ID CYH1_HUMAN Reviewed; 398 AA. AC Q15438; A6NFW7; B7Z1T4; Q9P123; Q9P124; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 24-JAN-2024, entry version 204. DE RecName: Full=Cytohesin-1; DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 1; DE AltName: Full=SEC7 homolog B2-1; GN Name=CYTH1 {ECO:0000312|HGNC:HGNC:9501}; Synonyms=D17S811E, PSCD1; 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]. RX PubMed=1511013; DOI=10.1016/0167-4781(92)90055-5; RA Liu L., Pohajdak B.; RT "Cloning and sequencing of a human cDNA from cytolytic NK/T cells with RT homology to yeast SEC7."; RL Biochim. Biophys. Acta 1132:75-78(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cerebellum; 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 GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin, and Testis; 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 [GENOMIC DNA] OF 9-398, FUNCTION, AND ALTERNATIVE RP SPLICING. RX PubMed=10652308; DOI=10.1074/jbc.275.5.3221; RA Ogasawara M., Kim S.C., Adamik R., Togawa A., Ferrans V.J., Takeda K., RA Kirby M., Moss J., Vaughan M.; RT "Similarities in function and gene structure of cytohesin-4 and cytohesin- RT 1, guanine nucleotide-exchange proteins for ADP-ribosylation factors."; RL J. Biol. Chem. 275:3221-3230(2000). RN [6] RP INTERACTION WITH TRIM23. RX PubMed=10748148; DOI=10.1074/jbc.m909642199; RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J., RA Vaughan M.; RT "Specific functional interaction of human cytohesin-1 and ADP-ribosylation RT factor domain protein (ARD1)."; RL J. Biol. Chem. 275:21331-21339(2000). RN [7] RP INTERACTION WITH CYTIP. RX PubMed=11867758; DOI=10.1073/pnas.052712999; RA Tang P., Cheng T.P., Agnello D., Wu C.-Y., Hissong B.D., Watford W.T., RA Ahn H.-J., Galon J., Moss J., Vaughan M., O'Shea J.J., Gadina M.; RT "Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates RT its activity."; RL Proc. Natl. Acad. Sci. U.S.A. 99:2625-2629(2002). RN [8] RP SUBCELLULAR LOCATION. RX PubMed=17398095; DOI=10.1016/j.cub.2007.03.007; RA Hofmann I., Thompson A., Sanderson C.M., Munro S.; RT "The Arl4 family of small G proteins can recruit the cytohesin Arf6 RT exchange factors to the plasma membrane."; RL Curr. Biol. 17:711-716(2007). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [10] RP INTERACTION WITH INAVA, UBIQUITINATION, AND FUNCTION. RX PubMed=29420262; DOI=10.1126/science.aan0814; RA Mohanan V., Nakata T., Desch A.N., Levesque C., Boroughs A., Guzman G., RA Cao Z., Creasey E., Yao J., Boucher G., Charron G., Bhan A.K., Schenone M., RA Carr S.A., Reinecker H.C., Daly M.J., Rioux J.D., Lassen K.G., Xavier R.J.; RT "C1orf106 is a colitis risk gene that regulates stability of epithelial RT adherens junctions."; RL Science 359:1161-1166(2018). RN [11] RP STRUCTURE BY NMR OF 58-256, FUNCTION, AND MUTAGENESIS OF GLU-157; TYR-187 RP AND MET-195. RX PubMed=9653114; DOI=10.1073/pnas.95.14.7909; RA Betz S.F., Schnuchel A., Wang H., Olejniczak E.T., Meadows R.P., RA Lipsky B.P., Harris E.A., Staunton D.E., Fesik S.W.; RT "Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its RT interaction with the GTPase ADP ribosylation factor 1."; RL Proc. Natl. Acad. Sci. U.S.A. 95:7909-7914(1998). CC -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1, ARF5 and ARF6. CC Promotes the activation of ARF factors through replacement of GDP with CC GTP. Plays an important role in membrane trafficking, during junctional CC remodeling and epithelial polarization, through regulation of ARF6 CC activity. {ECO:0000250|UniProtKB:Q9QX11, ECO:0000269|PubMed:10652308, CC ECO:0000269|PubMed:29420262, ECO:0000269|PubMed:9653114}. CC -!