NCS1_RAT
ID NCS1_RAT Reviewed; 190 AA.
AC P62168; P36610; Q9UK26;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Neuronal calcium sensor 1;
DE Short=NCS-1;
DE AltName: Full=Frequenin homolog;
DE AltName: Full=Frequenin-like protein;
DE AltName: Full=Frequenin-like ubiquitous protein;
GN Name=Ncs1; Synonyms=Flup, Freq;
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].
RX PubMed=7488079; DOI=10.1006/bbrc.1995.2601;
RA de Castro E., Nef S., Fiumelli H., Lenz S.E., Kawamura S., Nef P.;
RT "Regulation of rhodopsin phosphorylation by a family of neuronal calcium
RT sensors.";
RL Biochem. Biophys. Res. Commun. 216:133-140(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Lindemeier J.;
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP MYRISTOYLATION AT GLY-2, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=10514519; DOI=10.1074/jbc.274.42.30258;
RA McFerran B.W., Weiss J.L., Burgoyne R.D.;
RT "Neuronal Ca(2+) sensor 1. Characterization of the myristoylated protein,
RT its cellular effects in permeabilized adrenal chromaffin cells, Ca(2+)-
RT independent membrane association, and interaction with binding proteins,
RT suggesting a role in rapid Ca(2+) signal transduction.";
RL J. Biol. Chem. 274:30258-30265(1999).
RN [4]
RP INTERACTION WITH PI4KB, AND SUBCELLULAR LOCATION.
RX PubMed=11526106; DOI=10.1074/jbc.m104048200;
RA Zhao X., Varnai P., Tuymetova G., Balla A., Toth Z.E., Oker-Blom C.,
RA Roder J., Jeromin A., Balla T.;
RT "Interaction of neuronal calcium sensor-1 (NCS-1) with phosphatidylinositol
RT 4-kinase beta stimulates lipid kinase activity and affects membrane
RT trafficking in COS-7 cells.";
RL J. Biol. Chem. 276:40183-40189(2001).
RN [5]
RP FUNCTION.
RX PubMed=17502602; DOI=10.1073/pnas.0701133104;
RA Gambino F., Pavlowsky A., Begle A., Dupont J.-L., Bahi N., Courjaret R.,
RA Gardette R., Hadjkacem H., Skala H., Poulain B., Chelly J., Vitale N.,
RA Humeau Y.;
RT "IL1-receptor accessory protein-like 1 (IL1RAPL1), a protein involved in
RT cognitive functions, regulates N-type Ca2+-channel and neurite
RT elongation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:9063-9068(2007).
RN [6]
RP MUTAGENESIS OF ASP-73; GLU-84; ASP-109 AND GLU-120, CALCIUM-BINDING, AND
RP MAGNESIUM-BINDING.
RX PubMed=18199453; DOI=10.1016/j.jmb.2007.12.033;
RA Aravind P., Chandra K., Reddy P.P., Jeromin A., Chary K.V.R., Sharma Y.;
RT "Regulatory and structural EF-hand motifs of neuronal calcium sensor-1: Mg
RT 2+ modulates Ca 2+ binding, Ca 2+ -induced conformational changes, and
RT equilibrium unfolding transitions.";
RL J. Mol. Biol. 376:1100-1115(2008).
RN [7]
RP INTERACTION WITH PICK1.
RX PubMed=19109914; DOI=10.1016/j.neuron.2008.10.050;
RA Jo J., Heon S., Kim M.J., Son G.H., Park Y., Henley J.M., Weiss J.L.,
RA Sheng M., Collingridge G.L., Cho K.;
RT "Metabotropic glutamate receptor-mediated LTD involves two interacting
RT Ca(2+) sensors, NCS-1 and PICK1.";
RL Neuron 60:1095-1111(2008).
RN [8] {ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ, ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH CALCIUM; DRD2 AND
RP RK, AND SUBUNIT.
RX PubMed=25979333; DOI=10.1074/jbc.m114.627059;
RA Pandalaneni S., Karuppiah V., Saleem M., Haynes L.P., Burgoyne R.D.,
RA Mayans O., Derrick J.P., Lian L.Y.;
RT "Neuronal Calcium Sensor-1 Binds the D2 Dopamine Receptor and G-protein-
RT coupled Receptor Kinase 1 (GRK1) Peptides Using Different Modes of
RT Interactions.";
RL J. Biol. Chem. 290:18744-18756(2015).
CC -!- FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled
CC receptor phosphorylation in a calcium dependent manner. Directly
CC regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for
CC calmodulin. Stimulates PI4KB kinase activity. Involved in long-term
CC synaptic plasticity through its interaction with PICK1. May also play a
CC role in neuron differentiation through inhibition of the activity of N-
CC type voltage-gated calcium channel. {ECO:0000269|PubMed:17502602}.
CC -!- SUBUNIT: Monomer (PubMed:25979333). Interacts with KCND2 (By
CC similarity). Interacts in a calcium-independent manner with PI4KB, but
CC only if myristoylated (PubMed:11526106). This binding competes with
CC CALN2/CABP7 binding to PI4KB (PubMed:11526106). Interacts in a calcium-
CC dependent manner with PICK1 (via AH domain) (PubMed:19109914).
CC Interacts with ARF1, ARF3, ARF5 and ARF6 (By similarity). Interacts
CC with IL1RAPL1 (By similarity). {ECO:0000250|UniProtKB:P62166,
CC ECO:0000269|PubMed:11526106, ECO:0000269|PubMed:19109914,
CC ECO:0000269|PubMed:25979333}.
CC -!- INTERACTION:
CC P62168; P84080: ARF1; Xeno; NbExp=2; IntAct=EBI-907774, EBI-449051;
CC P62168; P14100: PDE1A; Xeno; NbExp=2; IntAct=EBI-907774, EBI-907809;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11526106}.
