ID CYH2_HUMAN Reviewed; 400 AA. AC Q99418; A8K8P0; Q8IXY9; Q92958; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 24-JAN-2024, entry version 209. DE RecName: Full=Cytohesin-2; DE AltName: Full=ARF exchange factor; DE AltName: Full=ARF nucleotide-binding site opener; DE Short=Protein ARNO; DE AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 2; GN Name=CYTH2 {ECO:0000312|HGNC:HGNC:9502}; Synonyms=ARNO, PSCD2, PSCD2L; 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] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=8945478; DOI=10.1038/384481a0; RA Chardin P., Paris S., Antonny B., Robineau S., Bernaud-Dufour S., RA Jackson C.L., Chabre M.; RT "A human exchange factor for ARF contains Sec7- and pleckstrin-homology RT domains."; RL Nature 384:481-484(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION. RC TISSUE=Brain; RX PubMed=9417041; DOI=10.1074/jbc.273.1.23; RA Frank S.F., Upender S.K., Hansen S.H., Casanova J.E.; RT "ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor RT 6."; RL J. Biol. Chem. 273:23-27(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, 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 INTERACTION WITH ARRB1. RX PubMed=17623778; DOI=10.1242/jcs.03469; RA Bouschet T., Martin S., Kanamarlapudi V., Mundell S., Henley J.M.; RT "The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO RT ARF6 ELMO protein network."; RL J. Cell Sci. 120:2489-2497(2007). RN [6] RP FUNCTION, INTERACTION WITH ARL4D AND ARRB1, MUTAGENESIS OF GLU-156; RP LYS-268; ARG-280; ILE-303 AND LYS-336, AND 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 [7] RP INTERACTION WITH CCDC120. RX PubMed=25326380; DOI=10.1074/jbc.m114.575787; RA Torii T., Miyamoto Y., Tago K., Sango K., Nakamura K., Sanbe A., Tanoue A., RA Yamauchi J.; RT "Arf6 guanine nucleotide exchange factor cytohesin-2 binds to CCDC120 and RT is transported along neurites to mediate neurite growth."; RL J. Biol. Chem. 289:33887-33903(2014). RN [8] RP INTERACTION WITH INAVA. 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 [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 51-252. RX PubMed=9476900; DOI=10.1016/s0092-8674(00)80933-2; RA Mossessova E., Gulbis J.M., Goldberg J.; RT "Structure of the guanine nucleotide exchange factor Sec7 domain of human RT ARNO and analysis of the interaction with ARF GTPase."; RL Cell 92:415-423(1998). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 51-252. RX PubMed=9510256; DOI=10.1038/32210; RA Cherfils J., Menetrey J., Mathieu M., le Bras G., Robineau S., RA Beraud-Dufour S., Antonny B., Chardin P.; RT "Structure of the Sec7 domain of the Arf exchange factor ARNO."; RL Nature 392:101-105(1998). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 50-252 IN COMPLEX WITH ARF1; GDP RP AND BREFELDIN A. RX PubMed=14654833; DOI=10.1038/nature02197; RA Renault L., Guibert B., Cherfils J.; RT "Structural snapshots of the mechanism and inhibition of a guanine RT nucleotide exchange factor."; RL Nature 426:525-530(2003). CC -!- FUNCTION: Acts as a guanine-nucleotide exchange factor (GEF). Promotes CC guanine-nucleotide exchange on ARF1, ARF3 and ARF6. Activates ARF CC factors through replacement of GDP with GTP (By similarity). The cell CC membrane form, in association with ARL4 proteins, recruits ARF6 to the CC plasma membrane (PubMed:17398095). Involved in neurite growth (By CC similarity). {ECO:0000250|UniProtKB:P63034, CC ECO:0000269|PubMed:17398095}. CC -!