- SUBUNIT: Interacts with TRIM23 and CYTIP (PubMed:10748148, CC PubMed:11867758). Interacts (via coiled-coil domain) with FRMD4A (via CC coiled-coil domain) (By similarity). Interacts with FRMD4B (By CC similarity). Found in a complex with PARD3, CYTH1 and FRMD4A (By CC similarity). Interacts (via N-terminal domain) with INAVA (via N- CC terminal domain) (PubMed:29420262). {ECO:0000250|UniProtKB:Q9QX11, CC ECO:0000269|PubMed:10748148, ECO:0000269|PubMed:11867758, CC ECO:0000269|PubMed:29420262}. CC -!- INTERACTION: CC Q15438; P31749: AKT1; NbExp=3; IntAct=EBI-997830, EBI-296087; CC Q15438; Q96BI3: APH1A; NbExp=3; IntAct=EBI-997830, EBI-2606935; CC Q15438; P23560-2: BDNF; NbExp=3; IntAct=EBI-997830, EBI-12275524; CC Q15438; P35520: CBS; NbExp=3; IntAct=EBI-997830, EBI-740135; CC Q15438; Q96HB5: CCDC120; NbExp=9; IntAct=EBI-997830, EBI-744556; CC Q15438; Q969H4: CNKSR1; NbExp=4; IntAct=EBI-997830, EBI-741671; CC Q15438; O60759: CYTIP; NbExp=6; IntAct=EBI-997830, EBI-997814; CC Q15438; Q92915-2: FGF14; NbExp=3; IntAct=EBI-997830, EBI-12836320; CC Q15438; P15408: FOSL2; NbExp=3; IntAct=EBI-997830, EBI-3893419; CC Q15438; P07900: HSP90AA1; NbExp=3; IntAct=EBI-997830, EBI-296047; CC Q15438; Q3KP66: INAVA; NbExp=6; IntAct=EBI-997830, EBI-7545562; CC Q15438; Q8WWN9: IPCEF1; NbExp=6; IntAct=EBI-997830, EBI-4401965; CC Q15438; Q9NZ42: PSENEN; NbExp=3; IntAct=EBI-997830, EBI-998468; CC Q15438; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-997830, EBI-12004298; CC Q15438; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-997830, EBI-357085; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17398095}; CC Peripheral membrane protein {ECO:0000269|PubMed:17398095}. Cytoplasm, CC cytosol {ECO:0000250|UniProtKB:Q9QX11}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:Q9QX11}. Cell junction, adherens junction CC {ECO:0000250|UniProtKB:Q9QX11}. Note=Colocalized with TJP1 during CC epithelial polarization. {ECO:0000250|UniProtKB:Q9QX11}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q15438-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15438-2; Sequence=VSP_006034; CC Name=3; CC IsoId=Q15438-3; Sequence=VSP_055884; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DOMAIN: Binds via its PH domain to the inositol head group of CC phosphatidylinositol 3,4,5-trisphosphate. {ECO:0000250}. CC -!- DOMAIN: Autoinhibited by its C-terminal basic region. CC {ECO:0000250|UniProtKB:Q9QX11}. CC -!- PTM: Ubiquitinated by SCF(FBXW11) E3 ubiquitin-protein ligase complex. CC Ubiquitination induces proteasomal degradation. CC {ECO:0000269|PubMed:29420262}. 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; M85169; AAA36602.1; -; mRNA. DR EMBL; AK293894; BAH11620.1; -; mRNA. DR EMBL; AK316277; BAH14648.1; -; mRNA. DR EMBL; AC022966; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038385; AAH38385.1; -; mRNA. DR EMBL; BC050452; AAH50452.1; -; mRNA. DR EMBL; AF125362; AAF37737.1; -; Genomic_DNA. DR EMBL; AF125350; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125351; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125352; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125353; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125354; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125355; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125356; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125357; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125359; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125360; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125361; AAF37737.1; JOINED; Genomic_DNA. DR EMBL; AF125362; AAF37738.1; -; Genomic_DNA. DR