RAN_CANLF
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 03-AUG-2022, entry version 140.
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:1A2K, 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 + H(+) + phosphate; 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:0000305}.
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DR EMBL; Z11922; CAA77980.1; -; mRNA.
DR PIR; JC1455; JC1455.
DR RefSeq; NP_001181913.1; NM_001194984.1.
DR PDB; 1A2K; X-ray; 2.50 A; C/D/E=1-216.
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 PDBsum; 1A2K; -.
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; -.
DR AlphaFoldDB; P62825; -.
DR BMRB; P62825; -.
DR SMR; P62825; -.
DR BioGRID; 1530947; 1.
DR IntAct; P62825; 2.
DR STRING; 9615.ENSCAFP00000009963; -.
DR PaxDb; P62825; -.
DR PRIDE; P62825; -.
DR GeneID; 100499482; -.
DR KEGG; cfa:100499482; -.
DR CTD; 5901; -.
DR eggNOG; KOG0096; Eukaryota.
DR InParanoid; P62825; -.
DR OrthoDB; 1083175at2759; -.
DR EvolutionaryTrace; P62825; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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 Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID50081; -.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002041; Ran_GTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR24071; PTHR24071; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00627; GTPRANTC4.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51418; RAN; 1.
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 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:1A2K, ECO:0007744|PDB:1BYU,
FT ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU,
FT ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3RAN,
FT ECO:0007744|PDB:3W3Z, 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:1A2K, ECO:0007744|PDB:1BYU,
FT ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU,
FT ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3RAN,
FT ECO:0007744|PDB:3W3Z, 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:1A2K, ECO:0007744|PDB:1BYU,
FT ECO:0007744|PDB:1WA5, ECO:0007744|PDB:2BKU,
FT ECO:0007744|PDB:3A6P, ECO:0007744|PDB:3RAN,
FT ECO:0007744|PDB:3W3Z, 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 STRAND 38..40
FT /evidence="ECO:0007829|PDB:1BYU"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3RAN"
FT STRAND 44..54
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 191..205
FT /evidence="ECO:0007829|PDB:1BYU"
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
