ID RAN_CANLF Reviewed; 216 AA. AC P62825; P17080; P28746; P28747; Q9CSP3; Q9CWI7; Q9CZA2; Q9UDJ5; Q9UEU9; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 153. DE RecName: Full=GTP-binding nuclear protein Ran; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P62826}; DE AltName: Full=GTPase Ran; DE AltName: Full=Ras-like protein TC4; DE AltName: Full=Ras-related nuclear protein; GN Name=RAN; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Cocker spaniel; TISSUE=Kidney; RX PubMed=1398150; DOI=10.1016/0378-1119(92)90118-9; RA Dupree P., Olkkonen V.M., Chavrier P.; RT "Sequence of a canine cDNA clone encoding a Ran/TC4 GTP-binding protein."; RL Gene 120:325-326(1992). RN [2] {ECO:0007744|PDB:5BXQ} RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GDP AND NUTF2. RX PubMed=9533885; DOI=10.1006/jmbi.1997.1602; RA Stewart M., Kent H.M., McCoy A.J.; RT "Structural basis for molecular recognition between nuclear transport RT factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran."; RL J. Mol. Biol. 277:635-646(1998). RN [3] {ECO:0007744|PDB:1BYU, ECO:0007744|PDB:3RAN} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANT LEU-69 IN COMPLEX WITH GDP RP AND MAGNESIUM, AND COFACTOR. RX PubMed=9878368; DOI=10.1006/jmbi.1998.2204; RA Stewart M., Kent H.M., McCoy A.J.; RT "The structure of the Q69L mutant of GDP-Ran shows a major conformational RT change in the switch II loop that accounts for its failure to bind nuclear RT transport factor 2 (NTF2)."; RL J. Mol. Biol. 284:1517-1527(1998). RN [4] {ECO:0007744|PDB:1WA5} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP AND RP YEAST ORTHOLOGS OF CSE1L AND KPNA2, AND SUBUNIT. RX PubMed=15602554; DOI=10.1038/nature03144; RA Matsuura Y., Stewart M.; RT "Structural basis for the assembly of a nuclear export complex."; RL Nature 432:872-877(2004). RN [5] {ECO:0007744|PDB:2BKU} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-177 IN COMPLEX WITH GTP AND RP YEAST KPNB1 HOMOLOG, AND INTERACTION WITH HUMAN KPNB1. RX PubMed=15864302; DOI=10.1038/nature03578; RA Lee S.J., Matsuura Y., Liu S.M., Stewart M.; RT "Structural basis for nuclear import complex dissociation by RanGTP."; RL Nature 435:693-696(2005). RN [6] {ECO:0007744|PDB:3A6P} RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEX WITH HUMAN XPO5; RP PRE-MIRNA AND GTP, AND INTERACTION WITH HUMAN XPO5. RX PubMed=19965479; DOI=10.1126/science.1178705; RA Okada C., Yamashita E., Lee S.J., Shibata S., Katahira J., Nakagawa A., RA Yoneda Y., Tsukihara T.; RT "A high-resolution structure of the pre-microRNA nuclear export RT machinery."; RL Science 326:1275-1279(2009). RN [7] {ECO:0007744|PDB:3W3Z} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP AND RP YEAST IMPORTIN PSE1. RX PubMed=23541588; DOI=10.1016/j.jmb.2013.02.035; RA Kobayashi J., Matsuura Y.; RT "Structural basis for cell-cycle-dependent nuclear import mediated by the RT karyopherin Kap121p."; RL J. Mol. Biol. 425:1852-1868(2013). CC -!- FUNCTION: GTPase involved in nucleocytoplasmic transport, participating CC both to the import and the export from the nucleus of proteins and CC RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state CC by nucleotide exchange and GTP hydrolysis. Nuclear import receptors CC such as importin beta bind their substrates only in the absence of GTP- CC bound RAN and release them upon direct interaction with GTP-bound RAN, CC while export receptors behave in the opposite way. Thereby, RAN CC controls cargo loading and release by transport receptors in the proper CC compartment and ensures the directionality of the transport. CC Interaction with RANBP1 induces a conformation change in the complex CC formed by XPO1 and RAN that triggers the release of the nuclear export CC signal of cargo proteins. RAN (GTP-bound form) triggers microtubule CC assembly at mitotic chromosomes and is required