EMBL; AF125350; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125351; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125352; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125353; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125354; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125355; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125356; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125357; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125358; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125359; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125360; AAF37738.1; JOINED; Genomic_DNA. DR EMBL; AF125361; AAF37738.1; JOINED; Genomic_DNA. DR CCDS; CCDS32754.1; -. [Q15438-2] DR CCDS; CCDS42392.3; -. [Q15438-1] DR CCDS; CCDS86644.1; -. [Q15438-3] DR PIR; S24168; S24168. DR RefSeq; NP_001278947.1; NM_001292018.1. [Q15438-3] DR RefSeq; NP_001278948.1; NM_001292019.1. [Q15438-3] DR RefSeq; NP_004753.1; NM_004762.3. [Q15438-1] DR RefSeq; NP_059430.2; NM_017456.3. [Q15438-2] DR RefSeq; XP_011523779.1; XM_011525477.1. [Q15438-3] DR PDB; 1BC9; NMR; -; A=58-256. DR PDB; 4A4P; X-ray; 2.00 A; A/B=63-248. DR PDBsum; 1BC9; -. DR PDBsum; 4A4P; -. DR AlphaFoldDB; Q15438; -. DR SMR; Q15438; -. DR BioGRID; 114688; 52. DR IntAct; Q15438; 29. DR MINT; Q15438; -. DR STRING; 9606.ENSP00000389095; -. DR iPTMnet; Q15438; -. DR PhosphoSitePlus; Q15438; -. DR BioMuta; CYTH1; -. DR DMDM; 2498175; -. DR EPD; Q15438; -. DR jPOST; Q15438; -. DR MassIVE; Q15438; -. DR MaxQB; Q15438; -. DR PaxDb; 9606-ENSP00000354398; -. DR PeptideAtlas; Q15438; -. DR ProteomicsDB; 60597; -. [Q15438-1] DR ProteomicsDB; 60598; -. [Q15438-2] DR ProteomicsDB; 6366; -. DR Pumba; Q15438; -. DR Antibodypedia; 19745; 287 antibodies from 33 providers. DR DNASU; 9267; -. DR Ensembl; ENST00000446868.8; ENSP00000389095.3; ENSG00000108669.18. [Q15438-1] DR Ensembl; ENST00000585509.5; ENSP00000465940.1; ENSG00000108669.18. [Q15438-3] DR Ensembl; ENST00000589297.5; ENSP00000466512.1; ENSG00000108669.18. [Q15438-3] DR Ensembl; ENST00000591455.5; ENSP00000465665.1; ENSG00000108669.18. [Q15438-2] DR GeneID; 9267; -. DR KEGG; hsa:9267; -. DR MANE-Select; ENST00000446868.8; ENSP00000389095.3; NM_004762.6; NP_004753.1. DR UCSC; uc002jvw.4; human. [Q15438-1] DR AGR; HGNC:9501; -. DR CTD; 9267; -. DR DisGeNET; 9267; -. DR GeneCards; CYTH1; -. DR HGNC; HGNC:9501; CYTH1. DR HPA; ENSG00000108669; Low tissue specificity. DR MIM; 182115; gene. DR neXtProt; NX_Q15438; -. DR OpenTargets; ENSG00000108669; -. DR PharmGKB; PA164718528; -. DR VEuPathDB; HostDB:ENSG00000108669; -. DR eggNOG; KOG0930; Eukaryota. DR GeneTree; ENSGT00940000157519; -. DR HOGENOM; CLU_032820_3_0_1; -. DR InParanoid; Q15438; -. DR OMA; IPDNKDR; -. DR OrthoDB; 204547at2759; -. DR PhylomeDB; Q15438; -. DR TreeFam; TF352091; -. DR PathwayCommons; Q15438; -. DR Reactome; R-HSA-6811438; Intra-Golgi traffic. DR SignaLink; Q15438; -. DR SIGNOR; Q15438; -. DR BioGRID-ORCS; 9267; 24 hits in 1156 CRISPR screens. DR ChiTaRS; CYTH1; human. DR EvolutionaryTrace; Q15438; -. DR GeneWiki; CYTH1; -. DR GenomeRNAi; 9267; -. DR Pharos; Q15438; Tbio. DR PRO; PR:Q15438; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q15438; Protein. DR Bgee; ENSG00000108669; Expressed in granulocyte and 198 other cell types or tissues. DR ExpressionAtlas; Q15438; baseline and differential. DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell. DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB. DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro. DR GO; GO:0030155; P:regulation of cell adhesion; IDA:MGI. