AR2BP_HUMAN
ID AR2BP_HUMAN Reviewed; 163 AA.
AC Q9Y2Y0; B3KQJ5; Q504R0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ADP-ribosylation factor-like protein 2-binding protein;
DE Short=ARF-like 2-binding protein;
DE Short=ARL2-binding protein;
DE AltName: Full=Binder of ARF2 protein 1;
GN Name=ARL2BP; Synonyms=BART, BART1;
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), INTERACTION WITH ARL2, AND TISSUE
RP SPECIFICITY.
RX PubMed=10488091; DOI=10.1074/jbc.274.39.27553;
RA Sharer J.D., Kahn R.A.;
RT "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and
RT initial characterization.";
RL J. Biol. Chem. 274:27553-27561(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Ovary;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Mammary gland;
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 ARL2 AND ARL3.
RX PubMed=11303027; DOI=10.1074/jbc.m102359200;
RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.;
RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific
RT and shared effectors: characterizing ARL1-binding proteins.";
RL J. Biol. Chem. 276:22826-22837(2001).
RN [6]
RP INTERACTION WITH ARL2 AND ARL3.
RX PubMed=11847227; DOI=10.1074/jbc.m200128200;
RA Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A.,
RA Cowan N.J.;
RT "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-
RT specific chaperone cofactor C.";
RL J. Biol. Chem. 277:14629-14634(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC25A4.
RX PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT transporter.";
RL Mol. Biol. Cell 13:71-83(2002).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=16525022; DOI=10.1091/mbc.e05-10-0929;
RA Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.;
RT "Arl2 and Arl3 regulate different microtubule-dependent processes.";
RL Mol. Biol. Cell 17:2476-2487(2006).
RN [9]
RP FUNCTION, INTERACTION WITH STAT3 AND ARL2, AND SUBCELLULAR LOCATION.
RX PubMed=18234692; DOI=10.1093/intimm/dxm154;
RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
RA Matsuda T.;
RT "BART is essential for nuclear retention of STAT3.";
RL Int. Immunol. 20:395-403(2008).
RN [10]
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., Buerckstuemmer T.,
RA 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP INVOLVEMENT IN RP82.
RX PubMed=27790702; DOI=10.1111/cge.12909;
RA Audo I., El Shamieh S., Mejecase C., Michiels C., Demontant V., Antonio A.,
RA Condroyer C., Boyard F., Letexier M., Saraiva J.P., Blanchard S.,
RA Mohand-Said S., Sahel J.A., Zeitz C.;
RT "ARL2BP mutations account for 0.1% of autosomal recessive rod-cone
RT dystrophies with the report of a novel splice variant.";
RL Clin. Genet. 92:109-111(2017).
RN [13]
RP STRUCTURE BY NMR OF 1-136, AND INTERACTION WITH ARL2.
RX PubMed=18981177; DOI=10.1074/jbc.m806167200;
RA Bailey L.K., Campbell L.J., Evetts K.A., Littlefield K., Rajendra E.,
RA Nietlispach D., Owen D., Mott H.R.;
RT "The structure of binder of Arl2 (BART) reveals a novel G protein binding
RT domain: implications for function.";
RL J. Biol. Chem. 284:992-999(2009).
RN [14]
RP INTERACTION WITH ARL2.
RX PubMed=30945270; DOI=10.1111/cge.13541;
RA Cai X.B., Wu K.C., Zhang X., Lv J.N., Jin G.H., Xiang L., Chen J.,
RA Huang X.F., Pan D., Lu B., Lu F., Qu J., Jin Z.B.;
RT "Whole-exome sequencing identified ARL2 as a novel candidate gene for MRCS
RT (microcornea, rod-cone dystrophy, cataract, and posterior staphyloma)
RT syndrome.";
RL Clin. Genet. 96:61-71(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN A COMPLEX WITH ARL2; GTP AND
RP MAGNESIUM IONS, INTERACTION WITH ARL2, AND MUTAGENESIS OF GLU-56; GLU-57;
RP GLU-74; TYR-76; PHE-109; ASP-110; MET-111; LEU-112 AND PHE-115.
RX PubMed=19368893; DOI=10.1016/j.str.2009.01.014;
RA Zhang T., Li S., Zhang Y., Zhong C., Lai Z., Ding J.;
RT "Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition
RT and binding mode of small GTPase with effector.";
RL Structure 17:602-610(2009).
RN [16]
RP VARIANT RP82 ARG-45, INTERACTION WITH ARL2, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=23849777; DOI=10.1016/j.ajhg.2013.06.003;
RA Davidson A.E., Schwarz N., Zelinger L., Stern-Schneider G., Shoemark A.,
RA Spitzbarth B., Gross M., Laxer U., Sosna J., Sergouniotis P.I.,
RA Waseem N.H., Wilson R., Kahn R.A., Plagnol V., Wolfrum U., Banin E.,
RA Hardcastle A.J., Cheetham M.E., Sharon D., Webster A.R.;
RT "Mutations in ARL2BP, encoding ADP-ribosylation-factor-like 2 binding
RT protein, cause autosomal-recessive retinitis pigmentosa.";
RL Am. J. Hum. Genet. 93:321-329(2013).