CC Postsynaptic density {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:P62166}. Cytoplasm
CC {ECO:0000269|PubMed:11526106}. Cell membrane
CC {ECO:0000269|PubMed:11526106}. Membrane {ECO:0000250|UniProtKB:P62166,
CC ECO:0000269|PubMed:10514519}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P62166}. Note=Associated with Golgi stacks.
CC Post-synaptic densities of dendrites, and in the pre-synaptic nerve
CC terminal at neuromuscular junctions. {ECO:0000250|UniProtKB:P62166,
CC ECO:0000269|PubMed:11526106, ECO:0000305}.
CC -!- DOMAIN: Binds 3 calcium ions via the second, third and fourth EF-hand.
CC EF-2 and EF-3 bind both magnesium and calcium, while EF-4 binds only
CC calcium. At the resting state, magnesium is bound to EF-2 and EF-3 and
CC upon activation, both sites bind calcium simultaneously while EF-4 is
CC the last one to be occupied.
CC -!- MISCELLANEOUS: Fourfold reduction in calcium affinity for NCS1/FREQ in
CC the presence of magnesium.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; L27421; AAA88510.1; -; mRNA.
DR EMBL; X82188; CAA57678.1; -; mRNA.
DR RefSeq; NP_077342.1; NM_024366.1.
DR PDB; 4OV2; X-ray; 2.60 A; A/B/C/D=1-177.
DR PDB; 4YRU; X-ray; 2.80 A; A/B/C/D=1-177.
DR PDB; 5AEQ; X-ray; 1.95 A; A/B=1-190.
DR PDB; 5AER; X-ray; 2.19 A; A=1-190.
DR PDB; 5AFP; X-ray; 2.30 A; A/B=1-190.
DR PDBsum; 4OV2; -.
DR PDBsum; 4YRU; -.
DR PDBsum; 5AEQ; -.
DR PDBsum; 5AER; -.
DR PDBsum; 5AFP; -.
DR AlphaFoldDB; P62168; -.
DR BMRB; P62168; -.
DR SMR; P62168; -.
DR IntAct; P62168; 7.
DR STRING; 10116.ENSRNOP00000011648; -.
DR iPTMnet; P62168; -.
DR jPOST; P62168; -.
DR PaxDb; P62168; -.
DR PRIDE; P62168; -.
DR Ensembl; ENSRNOT00000111270; ENSRNOP00000091251; ENSRNOG00000064701.
DR GeneID; 65153; -.
DR KEGG; rno:65153; -.
DR UCSC; RGD:68417; rat.
DR CTD; 23413; -.
DR RGD; 68417; Ncs1.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000163010; -.
DR HOGENOM; CLU_072366_1_2_1; -.
DR InParanoid; P62168; -.
DR OMA; EYVFNVF; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P62168; -.
DR TreeFam; TF300009; -.
DR PRO; PR:P62168; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008761; Expressed in frontal cortex and 17 other tissues.
DR Genevisible; P62168; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0008048; F:calcium sensitive guanylate cyclase activator activity; IBA:GO_Central.
DR GO; GO:0008427; F:calcium-dependent protein kinase inhibitor activity; TAS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; IDA:SynGO.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IDA:RGD.
DR GO; GO:0045921; P:positive regulation of exocytosis; IDA:RGD.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cytoplasm; Golgi apparatus;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Reference proteome;
KW Repeat; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10514519"
FT CHAIN 2..190
FT /note="Neuronal calcium sensor 1"
FT /id="PRO_0000073790"
FT DOMAIN 24..59
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 60..95
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 96..131
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 144..179
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 36..47
FT /note="Ancestral calcium site 1"
FT REGION 174..190
FT /note="Interaction with IL1RAPL1"
FT /evidence="ECO:0000250|UniProtKB:P62166"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER"
FT BINDING 77
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25979333,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP"
FT BINDING 161
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP"
FT BINDING 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:25979333, ECO:0007744|PDB:4OV2,
FT ECO:0007744|PDB:4YRU, ECO:0007744|PDB:5AEQ,
FT ECO:0007744|PDB:5AER, ECO:0007744|PDB:5AFP"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10514519"
FT MUTAGEN 73
FT /note="D->A: Loss of magnesium-binding; when associated
FT with Q-84, A-109 and Q-120."
FT /evidence="ECO:0000269|PubMed:18199453"
FT MUTAGEN 84
FT /note="E->Q: Loss of magnesium-binding; when associated
FT with A-73, A-109 and Q-120."
FT /evidence="ECO:0000269|PubMed:18199453"
FT MUTAGEN 109
FT /note="D->A: Loss of magnesium-binding; when associated
FT with A-73, Q-84 and Q-120."
FT /evidence="ECO:0000269|PubMed:18199453"
FT MUTAGEN 120
FT /note="E->Q: Loss of magnesium-binding; when associated
FT with A-73, Q-84 and A-109."
FT /evidence="ECO:0000269|PubMed:18199453"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:5AEQ"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:5AER"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:5AEQ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 45..49
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:5AEQ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5AER"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:5AEQ"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 118..130
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5AER"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:5AEQ"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:5AEQ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:5AER"
SQ SEQUENCE 190 AA; 21879 MW; 9AF8E26A23F80D4F CRC64;
MGKSNSKLKP EVVEELTRKT YFTEKEVQQW YKGFIKDCPS GQLDAAGFQK IYKQFFPFGD
PTKFATFVFN VFDENKDGRI EFSEFIQALS VTSRGTLDEK LRWAFKLYDL DNDGYITRNE
MLDIVDAIYQ MVGNTVELPE EENTPEKRVD RIFAMMDKNA DGKLTLQEFQ EGSKADPSIV
QALSLYDGLV
