CYH1_HUMAN
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 03-AUG-2022, entry version 196.
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}.
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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; 50.
DR IntAct; Q15438; 27.
DR MINT; Q15438; -.
DR STRING; 9606.ENSP00000354398; -.
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; Q15438; -.
DR PeptideAtlas; Q15438; -.
DR PRIDE; Q15438; -.
DR ProteomicsDB; 60597; -. [Q15438-1]
DR ProteomicsDB; 60598; -. [Q15438-2]
DR ProteomicsDB; 6366; -.
DR Antibodypedia; 19745; 259 antibodies from 33 providers.
DR DNASU; 9267; -.
DR Ensembl; ENST00000361101.8; ENSP00000354398.4; ENSG00000108669.17. [Q15438-1]
DR Ensembl; ENST00000446868.8; ENSP00000389095.3; ENSG00000108669.17. [Q15438-1]
DR Ensembl; ENST00000585509.5; ENSP00000465940.1; ENSG00000108669.17. [Q15438-3]
DR Ensembl; ENST00000589297.5; ENSP00000466512.1; ENSG00000108669.17. [Q15438-3]
DR Ensembl; ENST00000591455.5; ENSP00000465665.1; ENSG00000108669.17. [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 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; CRCNNGV; -.
DR OrthoDB; 657055at2759; -.
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 1082 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 196 other tissues.
DR ExpressionAtlas; Q15438; baseline and differential.
DR Genevisible; Q15438; HS.
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:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; 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; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 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 Pfam; PF00169; PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50190; SEC7; 1.
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; AAF37737/
FT 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
