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Protein

Rho GTPase-activating protein 17

Gene

Arhgap17

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Rho GTPase-activating protein involved in the maintenance of tight junction by regulating the activity of CDC42, thereby playing a central role in apical polarity of epithelial cells. Specifically acts as a GTPase activator for the CDC42 GTPase by converting it to an inactive GDP-bound state. The complex formed with AMOT acts by regulating the uptake of polarity proteins at tight junctions, possibly by deciding whether tight junction transmembrane proteins are recycled back to the plasma membrane or sent elsewhere. Participates in the Ca2+-dependent regulation of exocytosis, possibly by catalyzing GTPase activity of Rho family proteins and by inducing the reorganization of the cortical actin filaments. Acts as a GTPase activator in vitro for RAC1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rho GTPase-activating protein 17
Alternative name(s):
Neuron-associated developmentally-regulated protein
Short name:
Nadrin
Rho-type GTPase-activating protein 17
Gene namesi
Name:Arhgap17
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1917747. Arhgap17.

Subcellular locationi

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB-SubCell
  • cytoplasm Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 846846Rho GTPase-activating protein 17PRO_0000280463Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei484 – 4841PhosphoserineCombined sources
Modified residuei575 – 5751PhosphoserineCombined sources
Modified residuei698 – 6981PhosphoserineCombined sources
Modified residuei700 – 7001PhosphoserineCombined sources
Modified residuei730 – 7301PhosphothreonineCombined sources
Modified residuei734 – 7341PhosphothreonineCombined sources
Modified residuei736 – 7361PhosphothreonineCombined sources
Modified residuei739 – 7391PhosphoserineCombined sources
Modified residuei740 – 7401PhosphothreonineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3UIA2.
MaxQBiQ3UIA2.
PaxDbiQ3UIA2.
PeptideAtlasiQ3UIA2.
PRIDEiQ3UIA2.

PTM databases

iPTMnetiQ3UIA2.
PhosphoSiteiQ3UIA2.

Expressioni

Gene expression databases

BgeeiQ3UIA2.
CleanExiMM_ARHGAP17.
ExpressionAtlasiQ3UIA2. baseline and differential.
GenevisibleiQ3UIA2. MM.

Interactioni

Subunit structurei

Component of a complex whose core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85 (By similarity).By similarity

Protein-protein interaction databases

BioGridi214096. 1 interaction.
IntActiQ3UIA2. 1 interaction.
MINTiMINT-5047348.
STRINGi10090.ENSMUSP00000102050.

Structurei

3D structure databases

ProteinModelPortaliQ3UIA2.
SMRiQ3UIA2. Positions 4-232, 246-442.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 246233BARPROSITE-ProRule annotationAdd
BLAST
Domaini252 – 442191Rho-GAPPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi730 – 74314SH3-bindingSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi636 – 782147Pro-richAdd
BLAST
Compositional biasi674 – 69017Poly-GlnAdd
BLAST

Domaini

The BAR domain mediates the interaction with the coiled coil domain of AMOT, leading to its recruitment to tight junctions.By similarity

Sequence similaritiesi

Contains 1 BAR domain.PROSITE-ProRule annotation
Contains 1 Rho-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

SH3-binding

Phylogenomic databases

eggNOGiKOG4270. Eukaryota.
ENOG410XRR2. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000179193.
HOVERGENiHBG000015.
InParanoidiQ3UIA2.
OMAiKTLPEMR.
OrthoDBiEOG7MKW5G.
PhylomeDBiQ3UIA2.
TreeFamiTF350627.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00721. BAR. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q3UIA2-1) [UniParc]FASTAAdd to basket

