NU214_DROME
ID NU214_DROME Reviewed; 1711 AA.
AC Q9W1X4; Q8T3K4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Nuclear pore complex protein Nup214;
DE AltName: Full=214 kDa nucleoporin;
DE Short=DNup214;
DE AltName: Full=Nucleoporin Nup214;
GN Name=Nup214 {ECO:0000312|EMBL:AAF46928.2}; ORFNames=CG3820;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF46928.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF46928.2}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAM11320.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MBO/NUP88, AND SUBCELLULAR LOCATION.
RX PubMed=14638854; DOI=10.1083/jcb.200304046;
RA Roth P., Xylourgidis N., Sabri N., Uv A.E., Fornerod M., Samakovlis C.;
RT "The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the
RT nuclear envelope and attenuates NES-mediated nuclear export.";
RL J. Cell Biol. 163:701-706(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EMB AND MBO.
RX PubMed=17032737; DOI=10.1242/jcs.03201;
RA Xylourgidis N., Roth P., Sabri N., Tsarouhas V., Samakovlis C.;
RT "The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates
RT NFkappaB activation in Drosophila.";
RL J. Cell Sci. 119:4409-4419(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=17682050; DOI=10.1083/jcb.200612135;
RA Sabri N., Roth P., Xylourgidis N., Sadeghifar F., Adler J., Samakovlis C.;
RT "Distinct functions of the Drosophila Nup153 and Nup214 FG domains in
RT nuclear protein transport.";
RL J. Cell Biol. 178:557-565(2007).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20547758; DOI=10.1128/mcb.00124-10;
RA Chen X., Xu L.;
RT "Specific nucleoporin requirement for Smad nuclear translocation.";
RL Mol. Cell. Biol. 30:4022-4034(2010).
CC -!- FUNCTION: Part of the nuclear pore complex (PubMed:14638854). Serves as
CC a docking site in the receptor-mediated import of substrates across the
CC nuclear pore complex including emb, RanGAP and phosphorylated Mad
CC (PubMed:17682050, PubMed:20547758, PubMed:17032737). Protects mbo/Nup88
CC from proteasomal degradation at the nuclear pore (PubMed:17032737).
CC Together with mbo/Nup88, sequesters emb in the cytoplasm and thereby
CC attenuates nuclear export signal (NES)-mediated nuclear export
CC (PubMed:17032737). Together with mbo/Nup88, required for the nuclear
CC import of the Rel family transcription factors dorsal (dl) and Dorsal-
CC related immunity factor (Dif) and the activation of an immune response
CC (PubMed:17032737). {ECO:0000269|PubMed:14638854,
CC ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:17682050,
CC ECO:0000269|PubMed:20547758}.
CC -!- SUBUNIT: Component of the nuclear pore complex (PubMed:14638854).
CC Interacts with mbo/Nup88 and (via C-terminus) with emb to attenuate
CC emb-mediated protein export (PubMed:14638854, PubMed:17032737).
CC {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:20547758}. Nucleus
CC membrane {ECO:0000269|PubMed:17032737}; Peripheral membrane protein;
CC Cytoplasmic side {ECO:0000269|PubMed:20547758}. Note=Localization to
CC the nucleus membrane depends on mbo/Nup88.
CC {ECO:0000269|PubMed:17032737}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC FG-rich region is required for emb localization to the nuclear pore
CC complex. {ECO:0000269|PubMed:17682050}.
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DR EMBL; AE013599; AAF46928.2; -; Genomic_DNA.
DR EMBL; AY094967; AAM11320.1; -; mRNA.
DR RefSeq; NP_652039.2; NM_143782.3.
DR AlphaFoldDB; Q9W1X4; -.
DR SMR; Q9W1X4; -.
DR BioGRID; 70095; 14.
DR DIP; DIP-18878N; -.
DR IntAct; Q9W1X4; 3.
DR MINT; Q9W1X4; -.
DR STRING; 7227.FBpp0071905; -.
DR PaxDb; Q9W1X4; -.
DR PRIDE; Q9W1X4; -.
DR EnsemblMetazoa; FBtr0071996; FBpp0071905; FBgn0010660.
DR GeneID; 46091; -.
DR KEGG; dme:Dmel_CG3820; -.
DR UCSC; CG3820-RA; d. melanogaster.
DR CTD; 8021; -.
