT
QATPLMHTKP NSQGPPNPMA LPSEHGLEQP SHTPPQTPTP PSTPPLGKQN PSLPAPQTLA
GGNPETAQPH AGTLPRPRPV PKPRNRPSVP PPPQPPGVHS AGDSSLTNTA PTASKIVTDS
NSRVSEPHRS IFPEMHSDSA SKDVPGRILL DIDNDTESTA L
//
MIM
608293
*RECORD*
*FIELD* NO
608293
*FIELD* TI
*608293 RHO GTPase-ACTIVATING PROTEIN 17; ARHGAP17
;;RHOGAP INTERACTING WITH CIP4 HOMOLOGS 1; RICH1;;
read moreNADRIN, RAT, HOMOLOG OF
*FIELD* TX
CLONING
Using the SH3 domain of CIP4 (TRIP10; 604504) as bait in a yeast
2-hybrid screen of an Epstein-Barr virus-transformed B-cell cDNA
library, followed by screening a brain cDNA library, Richnau and
Aspenstrom (2001) cloned a splice variant of RICH1, which they
designated RICH1B. By PCR, they obtained full-length RICH1 cDNAs from
B-cell and HeLa cell cDNA libraries. The deduced full-length RICH1
protein contains 803 amino acids, and the RICH1B protein contains 226
amino acids. Both isoforms have an N-terminal domain that shares
homology with endophilins (see 604465), and RICH1 also has a central
RHOGAP domain and a C-terminal domain containing 4 proline-rich
sequences. Northern blot analysis using a probe that did not
differentiate between the variants detected a 4.0-kb transcript in all
tissues examined, with highest expression in heart and placenta. A probe
specific for RICH1 detected higher expression in skeletal muscle and
little expression in brain.
GENE FUNCTION
By coimmunoprecipitation experiments and colocalization assays, Richnau
and Aspenstrom (2001) confirmed that RICH1 and CIP4 interact in vivo.
The RHOGAP domain of RICH1 catalyzed GTP hydrolysis on CDC42 and RAC1,
but not on RHOA. Ectopic expression of the RHOGAP domain of RICH1 or the
full-length RICH1 protein interfered with membrane ruffling induced by
homodimeric PDGF (190040), but did not interfere with serum-induced
stress fiber formation.
Using functional and proteomic screens to identify regulators of Cdc42,
Wells et al. (2006) identified a network of proteins that centered on
Rich1 and organized apical polarity in canine kidney epithelial cells.
Rich1 bound the coiled-coil domain of Amot (300410) and was thereby
targeted to a complex at tight junctions containing the PDZ
domain-containing proteins Pals1 (MPP5; 606958), Patj (INADL; 603199),
and Par3 (PARD3; 606745). Regulation of Cdc42 by Rich1 was required for
maintenance of tight junctions. The coiled-coil domain of Amot was
required for its localization to apical membranes and for Amot to
relocalize Pals1 and Par3 to internal puncta. Wells et al. (2006)
proposed that RICH1 and AMOT maintain tight junction integrity by
coordinated regulation of CDC42 and by linking specific components of
the tight junction to intracellular protein trafficking.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RICH1
gene to chromosome 16 (TMAP STS-W92992).
*FIELD* RF
1. Richnau, N.; Aspenstrom, P.: RICH, a Rho GTPase-activating protein
domain-containing protein involved in signaling by Cdc42 and Rac1. J.
Biol. Chem. 276: 35060-35070, 2001.
