RHG17_RAT
ID RHG17_RAT Reviewed; 858 AA.
AC Q99N37; Q8R506; Q99N38; Q9EQV7;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 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 [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; 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 [MRNA] (ISOFORMS 1; 3 AND 4), AND TISSUE SPECIFICITY.
RX PubMed=12358749; DOI=10.1046/j.1471-4159.2002.01021.x;
RA Furuta B., Harada A., Kobayashi Y., Takeuchi K., Kobayashi T., Umeda M.;
RT "Identification and functional characterization of nadrin variants, a novel
RT family of GTPase activating protein for rho GTPases.";
RL J. Neurochem. 82:1018-1028(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 THR-742; THR-746 AND THR-748, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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: 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 (By similarity).
CC Participates in the Ca(2+)-dependent regulation of exocytosis, possibly
CC by catalyzing GTPase activity of Rho family proteins and by inducing
CC the reorganization of the cortical actin filaments. Acts as a GTPase
CC activator in vitro for RAC1. {ECO:0000250,
CC ECO:0000269|PubMed:10967100}.
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:0000269|PubMed:10967100};
CC Peripheral membrane protein {ECO:0000269|PubMed:10967100}. Cytoplasm
CC {ECO:0000269|PubMed:10967100}. Cell junction, tight junction
CC {ECO:0000250}. Note=Associates with membranes and concentrates at sites
CC of cell-cell contact. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Nadrin-126, Nadrin-E2;
CC IsoId=Q99N37-1; Sequence=Displayed;
CC Name=2; Synonyms=Nadrin-104;
CC IsoId=Q99N37-2; Sequence=VSP_023693;
CC Name=3; Synonyms=Nadrin-102;
CC IsoId=Q99N37-3; Sequence=VSP_023693, VSP_023694;
CC Name=4; Synonyms=Nadrin-116, Nadrin-E1;
CC IsoId=Q99N37-4; Sequence=VSP_023694;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain; neuron-specific (at
CC protein level). Isoform 2, isoform 3 and isoform 4 are predominantly
CC expressed in neuronal tissues and correlate well with the
CC differentiation of neurons, while isoform 1 is strongly expressed in
CC embryonic brain. {ECO:0000269|PubMed:10967100,
CC ECO:0000269|PubMed:12358749}.
CC -!- DEVELOPMENTAL STAGE: Becomes detectable at the second postnatal week in
CC the cerebral cortex and hippocampus and at the third postnatal week in
CC the cerebellum and olfactory bulb. The expression level is maximal
CC during the third and fourth postnatal weeks and remains high during
CC adulthood. Its expression is closely correlated with neuronal
CC differentiation (at protein level). {ECO:0000269|PubMed:10967100}.
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; AB042827; BAB12426.1; -; mRNA.
DR EMBL; AB060556; BAB43864.1; -; mRNA.
DR EMBL; AB060557; BAB43865.1; -; mRNA.
DR EMBL; AB080637; BAB85655.1; -; mRNA.
DR EMBL; BC085736; AAH85736.1; -; mRNA.
DR RefSeq; NP_001257621.1; NM_001270692.1. [Q99N37-1]
DR RefSeq; NP_001257622.1; NM_001270693.1. [Q99N37-4]
DR RefSeq; NP_001257623.1; NM_001270694.1. [Q99N37-3]
DR RefSeq; NP_071580.1; NM_022244.2. [Q99N37-2]
DR AlphaFoldDB; Q99N37; -.
DR SMR; Q99N37; -.
DR CORUM; Q99N37; -.
DR STRING; 10116.ENSRNOP00000038504; -.
DR iPTMnet; Q99N37; -.
DR PhosphoSitePlus; Q99N37; -.
DR jPOST; Q99N37; -.
DR PaxDb; Q99N37; -.
DR PRIDE; Q99N37; -.
DR Ensembl; ENSRNOT00000019304; ENSRNOP00000019305; ENSRNOG00000013836. [Q99N37-4]
DR Ensembl; ENSRNOT00000031770; ENSRNOP00000038504; ENSRNOG00000013836. [Q99N37-1]
DR GeneID; 63994; -.
DR KEGG; rno:63994; -.
DR UCSC; RGD:628767; rat. [Q99N37-1]
DR CTD; 55114; -.
DR RGD; 628767; Arhgap17.
DR eggNOG; KOG4270; Eukaryota.
DR GeneTree; ENSGT00940000156201; -.
DR InParanoid; Q99N37; -.
DR OrthoDB; 821331at2759; -.
DR PhylomeDB; Q99N37; -.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013405; RHOD GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR PRO; PR:Q99N37; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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; IDA:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA: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..858
FT /note="Rho GTPase-activating protein 17"
FT /id="PRO_0000280464"
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 516..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 742..755
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 544..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..796
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EM7"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q68EM7"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 742
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 746
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 748
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT MOD_RES 752
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3UIA2"
FT VAR_SEQ 497..574
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10967100,
FT ECO:0000303|PubMed:12358749"
FT /id="VSP_023693"
FT VAR_SEQ 817..858
FT /note="TNSRVSESLRNIFPEIHSDLASKEVPGHILLDIDNDTESTAL -> ALPGAL
FT TGGEGFQN (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12358749"
FT /id="VSP_023694"
SQ SEQUENCE 858 AA; 93754 MW; 4B3850A69090D88B CRC64;
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SMCHHSHKRL IACFQGQHGT
DAERRHKKLP LTALAQNMQE ASAQLEESLL GKMLETCGDA ENQLAFELSQ 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 GGTLNRKHIS PAFQPPLPPT DGNALAPAGP
ELPSQSSRAD SNSVGGPVPS SSGILEQGLS PGDSSPPKPK DSVSAAAPVA GRNSNQITTV
PNQAQTGGNS HQLSVGTAHS AAGPSPHTLR RAVKKPAPAP PKPGNPPPGH PGGQSSPGTG
TSPKPSTRSP SPPQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQTPGMRRCS SSLPPIQAPN
HPPPQPPTQP RLGEQGPEPG PTPPQTPTPP STPPPAKQNS SQSETTQLHG TLPRPRPVPK
PRNRPSVPPP PNPPGTHMGD GGLTPSVPTA SRIVTDTNSR VSESLRNIFP EIHSDLASKE
VPGHILLDID NDTESTAL