DR FlyBase; FBgn0010660; Nup214.
DR VEuPathDB; VectorBase:FBgn0010660; -.
DR eggNOG; KOG3630; Eukaryota.
DR GeneTree; ENSGT00940000165854; -.
DR HOGENOM; CLU_247466_0_0_1; -.
DR InParanoid; Q9W1X4; -.
DR OMA; WLSTFQF; -.
DR OrthoDB; 275785at2759; -.
DR PhylomeDB; Q9W1X4; -.
DR Reactome; R-DME-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-DME-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-DME-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-DME-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DME-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-DME-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DME-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 46091; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 46091; -.
DR PRO; PR:Q9W1X4; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010660; Expressed in eye disc (Drosophila) and 23 other tissues.
DR Genevisible; Q9W1X4; DM.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:FlyBase.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IMP:FlyBase.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; IMP:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0090204; P:protein localization to nuclear pore; IMP:FlyBase.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR026054; Nucleoporin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR23193; PTHR23193; 1.
PE 1: Evidence at protein level;
KW Membrane; mRNA transport; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..1711
FT /note="Nuclear pore complex protein Nup214"
FT /id="PRO_0000204860"
FT REPEAT 472..473
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 486..487
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 497..498
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 511..512
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 514..515
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 535..536
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 588..589
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 598..599
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1009..1010
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1075..1076
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1077..1078
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1097..1098
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1106..1107
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1135..1136
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1218..1219
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1229..1230
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 1240..1241
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 1356..1357
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 1388..1389
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 1399..1400
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 1434..1435
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 1449..1450
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 1458..1459
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 1472..1473
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 1481..1482
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 1487..1488
FT /note="26"
FT /evidence="ECO:0000305"
FT REPEAT 1507..1508
FT /note="27"
FT /evidence="ECO:0000305"
FT REPEAT 1512..1513
FT /note="28"
FT /evidence="ECO:0000305"
FT REPEAT 1539..1540
FT /note="29"
FT /evidence="ECO:0000305"
FT REPEAT 1547..1548
FT /note="30"
FT /evidence="ECO:0000305"
FT REPEAT 1562..1563
FT /note="31"
FT /evidence="ECO:0000305"
FT REPEAT 1571..1572
FT /note="32"
FT /evidence="ECO:0000305"
FT REPEAT 1584..1585
FT /note="33"
FT /evidence="ECO:0000305"
FT REPEAT 1588..1589
FT /note="34"
FT /evidence="ECO:0000305"
FT REPEAT 1601..1602
FT /note="35"
FT /evidence="ECO:0000305"
FT REPEAT 1617..1618
FT /note="36"
FT /evidence="ECO:0000305"
FT REPEAT 1623..1624
FT /note="37"
FT /evidence="ECO:0000305"
FT REPEAT 1629..1630
FT /note="38"