for normal mitotic CC spindle assembly and chromosome segregation. Required for normal CC progress through mitosis. The complex with BIRC5/survivin plays a role CC in mitotic spindle formation by serving as a physical scaffold to help CC deliver the RAN effector molecule TPX2 to microtubules. Acts as a CC negative regulator of the kinase activity of VRK1 and VRK2. Enhances CC AR-mediated transactivation. {ECO:0000250|UniProtKB:P62826}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P62826}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P62826}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:9878368}; CC Note=Mg(2+) interacts primarily with the phosphate groups of the bound CC guanine nucleotide. {ECO:0000269|PubMed:9878368}; CC -!- SUBUNIT: Monomer. Interacts with RANGAP1, which promotes RAN-mediated CC GTP hydrolysis. Interacts with KPNB1 (PubMed:15864302). Interaction CC with KPNB1 inhibits RANGAP1-mediated stimulation of GTPase activity. CC Interacts with RCC1 which promotes the exchange of RAN-bound GDP by CC GTP. Interaction with KPNB1 inhibits RCC1-mediated exchange of RAN- CC bound GDP by GTP. Interacts (GTP-bound form) with TNPO1; the CC interaction is direct. Interacts (GTP-bound form) with TNPO3; the CC interaction is direct (By similarity). Interacts with KPNB1 and with CC TNPO1; both inhibit RAN GTPase activity. Interacts (via C-terminus) CC with RANBP1, which alleviates the inhibition of RAN GTPase activity. CC Interacts with RANGRF, which promotes the release of bound guanine CC nucleotide. RANGRF and RCC1 compete for an overlapping binding site on CC RAN. Identified in a complex with KPNA2 and CSE1L; interaction with CC RANBP1 mediates dissociation of RAN from this complex CC (PubMed:15602554). Interaction with both RANBP1 and KPNA2 promotes CC dissociation of the complex between RAN and KPNB1. Identified in a CC complex composed of RAN, RANGAP1 and RANBP1. Identified in a complex CC that contains TNPO1, RAN and RANBP1. Identified in a nuclear export CC complex with XPO1. Found in a nuclear export complex with RANBP3 and CC XPO1. Interacts with RANBP2/NUP358. Interaction with RANBP1 or RANBP2 CC induces a conformation change in the complex formed by XPO1 and RAN CC that triggers the release of the nuclear export signal of cargo CC proteins. Component of a nuclear export receptor complex composed of CC KPNB1, RAN, SNUPN and XPO1 (By similarity). Found in a nuclear export CC complex with RAN, XPO5 and pre-miRNA (PubMed:19965479). Interacts (GTP- CC bound form) with XPO5 (PubMed:19965479). Part of a complex consisting CC of RANBP9, RAN, DYRK1B and COPS5. Interacts with RANBP9 and RANBP10. CC Interacts in its GTP-bound form with BIRC5/survivin at S and M phases CC of the cell cycle. Interacts with TERT; the interaction requires CC hydrogen peroxide-mediated phosphorylation of TERT and transports TERT CC to the nucleus. Interacts with MAD2L2. Interacts with VRK1 and VRK3. CC Interacts with VRK2 (By similarity). Interacts with NEMP1 and KPNB1 (By CC similarity). Interacts (GDP-bound form) with NUTF2; regulates RAN CC nuclear import (PubMed:9533885). Interacts with CAPG; mediates CAPG CC nuclear import. Interacts with NUP153. Interacts with the AR N-terminal CC poly-Gln region; the interaction with AR is inversely correlated with CC the poly-Gln length (By similarity). Interacts with MYCBP2, which CC promotes RAN-mediated GTP hydrolysis (By similarity). Interacts with CC EPG5 (By similarity). {ECO:0000250|UniProtKB:P62826, CC ECO:0000250|UniProtKB:P62827, ECO:0000269|PubMed:15864302, CC ECO:0000269|PubMed:19965479, ECO:0000269|PubMed:9533885, CC ECO:0000305|PubMed:15602554}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P62826}. Nucleus CC envelope {ECO:0000250|UniProtKB:P62826}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P62826}. Cytoplasm CC {ECO:0000250|UniProtKB:P62826}. Melanosome CC {ECO:0000250|UniProtKB:P62826}. Note=Predominantly nuclear during CC interphase. Becomes dispersed throughout the cytoplasm during mitosis CC (By similarity). Identified by mass spectrometry in melanosome CC fractions from stage I to stage IV (By similarity). CC {ECO:0000250|UniProtKB:P62826}. CC -!