- SUBUNIT: Heteromer. Composed of TAMALIN, CYTH2 and at least one GRM1 CC (By similarity). Interacts with ARRB1 (PubMed:17623778, CC PubMed:17398095). Interacts with ARL4D; the interaction is direct CC (PubMed:17398095). Directly interacts with CCDC120 through the coiled CC coil domain; this interaction stabilizes CCDC120, possibly by CC preventing its ubiquitination, and is required for neurite growth in CC neuroblastoma cells (PubMed:25326380). Interacts with ARF1 CC (PubMed:14654833). Interacts with FRMD4A (By similarity). Interacts CC (via N-terminal domain) with INAVA (via N-terminal domain) CC (PubMed:29420262). {ECO:0000250|UniProtKB:P63034, CC ECO:0000269|PubMed:14654833, ECO:0000269|PubMed:17398095, CC ECO:0000269|PubMed:17623778, ECO:0000269|PubMed:25326380, CC ECO:0000269|PubMed:29420262}. CC -!- INTERACTION: CC Q99418; P29274: ADORA2A; NbExp=6; IntAct=EBI-448974, EBI-2902702; CC Q99418; P84077: ARF1; NbExp=5; IntAct=EBI-448974, EBI-447171; CC Q99418; Q9Y487: ATP6V0A2; NbExp=2; IntAct=EBI-448974, EBI-988630; CC Q99418; Q96HB5: CCDC120; NbExp=4; IntAct=EBI-448974, EBI-744556; CC Q99418; Q96HB5-4: CCDC120; NbExp=4; IntAct=EBI-448974, EBI-10185348; CC Q99418; Q969H4: CNKSR1; NbExp=3; IntAct=EBI-448974, EBI-741671; CC Q99418; Q3KP66: INAVA; NbExp=2; IntAct=EBI-448974, EBI-7545562; CC Q99418; Q8WWN9: IPCEF1; NbExp=6; IntAct=EBI-448974, EBI-4401965; CC Q99418; Q99836-1: MYD88; NbExp=3; IntAct=EBI-448974, EBI-15855480; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17398095}; CC Peripheral membrane protein {ECO:0000269|PubMed:17398095}. Cytoplasm CC {ECO:0000269|PubMed:17398095}. Cell projection CC {ECO:0000250|UniProtKB:P63034}. Cell projection, growth cone CC {ECO:0000250|UniProtKB:P63034}. Cell junction, tight junction CC {ECO:0000250|UniProtKB:P63034}. Cell junction, adherens junction CC {ECO:0000250|UniProtKB:P63034}. Note=Both isoform 1 and isoform 2 are CC recruited to the cell membrane through its association with ARL4A, CC ARL4C and ARL4D. They require also interaction with phosphoinositides CC for targeting to plasma membrane (PubMed:17398095). In differentiating CC neuroblastoma cells, colocalizes with CCDC120 in both neurite shaft and CC growth cone areas. {ECO:0000250|UniProtKB:P63034, CC ECO:0000269|PubMed:17398095}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99418-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99418-2; Sequence=VSP_006036; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000305|PubMed:9417041}. CC -!- DOMAIN: Binds via its PH domain to the inositol head group of CC phosphatidylinositol 3,4,5-trisphosphate. The PH domain is necessary CC and sufficient for plasma membrane relocalization. CC -!- DOMAIN: Autoinhibited by its C-terminal basic region. {ECO:0000250}. CC -!- DOMAIN: The coiled coil domain is involved in interaction with CCDC120. CC {ECO:0000250|UniProtKB:P63034}. 