FT /evidence="ECO:0000305"
FT REPEAT 1635..1636
FT /note="39"
FT /evidence="ECO:0000305"
FT REPEAT 1641..1642
FT /note="40"
FT /evidence="ECO:0000305"
FT REPEAT 1647..1648
FT /note="41"
FT /evidence="ECO:0000305"
FT REPEAT 1650..1651
FT /note="42"
FT /evidence="ECO:0000305"
FT REPEAT 1662..1663
FT /note="43"
FT /evidence="ECO:0000305"
FT REPEAT 1686..1687
FT /note="44"
FT /evidence="ECO:0000305"
FT REPEAT 1702..1703
FT /note="45"
FT /evidence="ECO:0000305"
FT REGION 472..1703
FT /note="45 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 650..672
FT /note="Leucine-zipper 1"
FT REGION 767..788
FT /note="Leucine-zipper 2"
FT REGION 886..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1044..1711
FT /note="Interaction with emb"
FT /evidence="ECO:0000269|PubMed:17032737"
FT REGION 1251..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1533..1552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1557..1614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1034..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1596..1614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 72
FT /note="A -> G (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="V -> I (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="T -> N (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="S -> P (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1143
FT /note="A -> T (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1162
FT /note="T -> A (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1174
FT /note="V -> A (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1246
FT /note="V -> L (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1267
FT /note="P -> A (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1319
FT /note="S -> G (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1344
FT /note="A -> S (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
FT CONFLICT 1385
FT /note="A -> G (in Ref. 3; AAM11320)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1711 AA; 175176 MW; 7C73E46C789E55ED CRC64;
MAQNAPDCED TQDFQFKLHH KIVAFKKCGE PRSNVNLLAV SSSRGLLFAG SPTQPELKVI
IVKDLVNAKS TAQQPQARLV PLPSIPNYIA CSSDGNLLAV NHTQNGTSLL SIYAVLSFMT
PDVRPVYNIR LAAEDHVHGV QLLWNPVLPN SLAVVLSNGA LAMYALKEGG NFEMHSLDKN
QQVKCGCWSP KGKQIVLGFP GGTVKQFKPD LTLAKTLLCP PNIHDAPFDT IAIQWLSTFQ
FAVIFLQHGE DCSPSLYILN APKAGAPSYI NYYDICYSMN GPRNHQFVFS HVPQWNLLLV
VSANGVEVGI MRSTEAGDTP AWQQLTLLDE ARIEMPLSED KDETFPLGFA FDTSTTHQLT
INEKKLQTMP MVHVLSSDGE LLSFNFLNVL PTAVSVCSPP PPVADTSGQF KPLNMLLASE
EEEQPAWAAS PSKAPAATPA ASSDISFAFT PNTVTSTPAP SKDKQPSLFS GFGAAAAKAP
APQLSFGTAP TSSPVSFGAP TTNAAKPTTP FGGFGTQATT TAMGSMFSAS GANAFGGMAL
NKPAIASVTP RTAAPGSTVP ATPASAPANK PLYTVPLTFT PVDTKPATSA PPQIADESLK
PDDTEPIIKD MIALQIEAFS KDIQKQKEQT KELLKGIAAP SALRAYAKRL DDLQELNEQA
KDVEFELDVQ GLRQGLNEAY AIVAECRGKL EIYRKPEITR LMNSSSCDPS GRRMLARLQS
YVAANEAQLR LAQQHVDLQW EQFQDVVRRN SKSRMHMPCL EGIYQRLTRL QNLTSNQRIV
QNNIKSKLKE RGLLQAALLD QEKSRTRTNE AVDTLTDSIL TMSLSQVVDS NAAKLTRERL
QKIRNIVQLQ KINVICPQRP DRVGLKSEVI LETKRRAEQI KRAAAKPATA NKYTQAAVAP
PSPPDVAPTP AVAPMPQATV TVAPPLPKPM PSIPSVVEKP GVPTHPTTPV ATPFSFSQSI
PFVKTSTVTP TTNTVTPGEA AKPGLSIFGG STISSFSFGG GAAKSALSFG TGSPAVAAPT
PKPNPLSAVE KPTPEPTKPK EQKAAESKEF KAVQPETEES KVPQKPKAET ENKSFGFGGF
TGTGGTVGNT SSSPFSFGGL GSSLGFGGTA AAVPKSEPSS TATTSVATSA STAPFGIFSA
ALAKPSNSEP ITTVTSNTTT ITSKPTNVIA SSSVTDAPSV TTTNAVTSST DPIGGLFSSV
TICKPNTPAD TTKPANIFGG GLSAGSFSFG GTIDASKGLF GSTKPVATAP TSVTEANNKT
DPISTTPSAI STTTATTTVS SPAVVPAAVT AAVPATSSTT VTSSTAVPGS AFSFSNAFST
LSAGGAAAPT TSASAPLAAK SPTATSTGNN SSNSVFGGGF AVATSTAAPV ASPFQSAAKS
PVSSANIFGS IPKAETSVFG GATTAPSNTT AAATPDAPPA GLFASAAISN PSPFGSPTTR
APASGGNIFG QAVKPSVFGQ PAQAGDSGGS IFGGGSASTP FGSSSIFGGG NTQGAVGAPA
AGSTSIFGQK VFGQSSAAAP AAGGNIFSNP VGSPQASPFG GGGNSIFGSP ATAPPASGGS
IFGGGSSSGG FGSFTQTTPA QGGFGGGFGQ GGGGSVAQTG FGSPQAPQQQ TTTPGGFGAK
PVFGGSPAFG ASPTFGGGAT FGSPKGFGGF GGASPVASPP PFGAAAKPAQ GNIFETLGGQ
ESGLSFGNLA QTGNSNAQKP AFGGSSFMNY R