2. Wells, C. D.; Fawcett, J. P.; Traweger, A.; Yamanaka, Y.; Goudreault,
M.; Elder, K.; Kulkarni, S.; Gish, G.; Virag, C.; Lim, C.; Colwill,
K.; Starostine, A.; Metalnikov, P.; Pawson, T.: A Rich1/Amot complex
regulates the Cdc42 GTPase and apical-polarity proteins in epithelial
cells. Cell 125: 535-548, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 8/30/2007
*FIELD* CD
Patricia A. Hartz: 11/26/2003
*FIELD* ED
mgross: 10/04/2007
terry: 8/30/2007
carol: 10/16/2006
mgross: 11/26/2003
*RECORD*
*FIELD* NO
608293
*FIELD* TI
*608293 RHO GTPase-ACTIVATING PROTEIN 17; ARHGAP17
;;RHOGAP INTERACTING WITH CIP4 HOMOLOGS 1; RICH1;;
read moreNADRIN, RAT, HOMOLOG OF
*FIELD* TX
CLONING
Using the SH3 domain of CIP4 (TRIP10; 604504) as bait in a yeast
2-hybrid screen of an Epstein-Barr virus-transformed B-cell cDNA
library, followed by screening a brain cDNA library, Richnau and
Aspenstrom (2001) cloned a splice variant of RICH1, which they
designated RICH1B. By PCR, they obtained full-length RICH1 cDNAs from
B-cell and HeLa cell cDNA libraries. The deduced full-length RICH1
protein contains 803 amino acids, and the RICH1B protein contains 226
amino acids. Both isoforms have an N-terminal domain that shares
homology with endophilins (see 604465), and RICH1 also has a central
RHOGAP domain and a C-terminal domain containing 4 proline-rich
sequences. Northern blot analysis using a probe that did not
differentiate between the variants detected a 4.0-kb transcript in all
tissues examined, with highest expression in heart and placenta. A probe
specific for RICH1 detected higher expression in skeletal muscle and
little expression in brain.
GENE FUNCTION
By coimmunoprecipitation experiments and colocalization assays, Richnau
and Aspenstrom (2001) confirmed that RICH1 and CIP4 interact in vivo.
The RHOGAP domain of RICH1 catalyzed GTP hydrolysis on CDC42 and RAC1,
but not on RHOA. Ectopic expression of the RHOGAP domain of RICH1 or the
full-length RICH1 protein interfered with membrane ruffling induced by
homodimeric PDGF (190040), but did not interfere with serum-induced
stress fiber formation.
Using functional and proteomic screens to identify regulators of Cdc42,
Wells et al. (2006) identified a network of proteins that centered on
Rich1 and organized apical polarity in canine kidney epithelial cells.
Rich1 bound the coiled-coil domain of Amot (300410) and was thereby
targeted to a complex at tight junctions containing the PDZ
domain-containing proteins Pals1 (MPP5; 606958), Patj (INADL; 603199),
and Par3 (PARD3; 606745). Regulation of Cdc42 by Rich1 was required for
maintenance of tight junctions. The coiled-coil domain of Amot was
required for its localization to apical membranes and for Amot to
relocalize Pals1 and Par3 to internal puncta. Wells et al. (2006)
proposed that RICH1 and AMOT maintain tight junction integrity by
coordinated regulation of CDC42 and by linking specific components of
the tight junction to intracellular protein trafficking.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the RICH1
gene to chromosome 16 (TMAP STS-W92992).
*FIELD* RF
1. Richnau, N.; Aspenstrom, P.: RICH, a Rho GTPase-activating protein
domain-containing protein involved in signaling by Cdc42 and Rac1. J.
Biol. Chem. 276: 35060-35070, 2001.
2. Wells, C. D.; Fawcett, J. P.; Traweger, A.; Yamanaka, Y.; Goudreault,
M.; Elder, K.; Kulkarni, S.; Gish, G.; Virag, C.; Lim, C.; Colwill,
K.; Starostine, A.; Metalnikov, P.; Pawson, T.: A Rich1/Amot complex
regulates the Cdc42 GTPase and apical-polarity proteins in epithelial
cells. Cell 125: 535-548, 2006.
*FIELD* CN
Patricia A. Hartz - updated: 8/30/2007
*FIELD* CD
Patricia A. Hartz: 11/26/2003
*FIELD* ED
mgross: 10/04/2007
terry: 8/30/2007
carol: 10/16/2006
mgross: 11/26/2003