CC -!- FUNCTION: Together with ARL2, plays a role in the nuclear
CC translocation, retention and transcriptional activity of STAT3. May
CC play a role as an effector of ARL2. {ECO:0000269|PubMed:18234692}.
CC -!- SUBUNIT: Found in a complex with ARL2BP, ARL2 and SLC25A6. Found in a
CC complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and
CC STAT4. Interacts with GTP-bound ARL2 and ARL3; the complex ARL2-ARL2BP
CC as well as ARL2BP alone, binds to SLC25A4. Interaction with ARL2 may be
CC required for targeting to cilia basal body. Interacts with STAT3;
CC interaction is enhanced with ARL2. {ECO:0000269|PubMed:10488091,
CC ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:11809823,
CC ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:18234692,
CC ECO:0000269|PubMed:18981177, ECO:0000269|PubMed:19368893,
CC ECO:0000269|PubMed:23849777, ECO:0000269|PubMed:30945270}.
CC -!- INTERACTION:
CC Q9Y2Y0; P36404: ARL2; NbExp=24; IntAct=EBI-3449344, EBI-752365;
CC Q9Y2Y0; P36405: ARL3; NbExp=6; IntAct=EBI-3449344, EBI-712710;
CC Q9Y2Y0; P46379-2: BAG6; NbExp=3; IntAct=EBI-3449344, EBI-10988864;
CC Q9Y2Y0; Q9Y6A4: CFAP20; NbExp=4; IntAct=EBI-3449344, EBI-1046872;
CC Q9Y2Y0; P22607: FGFR3; NbExp=3; IntAct=EBI-3449344, EBI-348399;
CC Q9Y2Y0; P06396: GSN; NbExp=3; IntAct=EBI-3449344, EBI-351506;
CC Q9Y2Y0; O14901: KLF11; NbExp=3; IntAct=EBI-3449344, EBI-948266;
CC Q9Y2Y0; P17987: TCP1; NbExp=3; IntAct=EBI-3449344, EBI-356553;
CC Q9Y2Y0; Q9Y649; NbExp=3; IntAct=EBI-3449344, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion intermembrane space.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC Nucleus. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton,
CC cilium basal body. Note=The complex formed with ARL2BP, ARL2 and
CC SLC25A4 is expressed in mitochondria (By similarity). Detected in the
CC midbody matrix. Not detected in the Golgi, nucleus and on the mitotic
CC spindle. Centrosome-associated throughout the cell cycle. Not detected
CC to interphase microtubules. In retina photoreceptor cells, localized in
CC the distal connecting cilia, basal body, ciliary-associated centriole,
CC and ciliary rootlet. Interaction with ARL2 may be required for cilia
CC basal body localization. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2Y0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2Y0-2; Sequence=VSP_025317, VSP_025318;
CC -!- TISSUE SPECIFICITY: Expressed in retina pigment epithelial cells (at
CC protein level). Widely expressed. {ECO:0000269|PubMed:10488091,
CC ECO:0000269|PubMed:23849777}.
CC -!- DISEASE: Retinitis pigmentosa 82 with or without situs inversus (RP82)
CC [MIM:615434]: An autosomal recessive disorder characterized by variable
CC association of retinitis pigmentosa with situs inversus. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. Situs inversus is a congenital
CC abnormality in which organs in the thorax and the abdomen are opposite
CC to their normal positions due to lateral transposition.
CC {ECO:0000269|PubMed:23849777, ECO:0000269|PubMed:27790702}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ARL2BP family. {ECO:0000305}.
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DR EMBL; AF126062; AAD20633.1; -; mRNA.
DR EMBL; AK075050; BAG52057.1; -; mRNA.
DR EMBL; CH471092; EAW82913.1; -; Genomic_DNA.
DR EMBL; BC003087; AAH03087.1; -; mRNA.
DR EMBL; BC094878; AAH94878.1; -; mRNA.
DR CCDS; CCDS10776.1; -. [Q9Y2Y0-1]
DR RefSeq; NP_036238.1; NM_012106.3. [Q9Y2Y0-1]
DR PDB; 2K9A; NMR; -; A=1-136.
DR PDB; 3DOE; X-ray; 2.25 A; B=1-163.
DR PDB; 3DOF; X-ray; 3.30 A; B=1-163.
DR PDBsum; 2K9A; -.
DR PDBsum; 3DOE; -.
DR PDBsum; 3DOF; -.
DR AlphaFoldDB; Q9Y2Y0; -.
DR BMRB; Q9Y2Y0; -.
DR SMR; Q9Y2Y0; -.
DR BioGRID; 117110; 35.
DR DIP; DIP-48323N; -.
DR IntAct; Q9Y2Y0; 14.
DR STRING; 9606.ENSP00000219204; -.
DR iPTMnet; Q9Y2Y0; -.
DR PhosphoSitePlus; Q9Y2Y0; -.
DR BioMuta; ARL2BP; -.
DR DMDM; 74735245; -.
DR EPD; Q9Y2Y0; -.
DR jPOST; Q9Y2Y0; -.
DR MassIVE; Q9Y2Y0; -.
DR MaxQB; Q9Y2Y0; -.
DR PaxDb; Q9Y2Y0; -.
DR PeptideAtlas; Q9Y2Y0; -.
DR PRIDE; Q9Y2Y0; -.
DR ProteomicsDB; 85933; -. [Q9Y2Y0-1]
DR ProteomicsDB; 85934; -. [Q9Y2Y0-2]
DR TopDownProteomics; Q9Y2Y0-1; -. [Q9Y2Y0-1]
DR Antibodypedia; 28836; 322 antibodies from 25 providers.
DR DNASU; 23568; -.
DR Ensembl; ENST00000219204.8; ENSP00000219204.3; ENSG00000102931.8. [Q9Y2Y0-1]
DR GeneID; 23568; -.
DR KEGG; hsa:23568; -.
DR MANE-Select; ENST00000219204.8; ENSP00000219204.3; NM_012106.4; NP_036238.1.
DR UCSC; uc002elf.2; human. [Q9Y2Y0-1]
DR CTD; 23568; -.
DR DisGeNET; 23568; -.
DR GeneCards; ARL2BP; -.
DR HGNC; HGNC:17146; ARL2BP.
DR HPA; ENSG00000102931; Low tissue specificity.
DR MalaCards; ARL2BP; -.
DR MIM; 615407; gene.
DR MIM; 615434; phenotype.
DR neXtProt; NX_Q9Y2Y0; -.
DR OpenTargets; ENSG00000102931; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA134904608; -.
DR VEuPathDB; HostDB:ENSG00000102931; -.
DR eggNOG; ENOG502RYJD; Eukaryota.
DR GeneTree; ENSGT00390000015052; -.
DR HOGENOM; CLU_116781_0_0_1; -.
DR InParanoid; Q9Y2Y0; -.
DR OMA; LIQRNFM; -.
DR PhylomeDB; Q9Y2Y0; -.
DR TreeFam; TF315143; -.
DR PathwayCommons; Q9Y2Y0; -.
DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR SignaLink; Q9Y2Y0; -.
DR BioGRID-ORCS; 23568; 18 hits in 1012 CRISPR screens.
DR ChiTaRS; ARL2BP; human.
DR EvolutionaryTrace; Q9Y2Y0; -.
DR GenomeRNAi; 23568; -.
DR Pharos; Q9Y2Y0; Tbio.
DR PRO; PR:Q9Y2Y0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y2Y0; protein.
DR Bgee; ENSG00000102931; Expressed in adrenal tissue and 196 other tissues.
DR ExpressionAtlas; Q9Y2Y0; baseline and differential.
DR Genevisible; Q9Y2Y0; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0030695; F:GTPase regulator activity; TAS:ProtInc.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 1.20.1520.10; -; 1.
DR InterPro; IPR038849; ARL2BP.
DR InterPro; IPR023379; BART_dom.
DR InterPro; IPR042541; BART_sf.
DR PANTHER; PTHR15487; PTHR15487; 1.
DR Pfam; PF11527; ARL2_Bind_BART; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy; Cilium;
KW Cytoplasm; Cytoskeleton; Disease variant; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1..163
FT /note="ADP-ribosylation factor-like protein 2-binding
FT protein"
FT /id="PRO_0000287113"
FT VAR_SEQ 1..11
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025317"
FT VAR_SEQ 12..13
FT /note="SF -> MR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025318"
FT VARIANT 45
FT /note="M -> R (in RP82; drastic decrease ARL2-binding,
FT diffuse cytoplasmic localization, no enrichement at cilia
FT basal body; dbSNP:rs398123053)"
FT /evidence="ECO:0000269|PubMed:23849777"
FT /id="VAR_070227"
FT VARIANT 87
FT /note="E -> K (in dbSNP:rs7198865)"
FT /id="VAR_053904"
FT MUTAGEN 56
FT /note="E->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 57
FT /note="E->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 60
FT /note="L->A: Decreases interaction with ARL2."
FT MUTAGEN 74
FT /note="E->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 76
FT /note="Y->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 109
FT /note="F->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 110
FT /note="D->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 111
FT /note="M->A: Does not decrease interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 112
FT /note="L->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT MUTAGEN 115
FT /note="F->A: Decreases interaction with ARL2."
FT /evidence="ECO:0000269|PubMed:19368893"
FT CONFLICT 27
FT /note="Y -> C (in Ref. 4; AAH94878)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="L -> Q (in Ref. 4; AAH94878)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="I -> T (in Ref. 4; AAH94878)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="Q -> E (in Ref. 4; AAH94878)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="E -> G (in Ref. 4; AAH94878)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="L -> T (in Ref. 4; AAH94878)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:2K9A"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:2K9A"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:3DOE"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 62..84
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:3DOE"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3DOE"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2K9A"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:3DOE"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:3DOE"
SQ SEQUENCE 163 AA; 18822 MW; E35EB5AC73FC1FEC CRC64;
MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL EFEDTEENKL
IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH KDEVAGDIFD MLLTFTDFLA
FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK SSSLPASQNN LRH