Also known as: Nadrin-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SMCHHSHKRL
60 70 80 90 100
IACFQGQHGT DAERRHKKLP LTALAQNMQE ASAQLEESLL GKMLETCGDA
110 120 130 140 150
ENQLALELSQ HEVFVEKEIM DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS
160 170 180 190 200
VRARWNQAHK SSGTNFQGLP SKIDTLKEEM DEAGNKVEQC KDQLAADMYN
210 220 230 240 250
FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKALPEMRAH QDKWAEKPAF
260 270 280 290 300
GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
310 320 330 340 350
AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFSL YEEWTQVASV
360 370 380 390 400
QDQDKKLQYL WTTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA
410 420 430 440 450
IVLGPNLLWA KQEGTLAEIA AATSVHVVAV IEPIIQHADW FFPGEVEFNV
460 470 480 490 500
SEAFVPLATP NSNHSSHTGN DSDSGTLERK RPASMAVMEG DLVKKESFGV
510 520 530 540 550
KLMDFQAHRR GGTLNRKHIA PAFQPPLPPT DGNALAPAGP EPPSQSSRAD
560 570 580 590 600
SSSGGGPVFS STGILEQGLS PGDSSPPKPK DSVSAAVPAA GRNSNQMTTV
610 620 630 640 650
PNQAQTGGNS HQLSVSTPHS AAGPSPHTLR RAVKKPAPAP PKPGNLPPGH
660 670 680 690 700
PGGQSSPGTG TSPKPSARSP SPPQQQQQQQ QQQQQQQQQQ TPGMRRCSSS
710 720 730 740 750
LPPIQAPSHP PPQPPTQPRL GEQGPEPGPT PPQTPTPPST PPLAKQNPSQ
760 770 780 790 800
SETTQLHGTL PRPRPVPKPR NRPSVPPPPH PPGTHTVDGG LTSSVPTASR
810 820 830 840
IVTDTNSRVS ESLRSIFPEI HSDLASKEVP GHILLDIDND TESTAL
Length:846
Mass (Da):92,202
Last modified:October 11, 2005 - v1
Checksum:i3D12B030B41E6987
GO
Isoform 2 (identifier: Q3UIA2-2) [UniParc]FASTAAdd to basket

Also known as: Nadrin-2

The sequence of this isoform differs from the canonical sequence as follows:
     497-574: Missing.

Show »
Length:768
Mass (Da):84,309
Checksum:iC1CA4CD19FBAB0EF
GO
Isoform 3 (identifier: Q3UIA2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     497-574: Missing.
     805-846: TNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTAL → ALPGALTGGEGFQN

Show »
Length:740
Mass (Da):81,033
Checksum:iA644889614AE02E5
GO
Isoform 4 (identifier: Q3UIA2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     497-574: Missing.
     805-846: TNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTAL → V

Show »
Length:727
Mass (Da):79,819
Checksum:iABDA4E1853E6664D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti207 – 2071E → K in BAB43862 (PubMed:10967100).Curated
Sequence conflicti207 – 2071E → K in BAB43863 (PubMed:10967100).Curated
Sequence conflicti250 – 2501F → I in BAE29214 (PubMed:16141072).Curated
Sequence conflicti593 – 5931N → D in BAB43862 (PubMed:10967100).Curated
Sequence conflicti593 – 5931N → D in BAB43863 (PubMed:10967100).Curated
Sequence conflicti674 – 6763Missing in AAH03259 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei497 – 57478Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_023690Add
BLAST
Alternative sequencei805 – 84642TNSRV…ESTAL → ALPGALTGGEGFQN in isoform 3. 1 PublicationVSP_023691Add
BLAST
Alternative sequencei805 – 84642TNSRV…ESTAL → V in isoform 4. 2 PublicationsVSP_023692Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060553 mRNA. Translation: BAB43862.1.
AB060554 mRNA. Translation: BAB43863.1.
AK036468 mRNA. Translation: BAC29443.1.
AK036617 mRNA. Translation: BAC29508.1.
AK147010 mRNA. Translation: BAE27604.1.
AK149986 mRNA. Translation: BAE29214.1.
AK152266 mRNA. Translation: BAE31084.1.
BC003259 mRNA. Translation: AAH03259.1.
CCDSiCCDS52388.1. [Q3UIA2-4]
CCDS52389.1. [Q3UIA2-1]
RefSeqiNP_001116112.1. NM_001122640.1.
NP_001116113.1. NM_001122641.1. [Q3UIA2-2]
NP_001116114.1. NM_001122642.1. [Q3UIA2-3]
NP_001116115.1. NM_001122643.1. [Q3UIA2-4]
NP_001303642.1. NM_001316713.1.
NP_653112.2. NM_144529.2. [Q3UIA2-1]
UniGeneiMm.403318.

