ID G1STZ5_RABIT Unreviewed; 2499 AA.
AC G1STZ5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=LRRK2 {ECO:0000313|Ensembl:ENSOCUP00000006801.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000006801.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000006801.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000006801.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000006801.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000006801.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
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DR EMBL; AAGW02045241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02045242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02045243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02045244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02045245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02045246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR SMR; G1STZ5; -.
DR STRING; 9986.ENSOCUP00000006801; -.
DR PaxDb; 9986-ENSOCUP00000006801; -.
DR Ensembl; ENSOCUT00000007867.3; ENSOCUP00000006801.3; ENSOCUG00000007857.3.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158267; -.
DR HOGENOM; CLU_000815_0_0_1; -.
DR InParanoid; G1STZ5; -.
DR TreeFam; TF313679; -.
DR Proteomes; UP000001811; Chromosome 8.
DR Bgee; ENSOCUG00000007857; Expressed in upper lobe of left lung and 16 other cell types or tissues.
DR GO; GO:0044753; C:amphisome; IEA:Ensembl.
DR GO; GO:0044754; C:autolysosome; IEA:Ensembl.
DR GO; GO:0099400; C:caveola neck; IEA:Ensembl.
DR GO; GO:0032473; C:cytoplasmic side of mitochondrial outer membrane; IEA:Ensembl.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005798; C:Golgi-associated vesicle; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR GO; GO:0097487; C:multivesicular body, internal vesicle; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR GO; GO:1990909; C:Wnt signalosome; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:1904713; F:beta-catenin destruction complex binding; IEA:Ensembl.
DR GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0034211; F:GTP-dependent protein kinase activity; IEA:Ensembl.
DR GO; GO:0005096; F:GTPase activator activity; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0036479; F:peroxidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0051018; F:protein kinase A binding; IEA:Ensembl.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IEA:Ensembl.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:1903351; P:cellular response to dopamine; IEA:Ensembl.
DR GO; GO:0071287; P:cellular response to manganese ion; IEA:Ensembl.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0046039; P:GTP metabolic process; IEA:Ensembl.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl.
DR GO; GO:1902902; P:negative regulation of autophagosome assembly; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0010955; P:negative regulation of protein processing; IEA:Ensembl.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IEA:Ensembl.
DR GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IEA:Ensembl.
DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IEA:Ensembl.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IEA:Ensembl.
DR GO; GO:0035564; P:regulation of kidney size; IEA:Ensembl.
DR GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
DR GO; GO:0035751; P:regulation of lysosomal lumen pH; IEA:Ensembl.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:1902692; P:regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0014041; P:regulation of neuron maturation; IEA:Ensembl.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:1905279; P:regulation of retrograde transport, endosome to Golgi; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:1902803; P:regulation of synaptic vesicle transport; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl.