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; X99753; CAA68084.1; -; mRNA. DR EMBL; U70728; AAB09591.1; -; mRNA. DR EMBL; AK292405; BAF85094.1; -; mRNA. DR EMBL; BC004361; AAH04361.1; -; mRNA. DR EMBL; BC038713; AAH38713.1; -; mRNA. DR CCDS; CCDS12722.1; -. [Q99418-2] DR CCDS; CCDS86786.1; -. [Q99418-1] DR RefSeq; NP_004219.3; NM_004228.6. [Q99418-2] DR RefSeq; NP_059431.1; NM_017457.5. [Q99418-1] DR PDB; 1PBV; X-ray; 2.00 A; A=52-246. DR PDB; 1R8M; X-ray; 1.70 A; E=50-252. DR PDB; 1R8Q; X-ray; 1.86 A; E/F=50-252. DR PDB; 1R8S; X-ray; 1.46 A; E=50-252. DR PDB; 1S9D; X-ray; 1.80 A; E=50-252. DR PDB; 4JMI; X-ray; 1.50 A; A=56-251. DR PDB; 4JMO; X-ray; 1.80 A; A=56-251. DR PDB; 4JWL; X-ray; 1.95 A; A=56-251. DR PDB; 4JXH; X-ray; 1.47 A; A=56-251. DR PDB; 4L5M; X-ray; 1.80 A; A=56-251. DR PDB; 4Z21; X-ray; 2.05 A; A=51-252. DR PDBsum; 1PBV; -. DR PDBsum; 1R8M; -. DR PDBsum; 1R8Q; -. DR PDBsum; 1R8S; -. DR PDBsum; 1S9D; -. DR PDBsum; 4JMI; -. DR PDBsum; 4JMO; -. DR PDBsum; 4JWL; -. DR PDBsum; 4JXH; -. DR PDBsum; 4L5M; -. DR PDBsum; 4Z21; -. DR AlphaFoldDB; Q99418; -. DR BMRB; Q99418; -. DR SASBDB; Q99418; -. DR SMR; Q99418; -. DR BioGRID; 114687; 50. DR DIP; DIP-31598N; -. DR IntAct; Q99418; 20. DR MINT; Q99418; -. DR STRING; 9606.ENSP00000493357; -. DR BindingDB; Q99418; -. DR ChEMBL; CHEMBL5995; -. DR DrugBank; DB03401; 1D-myo-inositol 1,4,5-trisphosphate. DR DrugBank; DB07348; Brefeldin A. DR DrugBank; DB01942; Formic acid. DR DrugBank; DB01863; Inositol 1,3,4,5-Tetrakisphosphate. DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine. DR iPTMnet; Q99418; -. DR PhosphoSitePlus; Q99418; -. DR BioMuta; CYTH2; -. DR DMDM; 13124707; -. DR EPD; Q99418; -. DR jPOST; Q99418; -. DR MassIVE; Q99418; -. DR MaxQB; Q99418; -. DR PaxDb; 9606-ENSP00000408236; -. DR PeptideAtlas; Q99418; -. DR ProteomicsDB; 78258; -. [Q99418-1] DR ProteomicsDB; 78259; -. [Q99418-2] DR Pumba; Q99418; -. DR Antibodypedia; 4437; 323 antibodies from 33 providers. DR DNASU; 9266; -. DR Ensembl; ENST00000452733.7; ENSP00000408236.2; ENSG00000105443.17. [Q99418-2] DR Ensembl; ENST00000641098.1; ENSP00000493357.1; ENSG00000105443.17. [Q99418-1] DR GeneID; 9266; -. DR KEGG; hsa:9266; -. DR MANE-Select; ENST00000452733.7; ENSP00000408236.2; NM_004228.7; NP_004219.3. [Q99418-2] DR UCSC; uc002pjj.5; human. [Q99418-1] DR AGR; HGNC:9502; -. DR CTD; 9266; -. DR DisGeNET; 9266; -. DR GeneCards; CYTH2; -. DR HGNC; HGNC:9502; CYTH2. DR HPA; ENSG00000105443; Low tissue specificity. DR MIM; 602488; gene. DR neXtProt; NX_Q99418; -. DR OpenTargets; ENSG00000105443; -. DR PharmGKB; PA33849; -. DR VEuPathDB; HostDB:ENSG00000105443; -. DR eggNOG; KOG0930; Eukaryota. DR GeneTree; ENSGT00940000160074; -. DR HOGENOM; CLU_032820_3_0_1; -. DR InParanoid; Q99418; -. DR OMA; GASHWRA; -. DR OrthoDB; 204547at2759; -. DR PhylomeDB; Q99418; -. DR TreeFam; TF352091; -. DR PathwayCommons; Q99418; -. DR Reactome; R-HSA-6811438; Intra-Golgi traffic. DR SignaLink; Q99418; -. DR SIGNOR; Q99418; -. DR BioGRID-ORCS; 9266; 12 hits in 1157 CRISPR screens. DR ChiTaRS; CYTH2; human. DR EvolutionaryTrace; Q99418; -. DR GeneWiki; CYTH2; -. DR GenomeRNAi; 9266; -. DR Pharos; Q99418; Tbio. DR PRO; PR:Q99418; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q99418; Protein. DR Bgee; ENSG00000105443; Expressed in ganglionic eminence and 197 other cell types or tissues. DR ExpressionAtlas; Q99418; baseline and differential. DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell. DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB. DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISS:UniProtKB. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc. DR GO; GO:0006897; P:endocytosis; TAS:ProtInc. DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro. 