ARC_RAT
ID ARC_RAT Reviewed; 396 AA.
AC Q63053; Q62743;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Activity-regulated cytoskeleton-associated protein {ECO:0000303|PubMed:7857651};
DE AltName: Full=Activity-regulated gene 3.1 protein {ECO:0000250|UniProtKB:Q9WV31};
DE Short=ARC/ARG3.1 {ECO:0000250|UniProtKB:Q9WV31};
DE Short=Arg3.1 {ECO:0000250|UniProtKB:Q9WV31};
GN Name=Arc {ECO:0000303|PubMed:7857651, ECO:0000312|RGD:62037};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC TISSUE=Hippocampus;
RX PubMed=7857651; DOI=10.1016/0896-6273(95)90299-6;
RA Lyford G.L., Yamagata K., Kaufmann W.E., Barnes C.A., Sanders L.K.,
RA Copeland N.G., Gilbert D.J., Jenkins N.A., Lanahan A.A., Worley P.F.;
RT "Arc, a growth factor and activity-regulated gene, encodes a novel
RT cytoskeleton-associated protein that is enriched in neuronal dendrites.";
RL Neuron 14:433-445(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RX PubMed=7777577; DOI=10.1073/pnas.92.12.5734;
RA Link W., Konietzko U., Kauselmann G., Krug M., Schwanke B., Frey U.,
RA Kuhl D.;
RT "Somatodendritic expression of an immediate early gene is regulated by
RT synaptic activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:5734-5738(1995).
RN [3]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=9808461; DOI=10.1016/s0896-6273(00)80591-7;
RA Steward O., Wallace C.S., Lyford G.L., Worley P.F.;
RT "Synaptic activation causes the mRNA for the IEG Arc to localize
RT selectively near activated postsynaptic sites on dendrites.";
RL Neuron 21:741-751(1998).
RN [4]
RP INDUCTION.
RX PubMed=10570490; DOI=10.1038/16046;
RA Guzowski J.F., McNaughton B.L., Barnes C.A., Worley P.F.;
RT "Environment-specific expression of the immediate-early gene Arc in
RT hippocampal neuronal ensembles.";
RL Nat. Neurosci. 2:1120-1124(1999).
RN [5]
RP FUNCTION.
RX PubMed=10818134; DOI=10.1523/jneurosci.20-11-03993.2000;
RA Guzowski J.F., Lyford G.L., Stevenson G.D., Houston F.P., McGaugh J.L.,
RA Worley P.F., Barnes C.A.;
RT "Inhibition of activity-dependent arc protein expression in the rat
RT hippocampus impairs the maintenance of long-term potentiation and the
RT consolidation of long-term memory.";
RL J. Neurosci. 20:3993-4001(2000).
RN [6]
RP INDUCTION.
RX PubMed=11226315; DOI=10.1073/pnas.051623398;
RA Pinkstaff J.K., Chappell S.A., Mauro V.P., Edelman G.M., Krushel L.A.;
RT "Internal initiation of translation of five dendritically localized
RT neuronal mRNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2770-2775(2001).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNM2; SH3GL1 AND
RP SH3GL3.
RX PubMed=17088211; DOI=10.1016/j.neuron.2006.08.033;
RA Chowdhury S., Shepherd J.D., Okuno H., Lyford G., Petralia R.S., Plath N.,
RA Kuhl D., Huganir R.L., Worley P.F.;
RT "Arc/Arg3.1 interacts with the endocytic machinery to regulate AMPA
RT receptor trafficking.";
RL Neuron 52:445-459(2006).
RN [8]
RP FUNCTION.
RX PubMed=17088212; DOI=10.1016/j.neuron.2006.09.031;
RA Rial Verde E.M., Lee-Osbourne J., Worley P.F., Malinow R., Cline H.T.;
RT "Increased expression of the immediate-early gene arc/arg3.1 reduces AMPA
RT receptor-mediated synaptic transmission.";
RL Neuron 52:461-474(2006).
RN [9]
RP FUNCTION.
RX PubMed=17088213; DOI=10.1016/j.neuron.2006.08.034;
RA Shepherd J.D., Rumbaugh G., Wu J., Chowdhury S., Plath N., Kuhl D.,
RA Huganir R.L., Worley P.F.;
RT "Arc/Arg3.1 mediates homeostatic synaptic scaling of AMPA Receptors.";
RL Neuron 52:475-484(2006).
RN [10]
RP INDUCTION.