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc. DR CDD; cd01252; PH_GRP1-like; 1. DR CDD; cd00171; Sec7; 1. DR Gene3D; 1.10.220.20; -; 1. DR Gene3D; 1.10.1000.11; Arf Nucleotide-binding Site Opener,domain 2; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR023394; Sec7_C_sf. DR InterPro; IPR000904; Sec7_dom. DR InterPro; IPR035999; Sec7_dom_sf. DR PANTHER; PTHR10663:SF340; CYTOHESIN-1; 1. DR PANTHER; PTHR10663; GUANYL-NUCLEOTIDE EXCHANGE FACTOR; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF01369; Sec7; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00222; Sec7; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF48425; Sec7 domain; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50190; SEC7; 1. DR Genevisible; Q15438; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell junction; KW Cell membrane; Coiled coil; Cytoplasm; Guanine-nucleotide releasing factor; KW Lipid-binding; Membrane; Reference proteome; Tight junction; KW Ubl conjugation. FT CHAIN 1..398 FT /note="Cytohesin-1" FT /id="PRO_0000120194" FT DOMAIN 73..202 FT /note="SEC7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189" FT DOMAIN 260..377 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 388..396 FT /note="C-terminal autoinhibitory region" FT /evidence="ECO:0000250" FT COILED 10..67 FT /evidence="ECO:0000255" FT BINDING 269..277 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000250" FT BINDING 281 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000250" FT BINDING 292 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000250" FT BINDING 302 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000250" FT BINDING 351 FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo- FT inositol-3,4,5-trisphosphate)" FT /ligand_id="ChEBI:CHEBI:57836" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT VAR_SEQ 1..59 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055884" FT VAR_SEQ 273 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_006034" FT MUTAGEN 157 FT /note="E->A,K: Reduces guanine exchange factor activity by FT over 90%." FT /evidence="ECO:0000269|PubMed:9653114" FT MUTAGEN 187 FT /note="Y->A: Reduces guanine exchange factor activity by FT over 90%." FT /evidence="ECO:0000269|PubMed:9653114" FT MUTAGEN 195 FT /note="M->A: Reduces guanine exchange factor activity by FT over 90%." FT /evidence="ECO:0000269|PubMed:9653114" FT CONFLICT 353..361 FT /note="TVYRISAPT -> MFTGSQLRR (in Ref. 4; FT AAF37737/AAF37738)" FT /evidence="ECO:0000305" FT HELIX 64..75 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 77..86 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 94..103 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 109..116 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 121..133 FT /evidence="ECO:0007829|PDB:4A4P" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:1BC9" FT HELIX 141..150 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 158..175 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 183..201 FT /evidence="ECO:0007829|PDB:4A4P" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:1BC9" FT HELIX 211..217 FT /evidence="ECO:0007829|PDB:4A4P" FT TURN 218..221 FT /evidence="ECO:0007829|PDB:4A4P" FT HELIX 229..241 FT /evidence="ECO:0007829|PDB:4A4P" FT STRAND 246..248 FT /evidence="ECO:0007829|PDB:1BC9" SQ SEQUENCE 398 AA; 46413 MW; 067FEE0FEA7A4C86 CRC64; MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKDE IAEVANEIEN LGSTEERKNM QRNKQVAMGR KKFNMDPKKG IQFLIENDLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD EFNIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNNGVF QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP TPEEKEEWIK CIKAAISRDP FYEMLAARKK KVSSTKRH //