DR GO; GO:1904887; P:Wnt signalosome assembly; IEA:Ensembl.
DR CDD; cd14068; STKc_LRRK2; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR48005; LEUCINE RICH REPEAT KINASE 2; 1.
DR PANTHER; PTHR48005:SF13; SERINE_THREONINE-PROTEIN KINASE DDB_G0278509-RELATED; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; ARM repeat; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51419; RAB; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022530};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT DOMAIN 1301..1484
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1852..2119
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 958..977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..977
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1879
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2499 AA; 280866 MW; 6EA18DFBF8F83871 CRC64;
MASGGGSNQG SDEDEESLKK LLVKLNNVQE GKQVETLVQT LEDLLVFTYS ERASRLFRGK
SFHVPLLIVL DSYMRVASVQ QVGWSLLCKL IEVCPDTMQS LMGPQDVGSD WEVLGVHQLI
LRMLSVHSAS VNLLTVGLKA LDLLLTSGKI TLLILEEESD IFLLIFDAMR TFPANDEIQK
LGCKALHVLF ERVSEEQLTE FVENKDYMIL LSALKNFKDE EEIVLHVLHC LHSLAIPCNN
VEVLMSGNVR CYNIVVEAMK AFPVSEKIQE VSCCLLHRLT LGNFFNILVL NEVHAFVVRA
VRRYPENAAL QISALGCLAL LTETIFLNQD LEEKSEAQSG EEEEEEDKLF WLEACYKALT
GHRKNRHVQE AACWSLNNLL MYHSSLHERI GDEDGQLPAH REVMLSMLMH SSSKEVFQAS
ANALSTLLEQ NVNFRKILLS KGIYLNVLEL MQRHAHSPEV AESGCKMLNH LFEGSHISLD
TVAAVVPKII TVMRSHEASL SVQLEALRAI LHFMMPGMPE ESREETESQR NLNVVRKQCF
RSDIHKLVLA ALNRFVGNPG IQKCGLKVMA SITQVPDALE VLSLEGAVDS VLHTLHMYPD
DQEIQCLGLS LVGRLIAKKN LCTGTGHLLA KILVSSLQRF KDAAEVQLEG FRTVLAILEL
SVSFSKLLVH HSFDSVIFHQ MSSSITEQKD QQFLSLCCKC FAKLAMEDEL KNAMLQRACD
QNNSIMVECL LLLGADANQT KEATSLICQV CEKESSPKLV ELLLDSGSRE QDVRKALAVS
IGKGDSQVIS LLLKRLALDL ANNSICLGGF GIGKIEPSWL GPLFPDKTSN LRKQTNIGSI
LARMVLRHQM KSAVEEGAAP GSEENFPEGV LDKLDEWTFI PDSSMDSVFG QSDDLDSEGS
EGSFLVRKKS SSIGVGEFYR DPVLQRCSPN LPRHSNSLGP VFDQEDLRRQ KRKILSSDDS
LRSTKLQSHG RQSDSVSSLA SEREYITSLD LSANELREVD ALSRRGCLSG HLEHLERLEL
QQNALVSFPQ PLCENLDVSR NDIGPSVILD PAVRCLTLRQ LNLSYNQLSA VPESLAEVAE
KLEQLLLEGN KISGTCSPLS LKELKILNLS KNHISCLPEN FLEACPKVES FSARMNLLAD
MPFLPSSMTS LKLSQNKFTS VPEAILNLPH LRSLDMSSND IQCLPGPARW TSLNLRELLF
SYNQISVLDL SEKAHAWCRV EKLHLAHNKL KEIPPEIGYL ENLTSLDVSY NSELRSFPNE
MGKLSKIWDL PLDELRLNFD FKHVGCKAKD IIRFLQQRLR KAVPYNRMKL MIVGNTGSGK
TTLLQQLMRA KKADVGMQGA TVGIDVRDWP VQIRSKGKRD LVLNVWDFAG REEFYSTHPH
FMTQRALYLA VYDLSKGQAE VDAMKPWLFN IKARASSSPV ILVGTHLDVS DEKQRKACIG
KITRELLNKR GFPAIRDYHF VNATEESDAL AKLRKTIINE SLNFKIRDQP VVGQLIPDCY
VELEKIILSE RKNVPTEFPV IDRKRLLQLV RDNQLQLDEN ELPHAIHFLN ESGVLLHFQD
PALQLSDLYF VEPKWLCKVM AQILTVKVEG YPKHPKGIIS RRDVEKFLSK KRRFPKNYMT
QYVKLLEKFQ IALPIGEEYL LVPSSLSDHR PVIELPHCEN SEIIIRLYEM PYFPMGFWSR
LINRLLEISP YMLSGRERAL RPNRMYWRQG IYLNWSPEAY CLVGSEVLDH HPESFLKITV
PSCRKGCILL GQVVDHIDSL MEEWFPGLLE IDICGEGETL LKKWALYSFN DGEEHQKILL
DDLMKKAEEG DLLINPDQPR LTIPISQIAP DLVLADLPRN IMLNNDELEF QQAPEFLLGD
GSFGSVYRAV YEGEEVAVKI FNKHTSLRLL RQELVVLCHL HHPSLISLLA AGIRPRMLVM
ELAPKGSLDR LLQQDKASLT RTLQHRIALH VADGLRYLHS AMIIYRDLKP HNVLLFTLYP
NAAIIAKIAD YGISQYCCRM GIKTSEGTPG FRAPEVARGN VIYNQQADVY SFGLLLYDIL
TTGGRIVEGL KFPNEFDELA IQGKLPDPVK EYGCTPWPLV EKLIKKCLKE NPQERPTSAQ
VFDILNSAEL ICLMRHILIP KSVTVECMVA SSPGGKSTSI WLGCSHTDKG QLSFLNLNTE
GHTTEEVSES RVLCLALVSL PVEKESWIVC GTQSGALLAI STEDGKRRHS LEKMTDSVTC
LYCNSFPKQS KQKNFLLVGT ADGKLAIFED KTVKCEGAAP VKTLNIGNVS TPLMCLSESV
NSTEKNTMWG GCGTKIFSLS HDFTVQKLIE TRTNQLFSYA AFSDSNIIAV AVDTALYVAK
KNSPVVEVWD KKTEKLCELI DCVHFLKEAM AVGKQESKHS LFYSVRVKAL CLQKNTALWI
GTGGGHILLL DLSTRRVIRI IYNFCDSVRV MATAQSGSLK NVMLVLGYNR KSAEGMQHRE
IQSCLSIWDT NLPHEVQNLE KHIEVRKELA EKMRRTSVE
//
