CYH2_HUMAN
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 03-AUG-2022, entry version 201.
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}.
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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; 49.
DR DIP; DIP-31598N; -.
DR IntAct; Q99418; 20.
DR MINT; Q99418; -.
DR STRING; 9606.ENSP00000408236; -.
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; Q99418; -.
DR PeptideAtlas; Q99418; -.
DR PRIDE; Q99418; -.
DR ProteomicsDB; 78258; -. [Q99418-1]
DR ProteomicsDB; 78259; -. [Q99418-2]
DR Antibodypedia; 4437; 300 antibodies from 33 providers.
DR DNASU; 9266; -.
DR Ensembl; ENST00000452733.7; ENSP00000408236.2; ENSG00000105443.16. [Q99418-2]
DR Ensembl; ENST00000641098.1; ENSP00000493357.1; ENSG00000105443.16. [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 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; PDTCYVL; -.
DR OrthoDB; 657055at2759; -.
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 1079 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 195 other tissues.
DR ExpressionAtlas; Q99418; baseline and differential.
DR Genevisible; Q99418; HS.
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; 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; 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 GTP GDP 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 reduces ARL4D GTP-dependent
FT interaction but inhibits targeting to the plasma membrane
FT mediated by ARL4C, ARL4C and ARL4D."
FT /evidence="ECO:0000269|PubMed:17398095"
FT MUTAGEN 280
FT /note="R->D: Does not reduces ARL4D GTP-dependent
FT interaction but inhibits targeting to the plasma membrane
FT mediated by ARL4C, ARL4C and ARL4D."
FT /evidence="ECO:0000269|PubMed:17398095"
FT MUTAGEN 303
FT /note="I->A: Reduces ARL4D GTP-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 ARL4D GTP-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