RX PubMed=18614031; DOI=10.1016/j.neuron.2008.05.014;
RA Waung M.W., Pfeiffer B.E., Nosyreva E.D., Ronesi J.A., Huber K.M.;
RT "Rapid translation of Arc/Arg3.1 selectively mediates mGluR-dependent LTD
RT through persistent increases in AMPAR endocytosis rate.";
RL Neuron 59:84-97(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAMK2B.
RX PubMed=22579289; DOI=10.1016/j.cell.2012.02.062;
RA Okuno H., Akashi K., Ishii Y., Yagishita-Kyo N., Suzuki K., Nonaka M.,
RA Kawashima T., Fujii H., Takemoto-Kimura S., Abe M., Natsume R.,
RA Chowdhury S., Sakimura K., Worley P.F., Bito H.;
RT "Inverse synaptic tagging of inactive synapses via dynamic interaction of
RT Arc/Arg3.1 with CaMKIIbeta.";
RL Cell 149:886-898(2012).
RN [12]
RP FUNCTION.
RX PubMed=23791196; DOI=10.1016/j.neuron.2013.04.036;
RA Mikuni T., Uesaka N., Okuno H., Hirai H., Deisseroth K., Bito H., Kano M.;
RT "Arc/Arg3.1 is a postsynaptic mediator of activity-dependent synapse
RT elimination in the developing cerebellum.";
RL Neuron 78:1024-1035(2013).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND RNA-BINDING.
RX PubMed=29328916; DOI=10.1016/j.cell.2017.12.024;
RA Pastuzyn E.D., Day C.E., Kearns R.B., Kyrke-Smith M., Taibi A.V.,
RA McCormick J., Yoder N., Belnap D.M., Erlendsson S., Morado D.R.,
RA Briggs J.A.G., Feschotte C., Shepherd J.D.;
RT "The neuronal gene Arc encodes a repurposed retrotransposon Gag protein
RT that mediates intercellular RNA transfer.";
RL Cell 172:275-288(2018).
RN [14]
RP SUBUNIT.
RX PubMed=30028513; DOI=10.1111/jnc.14556;
RA Hallin E.I., Eriksen M.S., Baryshnikov S., Nikolaienko O., Groedem S.,
RA Hosokawa T., Hayashi Y., Bramham C.R., Kursula P.;
RT "Structure of monomeric full-length ARC sheds light on molecular
RT flexibility, protein interactions, and functional modalities.";
RL J. Neurochem. 147:323-343(2018).
RN [15] {ECO:0007744|PDB:4X3H, ECO:0007744|PDB:4X3I, ECO:0007744|PDB:4X3X}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 207-277, AND DOMAIN.
RX PubMed=25864631; DOI=10.1016/j.neuron.2015.03.030;
RA Zhang W., Wu J., Ward M.D., Yang S., Chuang Y.A., Xiao M., Li R.,
RA Leahy D.J., Worley P.F.;
RT "Structural basis of arc binding to synaptic proteins: implications for
RT cognitive disease.";
RL Neuron 86:490-500(2015).
RN [16]
RP STRUCTURE BY NMR OF 206-364, SUBUNIT, AND INTERACTION WITH GRIN2A AND
RP GRIN2B.
RX PubMed=31080121; DOI=10.1016/j.str.2019.04.001;
RA Nielsen L.D., Pedersen C.P., Erlendsson S., Teilum K.;
RT "The capsid domain of Arc changes its oligomerization propensity through
RT direct interaction with the NMDA receptor.";
RL Structure 0:0-0(2019).
CC -!- FUNCTION: Master regulator of synaptic plasticity that self-assembles
CC into virion-like capsids that encapsulate RNAs and mediate
CC intercellular RNA transfer in the nervous system (PubMed:29328916). ARC
CC protein is released from neurons in extracellular vesicles that mediate
CC the transfer of ARC mRNA into new target cells, where ARC mRNA can
CC undergo activity-dependent translation (PubMed:29328916). ARC capsids
CC are endocytosed and are able to transfer ARC mRNA into the cytoplasm of
CC neurons (PubMed:29328916). Acts as a key regulator of synaptic
CC plasticity: required for protein synthesis-dependent forms of long-term
CC potentiation (LTP) and depression (LTD) and for the formation of long-
CC term memory (PubMed:10818134, PubMed:17088211, PubMed:17088212,
CC PubMed:17088213). Regulates synaptic plasticity by promoting
CC endocytosis of AMPA receptors (AMPARs) in response to synaptic
CC activity: this endocytic pathway maintains levels of surface AMPARs in
CC response to chronic changes in neuronal activity through synaptic
CC scaling, thereby contributing to neuronal homeostasis (PubMed:17088211,
CC PubMed:17088212). Acts as a postsynaptic mediator of activity-dependent
CC synapse elimination in the developing cerebellum by mediating
CC elimination of surplus climbing fiber synapses (PubMed:23791196).
