ID RHG17_HUMAN Reviewed; 881 AA. AC Q68EM7; A8K6M6; Q6ZUS4; Q7Z2F2; Q8NDG2; Q96KS2; Q96KS3; Q96SS8; Q9BVF6; AC Q9H8U5; Q9NW54; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 24-JAN-2024, entry version 164. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 involved RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA 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 SEQUENCE RP [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 project: RT 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 NHERF1. 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 PALS1; PATJ; 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 IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT 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., Buerckstuemmer T., RA 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 IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT 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., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND SER-575, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND THR-682, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). 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. {ECO:0000269|PubMed:11431473, CC ECO:0000269|PubMed:16678097}. CC -!- SUBUNIT: Component of a complex whose core is composed of ARHGAP17, CC AMOT, PALS1, PATJ and PARD3/PAR3. Interacts with NHERF1, FNBP1, TRIP10, CC CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CD2AP and SH3KBP1/CIN85. CC {ECO:0000269|PubMed:11285285, ECO:0000269|PubMed:11431473, CC ECO:0000269|PubMed:16678097}. CC -!- INTERACTION: CC Q68EM7; Q4VCS5: AMOT; NbExp=2; IntAct=EBI-1642807, EBI-2511319; CC Q68EM7; Q4VCS5-2: AMOT; NbExp=4; IntAct=EBI-1642807, EBI-3891843; CC Q68EM7; Q15642: TRIP10; NbExp=3; IntAct=EBI-1642807, EBI-739936; CC Q68EM7; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-1642807, EBI-6550597; CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cytoplasm. CC Cell junction, tight junction. Note=Associates with membranes and CC 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 Name=4; Synonyms=RICH1B; CC IsoId=Q68EM7-4; Sequence=VSP_023684, VSP_023685; CC Name=5; CC IsoId=Q68EM7-5; Sequence=VSP_023688; CC Name=6; CC IsoId=Q68EM7-6; Sequence=VSP_023689; CC Name=7; CC IsoId=Q68EM7-7; Sequence=VSP_023682, VSP_023686; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed at higher level CC in heart and placenta. {ECO:0000269|PubMed:11431473}. 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:0000269|PubMed:16678097}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH01241.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAQ13586.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAQ13632.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CCDS; CCDS32408.1; -. [Q68EM7-2] DR CCDS; CCDS32409.1; -. [Q68EM7-1] DR PIR; F59433; F59433. DR RefSeq; NP_001006635.1; NM_001006634.2. [Q68EM7-1] DR RefSeq; NP_060524.4; NM_018054.5. [Q68EM7-2] DR AlphaFoldDB; Q68EM7; -. DR SMR; Q68EM7; -. DR BioGRID; 120424; 98. DR CORUM; Q68EM7; -. DR IntAct; Q68EM7; 24. DR MINT; Q68EM7; -. DR STRING; 9606.ENSP00000289968; -. DR GlyGen; Q68EM7; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q68EM7; -. DR MetOSite; Q68EM7; -. DR PhosphoSitePlus; Q68EM7; -. DR SwissPalm; Q68EM7; -. DR BioMuta; ARHGAP17; -. DR DMDM; 74736331; -. DR EPD; Q68EM7; -. DR jPOST; Q68EM7; -. DR MassIVE; Q68EM7; -. DR MaxQB; Q68EM7; -. DR PaxDb; 9606-ENSP00000289968; -. DR PeptideAtlas; Q68EM7; -. DR ProteomicsDB; 66129; -. [Q68EM7-1] DR ProteomicsDB; 66130; -. [Q68EM7-2] DR ProteomicsDB; 66131; -. [Q68EM7-3] DR ProteomicsDB; 66132; -. [Q68EM7-4] DR ProteomicsDB; 66133; -. [Q68EM7-5] DR ProteomicsDB; 66134; -. [Q68EM7-6] DR ProteomicsDB; 66135; -. [Q68EM7-7] DR Pumba; Q68EM7; -. DR Antibodypedia; 52174; 196 antibodies from 27 providers. DR DNASU; 55114; -. DR Ensembl; ENST00000289968.11; ENSP00000289968.6; ENSG00000140750.17. [Q68EM7-1] DR Ensembl; ENST00000303665.9; ENSP00000303130.5; ENSG00000140750.17. [Q68EM7-2] DR Ensembl; ENST00000673196.1; ENSP00000500849.1; ENSG00000288353.1. [Q68EM7-2] DR Ensembl; ENST00000673560.1; ENSP00000500372.1; ENSG00000288353.1. [Q68EM7-1] DR GeneID; 55114; -. DR KEGG; hsa:55114; -. DR MANE-Select; ENST00000289968.11; ENSP00000289968.6; NM_001006634.3; NP_001006635.1. DR UCSC; uc002dnb.5; human. [Q68EM7-1] DR AGR; HGNC:18239; -. DR CTD; 55114; -. DR DisGeNET; 55114; -. DR GeneCards; ARHGAP17; -. DR HGNC; HGNC:18239; ARHGAP17. DR HPA; ENSG00000140750; Low tissue specificity. DR MIM; 608293; gene. DR neXtProt; NX_Q68EM7; -. DR OpenTargets; ENSG00000140750; -. DR PharmGKB; PA134908575; -. DR VEuPathDB; HostDB:ENSG00000140750; -. DR eggNOG; KOG4270; Eukaryota. DR GeneTree; ENSGT00940000156201; -. DR HOGENOM; CLU_013806_0_0_1; -. DR InParanoid; Q68EM7; -. DR OMA; HAVAXVQ; -. DR OrthoDB; 7959at2759; -. DR PhylomeDB; Q68EM7; -. DR TreeFam; TF350627; -. DR PathwayCommons; Q68EM7; -. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013404; RAC2 GTPase cycle. DR Reactome; R-HSA-9013405; RHOD GTPase cycle. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR Reactome; R-HSA-9013423; RAC3 GTPase cycle. DR SignaLink; Q68EM7; -. DR SIGNOR; Q68EM7; -. DR BioGRID-ORCS; 55114; 13 hits in 1157 CRISPR screens. DR ChiTaRS; ARHGAP17; human. DR GenomeRNAi; 55114; -. DR Pharos; Q68EM7; Tbio. DR PRO; PR:Q68EM7; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q68EM7; Protein. DR Bgee; ENSG00000140750; Expressed in spleen and 96 other cell types or tissues. DR ExpressionAtlas; Q68EM7; baseline and differential. DR Genevisible; Q68EM7; HS. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. 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; IEA:Ensembl. DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl. 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 CDD; cd07618; BAR_Rich1; 1. DR CDD; cd04386; RhoGAP_nadrin; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR004148; BAR_dom. DR InterPro; IPR047165; RHG17/44/SH3BP1-like. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR PANTHER; PTHR14130; 3BP-1 RELATED RHOGAP; 1. DR PANTHER; PTHR14130:SF3; RHO GTPASE-ACTIVATING PROTEIN 17; 1. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00324; RhoGAP; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 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..881 FT /note="Rho GTPase-activating protein 17" FT /id="PRO_0000280462" 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 511..881 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 753..766 FT /note="SH3-binding" FT /evidence="ECO:0000255" FT COMPBIAS 522..544 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 545..564 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 589..621 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 664..685 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 686..708 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 709..723 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 753..771 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 794..818 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 820..847 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 575 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 679 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 682 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 702 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT MOD_RES 704 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT MOD_RES 753 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT MOD_RES 757 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT MOD_RES 759 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT MOD_RES 762 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT MOD_RES 763 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3UIA2" FT VAR_SEQ 1..467 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_023682" FT VAR_SEQ 1..273 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023683" FT VAR_SEQ 215..226 FT /note="LLEAQADYHRKA -> ISGRKNQPLGLP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11431473" FT /id="VSP_023684" FT VAR_SEQ 227..881 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11431473" FT /id="VSP_023685" FT VAR_SEQ 468..496 FT /note="TGNDSDSGTLERKRPASMAVMEGDLVKKE -> MCGFNTCGPMGFCLSSLLA FT WCVDCFFSLC (in isoform 7)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_023686" FT VAR_SEQ 497..574 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11431473, FT ECO:0000303|PubMed:14702039" FT /id="VSP_023687" FT VAR_SEQ 839..881 FT /note="DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL -> GFQNR FT IAASFLKCTQTQPAKTCLAASCWI (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023688" FT VAR_SEQ 840..881 FT /note="SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTAL -> V (in FT isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023689" FT MUTAGEN 288 FT /note="R->A: Loss of function; leading to defects in tight FT junction maintenance." FT /evidence="ECO:0000269|PubMed:11431473" FT CONFLICT 139 FT /note="K -> E (in Ref. 2; BAB55203)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="Q -> R (in Ref. 1; CAC37948)" FT /evidence="ECO:0000305" FT CONFLICT 186 FT /note="K -> R (in Ref. 1; CAC37948)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="E -> A (in Ref. 2; BAB14506)" FT /evidence="ECO:0000305" FT CONFLICT 404 FT /note="G -> A (in Ref. 2; BAB55203)" FT /evidence="ECO:0000305" FT CONFLICT 575 FT /note="S -> C (in Ref. 2; BAC86144)" FT /evidence="ECO:0000305" FT CONFLICT 855 FT /note="M -> V (in Ref. 2; BAB55203)" FT /evidence="ECO:0000305" 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 //