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:SF343; CYTOHESIN-2; 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; Q99418; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell junction; Cell membrane; KW Cell projection; Coiled coil; Cytoplasm; KW Guanine-nucleotide releasing factor; Lipid-binding; Membrane; KW Reference proteome; Tight junction. FT CHAIN 1..400 FT /note="Cytohesin-2" FT /id="PRO_0000120197" FT DOMAIN 72..201 FT /note="SEC7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189" FT DOMAIN 259..376 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 387..395 FT /note="C-terminal autoinhibitory region" FT /evidence="ECO:0000250" FT COILED 10..63 FT /evidence="ECO:0000255" FT BINDING 268..276 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 280 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 291 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 301 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 339 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 350 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 VAR_SEQ 272 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9417041" FT /id="VSP_006036" FT MUTAGEN 156 FT /note="E->D: Inhibits GTPGDP exchange activity. Abolishes FT recruitment of ARF6 to the plasma membrane." FT /evidence="ECO:0000269|PubMed:17398095" FT MUTAGEN 268 FT /note="K->R: Does not reduce ARL4DGTP-dependent interaction FT but inhibits targeting to the plasma membrane mediated by FT ARL4C, ARL4C and ARL4D." FT /evidence="ECO:0000269|PubMed:17398095" FT MUTAGEN 280 FT /note="R->D: Does not reduce ARL4DGTP-dependent interaction FT but inhibits targeting to the plasma membrane mediated by FT ARL4C, ARL4C and ARL4D." FT /evidence="ECO:0000269|PubMed:17398095" FT MUTAGEN 303 FT /note="I->A: Reduces ARL4DGTP-dependent interaction and FT targeting to the plasma membrane mediated by ARL4C, ARL4C FT and ARL4D." FT /evidence="ECO:0000269|PubMed:17398095" FT MUTAGEN 336 FT /note="K->A: Reduces ARL4DGTP-dependent interaction and FT targeting to the plasma membrane mediated by ARL4C, ARL4C FT and ARL4D." FT /evidence="ECO:0000269|PubMed:17398095" FT CONFLICT 306 FT /note="L -> Q (in Ref. 4; AAH38713)" FT /evidence="ECO:0000305" FT HELIX 63..74 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 76..85 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 108..115 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 120..131 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 140..149 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 157..174 FT /evidence="ECO:0007829|PDB:1R8S" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 182..200 FT /evidence="ECO:0007829|PDB:1R8S" FT HELIX 210..216 FT /evidence="ECO:0007829|PDB:1R8S" FT TURN 217..220 FT /evidence="ECO:0007829|PDB:1R8S" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:1R8M" FT HELIX 228..240 FT /evidence="ECO:0007829|PDB:1R8S" SQ SEQUENCE 400 AA; 46546 MW; 70441A58483BD0E1 CRC64; MEDGVYEPPD LTPEERMELE NIRRRKQELL VEIQRLREEL SEAMSEVEGL EANEGSKTLQ RNRKMAMGRK KFNMDPKKGI QFLVENELLQ NTPEEIARFL YKGEGLNKTA IGDYLGEREE LNLAVLHAFV DLHEFTDLNL VQALRQFLWS FRLPGEAQKI DRMMEAFAQR YCLCNPGVFQ STDTCYVLSF AVIMLNTSLH NPNVRDKPGL ERFVAMNRGI NEGGDLPEEL LRNLYDSIRN EPFKIPEDDG NDLTHTFFNP DREGWLLKLG GGRVKTWKRR WFILTDNCLY YFEYTTDKEP RGIIPLENLS IREVDDPRKP NCFELYIPNN KGQLIKACKT EADGRVVEGN HMVYRISAPT QEEKDEWIKS IQAAVSVDPF YEMLAARKKR ISVKKKQEQP //