CC Accumulates at weaker synapses, probably to prevent their undesired
CC enhancement (PubMed:22579289). This suggests that ARC-containing
CC virion-like capsids may be required to eliminate synaptic material
CC (PubMed:29328916). Required to transduce experience into long-lasting
CC changes in visual cortex plasticity and for long-term memory
CC (PubMed:10818134). Involved in postsynaptic trafficking and processing
CC of amyloid-beta A4 (APP) via interaction with PSEN1 (By similarity). In
CC addition to its role in synapses, also involved in the regulation of
CC the immune system: specifically expressed in skin-migratory dendritic
CC cells and regulates fast dendritic cell migration, thereby regulating
CC T-cell activation (By similarity). {ECO:0000250|UniProtKB:Q9WV31,
CC ECO:0000269|PubMed:10818134, ECO:0000269|PubMed:17088211,
CC ECO:0000269|PubMed:17088212, ECO:0000269|PubMed:17088213,
CC ECO:0000269|PubMed:22579289, ECO:0000269|PubMed:23791196,
CC ECO:0000269|PubMed:29328916}.
CC -!- SUBUNIT: Homooligomer; homooligomerizes into virion-like capsids
CC (PubMed:29328916, PubMed:30028513, PubMed:31080121). Interacts with
CC SH3GL1/endophilin-2, SH3GL3/endophilin-3 and DNM2/DYN2
CC (PubMed:17088211). Interacts with CAMK2B (in the kinase inactive
CC state); leading to target ARC to inactive synapses (PubMed:22579289).
CC Interacts with PSEN1 (By similarity). Interacts with GRIN2A and GRIN2B;
CC inhibiting homooligomerization (PubMed:31080121).
CC {ECO:0000250|UniProtKB:Q9WV31, ECO:0000269|PubMed:17088211,
CC ECO:0000269|PubMed:22579289, ECO:0000269|PubMed:29328916,
CC ECO:0000269|PubMed:30028513, ECO:0000269|PubMed:31080121}.
CC -!- INTERACTION:
CC Q63053; P08413: Camk2b; NbExp=6; IntAct=EBI-5275794, EBI-916155;
CC Q63053; PRO_0000025591 [P49768]: PSEN1; Xeno; NbExp=3; IntAct=EBI-5275794, EBI-2606326;
CC -!- SUBCELLULAR LOCATION: Extracellular vesicle membrane
CC {ECO:0000269|PubMed:29328916}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9WV31}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9WV31}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9WV31}. Synapse {ECO:0000269|PubMed:17088211,
CC ECO:0000269|PubMed:22579289}. Postsynaptic density
CC {ECO:0000269|PubMed:17088211}. Early endosome membrane
CC {ECO:0000269|PubMed:17088211}. Cell projection, dendrite
CC {ECO:0000269|PubMed:7857651, ECO:0000269|PubMed:9808461}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:7857651}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:7857651}. Cell projection, dendritic spine
CC {ECO:0000269|PubMed:17088211}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:Q9WV31}. Note=Forms virion-like
CC extracellular vesicles that are released from neurons
CC (PubMed:29328916). Enriched in postsynaptic density of dendritic spines
CC (PubMed:17088211). Targeted to inactive synapses following interaction
CC with CAMK2B in the kinase inactive state (PubMed:22579289).
CC Accumulation at weaker synapses may be required to prevent their
CC undesired enhancement (PubMed:22579289). Associated with the cell
CC cortex of neuronal soma and dendrites (PubMed:7857651). Associated with
CC the sperm tail (By similarity). {ECO:0000250|UniProtKB:Q9WV31,
CC ECO:0000269|PubMed:17088211, ECO:0000269|PubMed:22579289,
CC ECO:0000269|PubMed:29328916, ECO:0000269|PubMed:7777577,
CC ECO:0000269|PubMed:7857651}.
CC -!- TISSUE SPECIFICITY: Expressed exclusively in certain parts of the brain
CC including cortex and molecular layer of the hippocampus. Typically
CC expressed at high level in a minority of neurons. Basal expression
CC higher in cortex than in hippocampus, highest in visual cortex.