Genome annotation databases

EnsembliENSMUST00000098060; ENSMUSP00000095668; ENSMUSG00000030766. [Q3UIA2-2]
ENSMUST00000106442; ENSMUSP00000102050; ENSMUSG00000030766. [Q3UIA2-1]
ENSMUST00000205262; ENSMUSP00000146035; ENSMUSG00000030766. [Q3UIA2-4]
ENSMUST00000207010; ENSMUSP00000145628; ENSMUSG00000030766. [Q3UIA2-3]
GeneIDi70497.
KEGGimmu:70497.
UCSCiuc009jpi.2. mouse. [Q3UIA2-1]
uc009jpk.2. mouse. [Q3UIA2-4]
uc009jpm.2. mouse. [Q3UIA2-3]
uc009jpn.2. mouse. [Q3UIA2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB060553 mRNA. Translation: BAB43862.1.
AB060554 mRNA. Translation: BAB43863.1.
AK036468 mRNA. Translation: BAC29443.1.
AK036617 mRNA. Translation: BAC29508.1.
AK147010 mRNA. Translation: BAE27604.1.
AK149986 mRNA. Translation: BAE29214.1.
AK152266 mRNA. Translation: BAE31084.1.
BC003259 mRNA. Translation: AAH03259.1.
CCDSiCCDS52388.1. [Q3UIA2-4]
CCDS52389.1. [Q3UIA2-1]
RefSeqiNP_001116112.1. NM_001122640.1.
NP_001116113.1. NM_001122641.1. [Q3UIA2-2]
NP_001116114.1. NM_001122642.1. [Q3UIA2-3]
NP_001116115.1. NM_001122643.1. [Q3UIA2-4]
NP_001303642.1. NM_001316713.1.
NP_653112.2. NM_144529.2. [Q3UIA2-1]
UniGeneiMm.403318.

3D structure databases

ProteinModelPortaliQ3UIA2.
SMRiQ3UIA2. Positions 4-232, 246-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214096. 1 interaction.
IntActiQ3UIA2. 1 interaction.
MINTiMINT-5047348.
STRINGi10090.ENSMUSP00000102050.

PTM databases

iPTMnetiQ3UIA2.
PhosphoSiteiQ3UIA2.

Proteomic databases

EPDiQ3UIA2.
MaxQBiQ3UIA2.
PaxDbiQ3UIA2.
PeptideAtlasiQ3UIA2.
PRIDEiQ3UIA2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000098060; ENSMUSP00000095668; ENSMUSG00000030766. [Q3UIA2-2]
ENSMUST00000106442; ENSMUSP00000102050; ENSMUSG00000030766. [Q3UIA2-1]
ENSMUST00000205262; ENSMUSP00000146035; ENSMUSG00000030766. [Q3UIA2-4]
ENSMUST00000207010; ENSMUSP00000145628; ENSMUSG00000030766. [Q3UIA2-3]
GeneIDi70497.
KEGGimmu:70497.
UCSCiuc009jpi.2. mouse. [Q3UIA2-1]
uc009jpk.2. mouse. [Q3UIA2-4]
uc009jpm.2. mouse. [Q3UIA2-3]
uc009jpn.2. mouse. [Q3UIA2-2]

Organism-specific databases

CTDi55114.
MGIiMGI:1917747. Arhgap17.

Phylogenomic databases

eggNOGiKOG4270. Eukaryota.
ENOG410XRR2. LUCA.
GeneTreeiENSGT00760000118863.
HOGENOMiHOG000179193.
HOVERGENiHBG000015.
InParanoidiQ3UIA2.
OMAiKTLPEMR.
OrthoDBiEOG7MKW5G.
PhylomeDBiQ3UIA2.
TreeFamiTF350627.

Enzyme and pathway databases

ReactomeiR-MMU-194840. Rho GTPase cycle.

Miscellaneous databases

ChiTaRSiArhgap17. mouse.
PROiQ3UIA2.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UIA2.
CleanExiMM_ARHGAP17.
ExpressionAtlasiQ3UIA2. baseline and differential.
GenevisibleiQ3UIA2. MM.

Family and domain databases

Gene3Di1.10.555.10. 1 hit.
1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR004148. BAR_dom.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
[Graphical view]
PfamiPF03114. BAR. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTiSM00721. BAR. 1 hit.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
PROSITEiPS51021. BAR. 1 hit.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nadrin, a novel neuron-specific GTPase-activating protein involved in regulated exocytosis."
    Harada A., Furuta B., Takeuchi K., Itakura M., Takahashi M., Umeda M.
    J. Biol. Chem. 275:36885-36891(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
    Strain: C57BL/6J.
    Tissue: Bone, Bone marrow and Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Strain: Czech II.
    Tissue: Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-575; SER-698; SER-700; THR-730; THR-734; THR-736; SER-739 AND THR-740, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRHG17_MOUSE
AccessioniPrimary (citable) accession number: Q3UIA2
Secondary accession number(s): Q3UDP7
, Q8BGD1, Q99LH3, Q99N39, Q99N40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2005
Last modified: July 6, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.