ID RHG17_HUMAN Reviewed; 881 AA. AC Q68EM7; A8K6M6; Q6ZUS4; Q7Z2F2; Q8NDG2; Q96KS2; Q96KS3; Q96SS8; AC Q9BVF6; Q9H8U5; Q9NW54; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 08-MAY-2019, entry version 138. 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; 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 RP BY 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 RP BY 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., 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 IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver 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., RA Ayoub D., 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 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. {ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:16678097}. CC -!- SUBUNIT: Component of a complex whose core is composed of CC ARHGAP17, AMOT, MPP5/PALS1, PATJ and PARD3/PAR3. Interacts with CC SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3), CAPZB, CC CD2AP and SH3KBP1/CIN85. {ECO:0000269|PubMed:11285285, CC ECO:0000269|PubMed:11431473, ECO:0000269|PubMed:16678097}. CC -!- INTERACTION: CC Q4VCS5:AMOT; NbExp=2; IntAct=EBI-1642807, EBI-2511319; CC Q4VCS5-2:AMOT; NbExp=4; IntAct=EBI-1642807, EBI-3891843; CC Q15642:TRIP10; NbExp=3; IntAct=EBI-1642807, EBI-739936; 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. {ECO:0000269|PubMed:11431473}. CC -!- DOMAIN: The BAR domain mediates the interaction with the coiled CC coil domain of AMOT, leading to its recruitment to tight CC junctions. {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 SMR; Q68EM7; -. DR BioGrid; 120424; 53. DR CORUM; Q68EM7; -. DR IntAct; Q68EM7; 11. DR MINT; Q68EM7; -. DR STRING; 9606.ENSP00000289968; -. DR iPTMnet; Q68EM7; -. DR PhosphoSitePlus; Q68EM7; -. DR SwissPalm; Q68EM7; -. DR BioMuta; ARHGAP17; -. DR DMDM; 74736331; -. DR EPD; Q68EM7; -. DR jPOST; Q68EM7; -. DR MaxQB; Q68EM7; -. DR PaxDb; Q68EM7; -. DR PeptideAtlas; Q68EM7; -. DR PRIDE; Q68EM7; -. DR ProteomicsDB; 66129; -. 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 Ensembl; ENST00000289968; ENSP00000289968; ENSG00000140750. [Q68EM7-1] DR Ensembl; ENST00000303665; ENSP00000303130; ENSG00000140750. [Q68EM7-2] DR GeneID; 55114; -. DR KEGG; hsa:55114; -. DR UCSC; uc002dnb.5; human. [Q68EM7-1] DR CTD; 55114; -. DR GeneCards; ARHGAP17; -. DR HGNC; HGNC:18239; ARHGAP17. DR HPA; HPA041703; -. DR MIM; 608293; gene. DR neXtProt; NX_Q68EM7; -. DR OpenTargets; ENSG00000140750; -. DR PharmGKB; PA134908575; -. DR eggNOG; KOG4270; Eukaryota. DR eggNOG; ENOG410XRR2; LUCA. DR GeneTree; ENSGT00940000156201; -. DR InParanoid; Q68EM7; -. DR KO; K20638; -. DR OMA; FRDPLRG; -. DR OrthoDB; 821331at2759; -. DR PhylomeDB; Q68EM7; -. DR TreeFam; TF350627; -. DR Reactome; R-HSA-194840; Rho GTPase cycle. DR ChiTaRS; ARHGAP17; human. DR GenomeRNAi; 55114; -. DR PRO; PR:Q68EM7; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000140750; Expressed in 221 organ(s), highest expression level in corpus callosum. DR ExpressionAtlas; Q68EM7; baseline and differential. DR Genevisible; Q68EM7; HS. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central. DR GO; GO:0048365; F:Rac GTPase binding; IBA:GO_Central. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0017156; P:calcium ion regulated exocytosis; IBA:GO_Central. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome. 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; 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. {ECO:0000255|PROSITE- FT ProRule:PRU00361}. FT DOMAIN 252 442 Rho-GAP. {ECO:0000255|PROSITE- FT ProRule:PRU00172}. FT MOTIF 753 766 SH3-binding. {ECO:0000255}. FT COMPBIAS 521 816 Pro-rich. FT MOD_RES 484 484 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 575 575 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:21406692, FT ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 679 679 Phosphothreonine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 682 682 Phosphothreonine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 702 702 Phosphoserine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT MOD_RES 704 704 Phosphoserine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT MOD_RES 753 753 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT MOD_RES 757 757 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT MOD_RES 759 759 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT MOD_RES 762 762 Phosphoserine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT MOD_RES 763 763 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q3UIA2}. FT VAR_SEQ 1 467 Missing (in isoform 7). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_023682. FT VAR_SEQ 1 273 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_023683. FT VAR_SEQ 215 226 LLEAQADYHRKA -> ISGRKNQPLGLP (in isoform FT 4). {ECO:0000303|PubMed:11431473}. FT /FTId=VSP_023684. FT VAR_SEQ 227 881 Missing (in isoform 4). FT {ECO:0000303|PubMed:11431473}. FT /FTId=VSP_023685. FT VAR_SEQ 468 496 TGNDSDSGTLERKRPASMAVMEGDLVKKE -> MCGFNTCG FT PMGFCLSSLLAWCVDCFFSLC (in isoform 7). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_023686. FT VAR_SEQ 497 574 Missing (in isoform 2). FT {ECO:0000303|PubMed:11431473, FT ECO:0000303|PubMed:14702039}. FT /FTId=VSP_023687. FT VAR_SEQ 839 881 DSNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTEST FT AL -> GFQNRIAASFLKCTQTQPAKTCLAASCWI (in FT isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_023688. FT VAR_SEQ 840 881 SNSRVSEPHRSIFPEMHSDSASKDVPGRILLDIDNDTESTA FT L -> V (in isoform 6). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_023689. FT MUTAGEN 288 288 R->A: Loss of function; leading to FT defects in tight junction maintenance. FT {ECO:0000269|PubMed:11431473}. FT CONFLICT 139 139 K -> E (in Ref. 2; BAB55203). FT {ECO:0000305}. FT CONFLICT 167 167 Q -> R (in Ref. 1; CAC37948). FT {ECO:0000305}. FT CONFLICT 186 186 K -> R (in Ref. 1; CAC37948). FT {ECO:0000305}. FT CONFLICT 255 255 E -> A (in Ref. 2; BAB14506). FT {ECO:0000305}. FT CONFLICT 404 404 G -> A (in Ref. 2; BAB55203). FT {ECO:0000305}. FT CONFLICT 575 575 S -> C (in Ref. 2; BAC86144). FT {ECO:0000305}. FT CONFLICT 855 855 M -> V (in Ref. 2; BAB55203). FT {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 //