CC {ECO:0000269|PubMed:7777577, ECO:0000269|PubMed:7857651}.
CC -!- DEVELOPMENTAL STAGE: Expressed during postnatal development from day 8
CC (PubMed:7857651). Highest expression around day 23 with moderate levels
CC expressed to adulthood (PubMed:7857651). {ECO:0000269|PubMed:7857651}.
CC -!- INDUCTION: Arc expression is regulated at transcription, post-
CC transcription and translation levels (PubMed:9808461, PubMed:10570490,
CC PubMed:11226315, PubMed:18614031). Transcription is tightly coupled to
CC encoding of information in neuronal circuits (PubMed:10570490).
CC Expression is induced by neuronal and synaptic activity
CC (PubMed:7777577, PubMed:7857651, PubMed:10570490). Induced at highest
CC level in hippocampus within 30 minutes, dropping to basal levels within
CC 24 hours (PubMed:7777577, PubMed:7857651). Arc transcripts are
CC transported to dendrites and become enriched at sites of local synaptic
CC activity where they are locally translated into protein
CC (PubMed:9808461, PubMed:18614031). Arc transcripts resemble some viral
CC RNAs and contain an internal ribosomal entry site (IRES) that allows
CC cap-independent translation (PubMed:11226315).
CC {ECO:0000269|PubMed:10570490, ECO:0000269|PubMed:11226315,
CC ECO:0000269|PubMed:18614031, ECO:0000269|PubMed:7777577,
CC ECO:0000269|PubMed:7857651, ECO:0000269|PubMed:9808461}.
CC -!- DOMAIN: The protein is evolutionarily related to retrotransposon Gag
CC proteins: it contains large N- and C-terminal domains that form a bi-
CC lobar architecture similar to the capsid domain of human
CC immunodeficiency virus (HIV) gag protein (PubMed:29328916,
CC PubMed:25864631). It contains structural elements found within viral
CC Gag polyproteins originated from the Ty3/gypsy retrotransposon family
CC and retains the ability to form virion-like capsid structures that can
CC mediate mRNA transfer between cells (PubMed:29328916). Tetrapod and fly
CC Arc protein-coding genes originated independently from distinct
CC lineages of Ty3/gypsy retrotransposons (PubMed:29328916).
CC {ECO:0000269|PubMed:25864631, ECO:0000269|PubMed:29328916}.
CC -!- PTM: Palmitoylation anchors the protein into the membrane by allowing
CC direct insertion into the hydrophobic core of the lipid bilayer.
CC {ECO:0000250|UniProtKB:Q9WV31}.
CC -!- PTM: Ubiquitinated by UBE3A, leading to its degradation by the
CC proteasome, thereby promoting AMPA receptors (AMPARs) expression at
CC synapses. {ECO:0000250|UniProtKB:Q9WV31}.
CC -!- PTM: Phosphorylation at Ser-260 by CaMK2 prevents homooligomerization
CC into virion-like capsids by disrupting an interaction surface essential
CC for high-order oligomerization. Phosphorylation by CaMK2 inhibits
CC synaptic activity. {ECO:0000250|UniProtKB:Q9WV31}.
CC -!- MISCELLANEOUS: Transcripts enriched in dendrites may be translated
CC locally. {ECO:0000269|PubMed:7777577}.
CC -!- SIMILARITY: Belongs to the ARC/ARG3.1 family. {ECO:0000305}.
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DR EMBL; U19866; AAA68695.1; -; mRNA.
DR EMBL; Z46925; CAA87033.1; -; mRNA.
DR PIR; I58168; I58168.
DR RefSeq; NP_062234.1; NM_019361.1.
DR RefSeq; XP_017450553.1; XM_017595064.1.
DR PDB; 4X3H; X-ray; 2.40 A; A=207-277.
DR PDB; 4X3I; X-ray; 1.80 A; A=207-277.
DR PDB; 4X3X; X-ray; 2.00 A; A=278-362.
DR PDB; 6GSE; NMR; -; A=206-364.
DR PDBsum; 4X3H; -.
DR PDBsum; 4X3I; -.
DR PDBsum; 4X3X; -.
DR PDBsum; 6GSE; -.
DR AlphaFoldDB; Q63053; -.
DR SMR; Q63053; -.
DR BioGRID; 248539; 8.
DR IntAct; Q63053; 6.
DR STRING; 10116.ENSRNOP00000063719; -.