- PTM: Acetylation by KAT5 at Lys-134 is increased during mitosis, CC impairs RANGRF binding and enhances RCC1 binding. Acetylation at Lys-37 CC enhances the association with nuclear export components. Deacetylation CC of Lys-37 by SIRT7 regulates the nuclear export of NF-kappa-B subunit CC RELA/p65. {ECO:0000250|UniProtKB:P62826}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ran family. CC {ECO:0000255|PROSITE-ProRule:PRU00752, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z11922; CAA77980.1; -; mRNA. DR PIR; JC1455; JC1455. DR RefSeq; NP_001181913.1; NM_001194984.1. DR RefSeq; XP_038291993.1; XM_038436065.1. DR PDB; 1BYU; X-ray; 2.15 A; A/B=1-216. DR PDB; 1QG2; X-ray; 2.50 A; A=1-216. DR PDB; 1QG4; X-ray; 2.50 A; A/B=1-216. DR PDB; 1WA5; X-ray; 2.00 A; A=1-176. DR PDB; 2BKU; X-ray; 2.70 A; A/C=1-177. DR PDB; 3A6P; X-ray; 2.92 A; C/H=1-216. DR PDB; 3RAN; X-ray; 2.15 A; A/B/C/D=1-216. DR PDB; 3W3Z; X-ray; 2.70 A; B=1-176. DR PDB; 5BXQ; X-ray; 2.50 A; C/D/E=1-216. DR PDB; 5YU6; X-ray; 3.00 A; B/D=1-216. DR AlphaFoldDB; P62825; -. DR BMRB; P62825; -. DR MDposit; P62825; -. DR SMR; P62825; -. DR BioGRID; 1530947; 2. DR FunCoup; P62825; 2845. DR IntAct; P62825; 2. DR STRING; 9615.ENSCAFP00000009963; -. DR PaxDb; 9615-ENSCAFP00000009963; -. DR GeneID; 100499482; -. DR KEGG; cfa:100499482; -. DR CTD; 5901; -. DR eggNOG; KOG0096; Eukaryota. DR InParanoid; P62825; -. DR OrthoDB; 1589at33554; -. DR EvolutionaryTrace; P62825; -. DR Proteomes; UP000805418; Unplaced. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0042470; C:melanosome; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0016442; C:RISC complex; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0005049; F:nuclear export signal receptor activity; IMP:UniProtKB. DR GO; GO:0070883; F:pre-miRNA binding; NAS:UniProtKB. DR GO; GO:1905172; F:RISC complex binding; IDA:GO_Central. DR GO; GO:0046039; P:GTP metabolic process; ISS:UniProtKB. DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISS:UniProtKB. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB. DR GO; GO:0035281; P:pre-miRNA export from nucleus; NAS:UniProtKB. DR GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB. DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB. DR GO; GO:0000054; P:ribosomal subunit export from nucleus; IBA:GO_Central. DR GO; GO:0061015; P:snRNA import into nucleus; ISS:UniProtKB. DR CDD; cd00877; Ran; 1. DR FunFam; 3.40.50.300:FF:000131; GTP-binding nuclear protein Ran; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR IDEAL; IID50081; -. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002041; Ran_GTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24071:SF0; GTP-BINDING NUCLEAR PROTEIN RAN; 1. DR PANTHER; PTHR24071; RAN GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00627; GTPRANTC4. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51418; RAN; 1. DR PDBsum; 1BYU; -. DR PDBsum; 1QG2; -. DR PDBsum; 1QG4; -. DR PDBsum; 1WA5; -. DR PDBsum; 2BKU; -. DR PDBsum; 3A6P; -. DR PDBsum; 3RAN; -. DR PDBsum; 3W3Z; -. DR PDBsum; 5BXQ; -. DR PDBsum; 5YU6; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Cell division; Cytoplasm; KW GTP-binding; Hydrolase; Isopeptide bond; Magnesium; Metal-binding; Mitosis; KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; Transport; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P62826" FT CHAIN 2..216 FT /note="GTP-binding nuclear protein Ran" FT /id="PRO_0000208695" FT DOMAIN 7..171 FT /note="Small GTPase Ran-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00752" FT