ARF1_MOUSE
ID ARF1_MOUSE Reviewed; 181 AA.
AC P84078; P10947; P32889; Q3THZ2; Q3U849; Q3UDG1; Q3UF76;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=ADP-ribosylation factor 1;
GN Name=Arf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=8947846; DOI=10.1093/oxfordjournals.jbchem.a021484;
RA Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT "Structure and intracellular localization of mouse ADP-ribosylation factors
RT type 1 to type 6 (ARF1-ARF6).";
RL J. Biochem. 120:813-819(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Bone marrow, Heart, Kidney, Pancreas, Placenta, and
RC Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 PROTEIN SEQUENCE OF 20-30; 39-73; 80-97 AND 110-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP FUNCTION, INTERACTION WITH GGA1; GGA2 AND GGA3, AND SUBCELLULAR LOCATION.
RX PubMed=11950392; DOI=10.1042/bj20020428;
RA Takatsu H., Yoshino K., Toda K., Nakayama K.;
RT "GGA proteins associate with Golgi membranes through interaction between
RT their GGAH domains and ADP-ribosylation factors.";
RL Biochem. J. 365:369-378(2002).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH C9ORF72.
RX PubMed=27723745; DOI=10.1038/nn.4407;
RA Sivadasan R., Hornburg D., Drepper C., Frank N., Jablonka S., Hansel A.,
RA Lojewski X., Sterneckert J., Hermann A., Shaw P.J., Ince P.G., Mann M.,
RA Meissner F., Sendtner M.;
RT "C9ORF72 interaction with cofilin modulates actin dynamics in motor
RT neurons.";
RL Nat. Neurosci. 19:1610-1618(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 19-182 IN COMPLEX WITH GTP AND
RP GGA1.
RX PubMed=12679809; DOI=10.1038/nsb920;
RA Shiba T., Kawasaki M., Takatsu H., Nogi T., Matsugaki N., Igarashi N.,
RA Suzuki M., Kato R., Nakayama K., Wakatsuki S.;
RT "Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal
RT protein transport.";
RL Nat. Struct. Biol. 10:386-393(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 18-180 IN COMPLEX WITH ARHGAP21.
RX PubMed=17347647; DOI=10.1038/sj.emboj.7601634;
RA Menetrey J., Perderiset M., Cicolari J., Dubois T., Elkhatib N.,
RA El Khadali F., Franco M., Chavrier P., Houdusse A.;
RT "Structural basis for ARF1-mediated recruitment of ARHGAP21 to Golgi
RT membranes.";
RL EMBO J. 26:1953-1962(2007).
CC -!- FUNCTION: GTP-binding protein involved in protein trafficking among
CC different compartments (PubMed:11950392). Modulates vesicle budding and
CC uncoating within the Golgi complex. Deactivation induces the
CC redistribution of the entire Golgi complex to the endoplasmic
CC reticulum, suggesting a crucial role in protein trafficking. In its
CC GTP-bound form, its triggers the association with coat proteins with
CC the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated
CC by ARFGAPs proteins, is required for dissociation of coat proteins from
CC Golgi membranes and vesicles. The GTP-bound form interacts with PICK1
CC to limit PICK1-mediated inhibition of Arp2/3 complex activity; the
CC function is linked to AMPA receptor (AMPAR) trafficking, regulation of
CC synaptic plasicity of excitatory synapses and spine shrinkage during
CC long-term depression (LTD). {ECO:0000269|PubMed:11950392}.
CC -!- SUBUNIT: Interacts (when activated) with GGA1, GGA2 and GGA3; the
CC interaction is required for proper subcellular location of GGA1, GGA2
CC and GGA3 (PubMed:11950392, PubMed:12679809). Interacts with ARHGAP21,
CC ASAP2, HERC1, PRKCABP, PIP5K1B, TMED2, PSCD2, TMED10 and GRIA2
CC (PubMed:17347647). Interacts with ARFGAP1, which hydrolyzes GTP and
CC thus, regulates its function. Interacts with PI4KB in the Golgi
CC complex. Interacts with NCS1/FREQ in the Golgi and at the plasma
CC membrane. Interacts with PLEKHA3. Interacts with PLEKHA8; the
CC interaction, together with phosphatidylinositol 4-phosphate binding, is
CC required for FAPP2-mediated glucosylceramide transfer activity.
CC Interacts (activated) with PICK1 (via PDZ domain); the interaction
CC blocks Arp2/3 complex inhibition. Interacts with IQSEC1 (By
CC similarity). Interacts with C9orf72 (PubMed:27723745) (By similarity).
CC {ECO:0000250|UniProtKB:P84077, ECO:0000250|UniProtKB:P84079,
CC ECO:0000250|UniProtKB:P84080, ECO:0000269|PubMed:11950392,
CC ECO:0000269|PubMed:12679809, ECO:0000269|PubMed:17347647,
CC ECO:0000269|PubMed:27723745}.
CC -!- INTERACTION:
CC P84078; Q5T5U3: ARHGAP21; Xeno; NbExp=3; IntAct=EBI-2308190, EBI-1642518;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, perinuclear region
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Postsynaptic density
CC {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P84077}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P84077}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:11950392}; Lipid-anchor {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC {ECO:0000305}.
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DR EMBL; D87898; BAA13490.1; -; mRNA.
DR EMBL; AK148458; BAE28566.1; -; mRNA.
DR EMBL; AK148873; BAE28685.1; -; mRNA.
DR EMBL; AK150092; BAE29300.1; -; mRNA.
DR EMBL; AK150699; BAE29778.1; -; mRNA.
DR EMBL; AK151223; BAE30215.1; -; mRNA.
DR EMBL; AK151225; BAE30217.1; -; mRNA.
DR EMBL; AK151696; BAE30620.1; -; mRNA.
DR EMBL; AK151821; BAE30718.1; -; mRNA.
DR EMBL; AK152015; BAE30877.1; -; mRNA.
DR EMBL; AK152382; BAE31170.1; -; mRNA.
DR EMBL; AK152479; BAE31253.1; -; mRNA.
DR EMBL; AK153132; BAE31745.1; -; mRNA.
DR EMBL; AK159174; BAE34874.1; -; mRNA.
DR EMBL; AK167000; BAE39179.1; -; mRNA.
DR EMBL; AK167129; BAE39276.1; -; mRNA.
DR EMBL; AK167543; BAE39610.1; -; mRNA.
DR EMBL; AK167931; BAE39935.1; -; mRNA.
DR EMBL; AK168081; BAE40054.1; -; mRNA.
DR EMBL; AK168686; BAE40532.1; -; mRNA.
DR EMBL; AK169166; BAE40945.1; -; mRNA.
DR EMBL; AK170586; BAE41895.1; -; mRNA.
DR EMBL; AL645854; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031986; AAH31986.1; -; mRNA.
DR CCDS; CCDS24765.1; -.
DR PIR; JC4945; JC4945.
DR RefSeq; NP_001123880.1; NM_001130408.1.
DR RefSeq; NP_031502.1; NM_007476.3.
DR PDB; 1O3Y; X-ray; 1.50 A; A/B=18-181.
DR PDB; 2J59; X-ray; 2.10 A; A/B/C/D/E/F=18-181.
DR PDBsum; 1O3Y; -.
DR PDBsum; 2J59; -.
DR AlphaFoldDB; P84078; -.
DR BMRB; P84078; -.
DR SMR; P84078; -.
DR BioGRID; 198184; 27.
DR CORUM; P84078; -.
DR IntAct; P84078; 7.
DR MINT; P84078; -.
DR STRING; 10090.ENSMUSP00000079905; -.
DR ChEMBL; CHEMBL1075273; -.
DR iPTMnet; P84078; -.
DR PhosphoSitePlus; P84078; -.
DR SwissPalm; P84078; -.
DR EPD; P84078; -.
DR jPOST; P84078; -.
DR MaxQB; P84078; -.
DR PaxDb; P84078; -.
DR PeptideAtlas; P84078; -.
DR PRIDE; P84078; -.
DR ProteomicsDB; 282011; -.
DR TopDownProteomics; P84078; -.
DR Antibodypedia; 3569; 584 antibodies from 38 providers.
DR DNASU; 11840; -.
DR Ensembl; ENSMUST00000061242; ENSMUSP00000079905; ENSMUSG00000048076.
DR Ensembl; ENSMUST00000163300; ENSMUSP00000126120; ENSMUSG00000048076.
DR GeneID; 11840; -.
DR KEGG; mmu:11840; -.
DR UCSC; uc007jdm.2; mouse.
DR CTD; 375; -.
DR MGI; MGI:99431; Arf1.
DR VEuPathDB; HostDB:ENSMUSG00000048076; -.
DR eggNOG; KOG0070; Eukaryota.
DR GeneTree; ENSGT00950000183080; -.
DR HOGENOM; CLU_040729_9_3_1; -.
DR InParanoid; P84078; -.
DR OMA; VEYRNIQ; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P84078; -.
DR TreeFam; TF300808; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-MMU-1660514; Synthesis of PIPs at the Golgi membrane.
DR Reactome; R-MMU-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR BioGRID-ORCS; 11840; 18 hits in 79 CRISPR screens.
DR ChiTaRS; Arf1; mouse.
DR EvolutionaryTrace; P84078; -.
DR PRO; PR:P84078; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P84078; protein.
DR Bgee; ENSMUSG00000048076; Expressed in animal zygote and 81 other tissues.
DR Genevisible; P84078; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0030137; C:COPI-coated vesicle; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0012505; C:endomembrane system; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0019003; F:GDP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IMP:CAFA.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
DR GO; GO:1990583; F:phospholipase D activator activity; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IEA:Ensembl.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0097061; P:dendritic spine organization; ISS:UniProtKB.
DR GO; GO:0055108; P:Golgi to transport vesicle transport; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0060292; P:long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0097212; P:lysosomal membrane organization; ISO:MGI.
DR GO; GO:1990386; P:mitotic cleavage furrow ingression; IGI:UniProtKB.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISO:MGI.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:1902824; P:positive regulation of late endosome to lysosome transport; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0015031; P:protein transport; TAS:MGI.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:1903725; P:regulation of phospholipid metabolic process; ISO:MGI.
DR GO; GO:0002090; P:regulation of receptor internalization; ISS:UniProtKB.
DR GO; GO:0070142; P:synaptic vesicle budding; ISO:MGI.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; ISO:MGI.
DR GO; GO:0016192; P:vesicle-mediated transport; IDA:MGI.
DR CDD; cd04150; Arf1_5_like; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045872; Arf1-5-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Protein transport; Reference proteome;
KW Synapse; Synaptosome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P84077"
FT CHAIN 2..181
FT /note="ADP-ribosylation factor 1"
FT /id="PRO_0000207380"
FT BINDING 24..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12679809,
FT ECO:0007744|PDB:1O3Y, ECO:0007744|PDB:2J59"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:12679809,
FT ECO:0007744|PDB:1O3Y, ECO:0007744|PDB:2J59"
FT BINDING 160
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:1O3Y, ECO:0007744|PDB:2J59"
FT MOD_RES 2
FT /note="N-acetylglycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84077"
FT LIPID 2
FT /note="N-myristoyl glycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P84077"
FT CONFLICT 168
FT /note="E -> K (in Ref. 2; BAE31170)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> C (in Ref. 2; BAE28685)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="Q -> R (in Ref. 2; BAE40054)"
FT /evidence="ECO:0000305"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:1O3Y"
FT STRAND 49..58
FT /evidence="ECO:0007829|PDB:1O3Y"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1O3Y"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1O3Y"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1O3Y"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1O3Y"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1O3Y"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:1O3Y"
SQ SEQUENCE 181 AA; 20697 MW; AAC773D4A60186B6 CRC64;
MGNIFANLFK GLFGKKEMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
ISFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERV NEAREELMRM LAEDELRDAV
LLVFANKQDL PNAMNAAEIT DKLGLHSLRH RNWYIQATCA TSGDGLYEGL DWLSNQLRNQ
K