DR iPTMnet; Q63053; -.
DR PhosphoSitePlus; Q63053; -.
DR PaxDb; Q63053; -.
DR Ensembl; ENSRNOT00000076998; ENSRNOP00000068090; ENSRNOG00000043465.
DR GeneID; 54323; -.
DR KEGG; rno:54323; -.
DR UCSC; RGD:62037; rat.
DR CTD; 23237; -.
DR RGD; 62037; Arc.
DR eggNOG; ENOG502QSPT; Eukaryota.
DR GeneTree; ENSGT00390000003914; -.
DR HOGENOM; CLU_782004_0_0_1; -.
DR InParanoid; Q63053; -.
DR OMA; AKKWWEY; -.
DR OrthoDB; 904267at2759; -.
DR PhylomeDB; Q63053; -.
DR TreeFam; TF335604; -.
DR PRO; PR:Q63053; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000043465; Expressed in frontal cortex and 16 other tissues.
DR Genevisible; Q63053; RN.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:RGD.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1903561; C:extracellular vesicle; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0071598; C:neuronal ribonucleoprotein granule; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098845; C:postsynaptic endosome; IDA:SynGO.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007492; P:endoderm development; ISO:RGD.
DR GO; GO:0007612; P:learning; IEP:RGD.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0051028; P:mRNA transport; IDA:UniProtKB.
DR GO; GO:2000969; P:positive regulation of AMPA receptor activity; IMP:CACAO.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IGI:ARUK-UCL.
DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:1900271; P:regulation of long-term synaptic potentiation; IMP:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEP:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:RGD.
DR GO; GO:0110077; P:vesicle-mediated intercellular transport; IDA:UniProtKB.
DR InterPro; IPR023263; Arc.
DR InterPro; IPR040814; Arc_C.
DR InterPro; IPR045557; Arc_N.
DR PANTHER; PTHR15962; PTHR15962; 1.
DR Pfam; PF18162; Arc_C; 1.
DR Pfam; PF19284; Arc_MA; 1.
DR PRINTS; PR02027; ARCARG31.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Developmental protein; Endocytosis;
KW Endosome; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; RNA-binding; Synapse;
KW Transport; Ubl conjugation.
FT CHAIN 1..396
FT /note="Activity-regulated cytoskeleton-associated protein"
FT /id="PRO_0000273287"
FT REGION 89..100
FT /note="Interaction with SH3GL1 or SH3GL3"
FT /evidence="ECO:0000269|PubMed:17088211"
FT REGION 195..214
FT /note="Interaction with DNM2"
FT /evidence="ECO:0000269|PubMed:17088211"
FT REGION 358..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..78
FT /evidence="ECO:0000255"
FT COMPBIAS 378..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV31"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV31"
FT CONFLICT 209
FT /note="V -> L (in Ref. 1; AAA68695)"
FT /evidence="ECO:0000305"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:4X3I"
FT STRAND 211..216
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 217..231
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 264..276
FT /evidence="ECO:0007829|PDB:4X3I"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:4X3X"
FT HELIX 298..312
FT /evidence="ECO:0007829|PDB:4X3X"
FT HELIX 318..327
FT /evidence="ECO:0007829|PDB:4X3X"
FT HELIX 331..337
FT /evidence="ECO:0007829|PDB:4X3X"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:4X3X"
FT HELIX 345..359
FT /evidence="ECO:0007829|PDB:4X3X"
SQ SEQUENCE 396 AA; 45353 MW; 4E95B46B75853CA5 CRC64;
MELDHMTTGG LHAYPAPRGG PAAKPNVILQ IGKCRAEMLE HVRRTHRHLL TEVSKQVERE
LKGLHRSVGK LENNLDGYVP TGDSQRWKKS IKACLCRCQE TIANLERWVK REMHVWREVF
YRLERWADRL ESMGGKYPVG SEPARHTVSV GVGGPEPYCQ EADGYDYTVS PYAITPPPAA
GELPEQESVG AQQYQSWVPG EDGQPSPGVD TQIFEDPREF LSHLEEYLRQ VGGSEEYWLS
QIQNHMNGPA KKWWEFKQGS VKNWVEFKKE FLQYSEGTLS REAIQRELDL PQKQGEPLDQ
FLWRKRDLYQ TLYVDAEEEE IIQYVVGTLQ PKFKRFLRHP LPKTLEQLIQ RGMEVQDGLE
QAAEPSVTPL PTEDETEALT PALTSESVAS DRTQPE