REGION 37..45 FT /note="Switch-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00752" FT REGION 68..84 FT /note="Switch-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00752" FT REGION 211..216 FT /note="Interaction with RANBP1" FT /evidence="ECO:0000250|UniProtKB:P62826" FT BINDING 18..25 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:15602554, FT ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, FT ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9878368, FT ECO:0007744|PDB:1BYU, ECO:0007744|PDB:1WA5, FT ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, FT ECO:0007744|PDB:3RAN, ECO:0007744|PDB:3W3Z, FT ECO:0007744|PDB:5BXQ" FT BINDING 36..42 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:15602554, FT ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, FT ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, FT ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3W3Z" FT BINDING 68 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:15602554, FT ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, FT ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU, FT ECO:0007744|PDB:3W3Z" FT BINDING 122..125 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:15602554, FT ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, FT ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9878368, FT ECO:0007744|PDB:1BYU, ECO:0007744|PDB:1WA5, FT ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, FT ECO:0007744|PDB:3RAN, ECO:0007744|PDB:3W3Z, FT ECO:0007744|PDB:5BXQ" FT BINDING 150..152 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:15602554, FT ECO:0000269|PubMed:15864302, ECO:0000269|PubMed:19965479, FT ECO:0000269|PubMed:9533885, ECO:0000269|PubMed:9878368, FT ECO:0007744|PDB:1BYU, ECO:0007744|PDB:1WA5, FT ECO:0007744|PDB:2BKU, ECO:0007744|PDB:3A6P, FT ECO:0007744|PDB:3RAN, ECO:0007744|PDB:3W3Z, FT ECO:0007744|PDB:5BXQ" FT SITE 69 FT /note="Essential for GTP hydrolysis" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 24 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 37 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 71 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 99 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 134 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 159 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT MOD_RES 159 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62827" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P62826" FT CROSSLNK 152 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62826" FT TURN 3..5 FT /evidence="ECO:0007829|PDB:1BYU" FT STRAND 9..18 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 23..32 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:1BYU" FT HELIX 41..43 FT /evidence="ECO:0007829|PDB:3RAN" FT STRAND 44..55 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 57..66 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 76..80 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 85..91 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 95..99 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 101..111 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:1BYU" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:1WA5" FT TURN 151..153 FT /evidence="ECO:0007829|PDB:1WA5" FT TURN 155..158 FT /evidence="ECO:0007829|PDB:1WA5" FT HELIX 159..169 FT /evidence="ECO:0007829|PDB:1WA5" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:1BYU" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:1BYU" FT HELIX 183..185 FT /evidence="ECO:0007829|PDB:3RAN" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:5BXQ" FT HELIX 191..205 FT /evidence="ECO:0007829|PDB:1BYU" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:5BXQ" SQ SEQUENCE 216 AA; 24423 MW; D5C9B7275C34BCE0 CRC64; MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL //