NU214_MOUSE
ID NU214_MOUSE Reviewed; 2085 AA.
AC Q80U93; A2ATN2;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Nuclear pore complex protein Nup214;
DE AltName: Full=214 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup214;
GN Name=Nup214; Synonyms=Kiaa0023;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-1139, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Part of the nuclear pore complex. Has a critical role in
CC nucleocytoplasmic transport. May serve as a docking site in the
CC receptor-mediated import of substrates across the nuclear pore complex.
CC {ECO:0000250|UniProtKB:P35658}.
CC -!- SUBUNIT: Homodimer. Part of the nuclear pore complex (NPC). Interacts
CC with NUP88. Interacts with ZFP36; this interaction increases upon
CC lipopolysaccharide (LPS) stimulation. Interacts with DDX19. Interacts
CC with XPO1. Interacts with XPO5. {ECO:0000250|UniProtKB:P35658}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:P35658}. Note=Cytoplasmic side of the nuclear
CC pore complex. {ECO:0000250|UniProtKB:P35658}.
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 {ECO:0000305}.
CC -!- DOMAIN: The beta-propeller contains long interblade connector loops,
CC and mediates interaction with DDX19B. {ECO:0000250}.
CC -!- PTM: Probably glycosylated as it reacts with wheat germ agglutinin
CC (WGA). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122189; BAC65471.1; ALT_INIT; mRNA.
DR EMBL; AL928893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38098.1; -.
DR RefSeq; NP_758472.2; NM_172268.2.
DR AlphaFoldDB; Q80U93; -.
DR SMR; Q80U93; -.
DR BioGRID; 230673; 40.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q80U93; 30.
DR STRING; 10090.ENSMUSP00000066492; -.
DR iPTMnet; Q80U93; -.
DR PhosphoSitePlus; Q80U93; -.
DR SwissPalm; Q80U93; -.
DR EPD; Q80U93; -.
DR jPOST; Q80U93; -.
DR MaxQB; Q80U93; -.
DR PaxDb; Q80U93; -.
DR PeptideAtlas; Q80U93; -.
DR PRIDE; Q80U93; -.
DR ProteomicsDB; 287842; -.
DR Antibodypedia; 18059; 80 antibodies from 19 providers.
DR Ensembl; ENSMUST00000065398; ENSMUSP00000066492; ENSMUSG00000001855.
DR GeneID; 227720; -.
DR KEGG; mmu:227720; -.
DR UCSC; uc008jeh.1; mouse.
DR CTD; 8021; -.
DR MGI; MGI:1095411; Nup214.
DR VEuPathDB; HostDB:ENSMUSG00000001855; -.
DR eggNOG; KOG3630; Eukaryota.
DR GeneTree; ENSGT00940000153253; -.
DR HOGENOM; CLU_001606_0_0_1; -.
DR InParanoid; Q80U93; -.
DR OMA; WLSTFQF; -.
DR OrthoDB; 747759at2759; -.
DR PhylomeDB; Q80U93; -.
DR TreeFam; TF323517; -.
DR Reactome; R-MMU-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-MMU-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-MMU-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
DR BioGRID-ORCS; 227720; 25 hits in 75 CRISPR screens.
DR ChiTaRS; Nup214; mouse.
DR PRO; PR:Q80U93; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80U93; protein.
DR Bgee; ENSMUSG00000001855; Expressed in animal zygote and 166 other tissues.
DR ExpressionAtlas; Q80U93; baseline and differential.
DR Genevisible; Q80U93; MM.
DR GO; GO:1990876; C:cytoplasmic side of nuclear pore; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR GO; GO:0005049; F:nuclear export signal receptor activity; ISO:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; ISO:MGI.
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 InterPro; IPR001680; WD40_repeat.
DR PANTHER; PTHR23193; PTHR23193; 1.
DR SMART; SM00320; WD40; 2.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Glycoprotein; Isopeptide bond; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT CHAIN 2..2085
FT /note="Nuclear pore complex protein Nup214"
FT /id="PRO_0000345014"
FT REPEAT 41..93
FT /note="Blade 1"
FT /evidence="ECO:0000250"
FT REPEAT 94..150
FT /note="Blade 2"
FT /evidence="ECO:0000250"
FT REPEAT 151..193
FT /note="Blade 3"
FT /evidence="ECO:0000250"
FT REPEAT 194..239
FT /note="Blade 4"
FT /evidence="ECO:0000250"
FT REPEAT 240..303
FT /note="Blade 5"
FT /evidence="ECO:0000250"
FT REPEAT 304..359
FT /note="Blade 6"
FT /evidence="ECO:0000250"
FT REPEAT 360..404
FT /note="Blade 7"
FT /evidence="ECO:0000250"
FT REPEAT 482..483
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 546..547
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 1232..1233
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 1264..1265
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 1423..1424
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 1439..1440
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 1453..1454
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 1486..1487
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1643..1644
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1682..1683
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1704..1705
FT /note="11"
FT /evidence="ECO:0000305"
FT REPEAT 1709..1710
FT /note="12"
FT /evidence="ECO:0000305"
FT REPEAT 1717..1718
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 1722..1723
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 1728..1729
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 1752..1753
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 1768..1769
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 1782..1783
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 1794..1795
FT /note="19"
FT /evidence="ECO:0000305"
FT REPEAT 1802..1803
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 1808..1809
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 1815..1816
FT /note="22"
FT /evidence="ECO:0000305"
FT REPEAT 1838..1839
FT /note="23"
FT /evidence="ECO:0000305"
FT REPEAT 1847..1848
FT /note="24"
FT /evidence="ECO:0000305"
FT REPEAT 1858..1859
FT /note="25"
FT /evidence="ECO:0000305"
FT REPEAT 1869..1870
FT /note="26"
FT /evidence="ECO:0000305"
FT REPEAT 1905..1906
FT /note="27"
FT /evidence="ECO:0000305"
FT REPEAT 1917..1918
FT /note="28"
FT /evidence="ECO:0000305"
FT REPEAT 1925..1926
FT /note="29"
FT /evidence="ECO:0000305"
FT REPEAT 1928..1929
FT /note="30"
FT /evidence="ECO:0000305"
FT REPEAT 1933..1934
FT /note="31"
FT /evidence="ECO:0000305"
FT REPEAT 1954..1955
FT /note="32"
FT /evidence="ECO:0000305"
FT REPEAT 1965..1966
FT /note="33"
FT /evidence="ECO:0000305"
FT REPEAT 1971..1972
FT /note="34"
FT /evidence="ECO:0000305"
FT REPEAT 1977..1978
FT /note="35"
FT /evidence="ECO:0000305"
FT REPEAT 1983..1984
FT /note="36"
FT /evidence="ECO:0000305"
FT REPEAT 1989..1990
FT /note="37"
FT /evidence="ECO:0000305"
FT REPEAT 2007..2008
FT /note="38"
FT /evidence="ECO:0000305"
FT REPEAT 2019..2020
FT /note="39"
FT /evidence="ECO:0000305"
FT REPEAT 2021..2022
FT /note="40"
FT /evidence="ECO:0000305"
FT REPEAT 2030..2031
FT /note="41"
FT /evidence="ECO:0000305"
FT REPEAT 2041..2042
FT /note="42"
FT /evidence="ECO:0000305"
FT REPEAT 2051..2052
FT /note="43"
FT /evidence="ECO:0000305"
FT REPEAT 2061..2062
FT /note="44"
FT /evidence="ECO:0000305"
FT REPEAT 2070..2071
FT /note="45"
FT /evidence="ECO:0000305"
FT REPEAT 2080..2081
FT /note="46"
FT /evidence="ECO:0000305"
FT REGION 41..404
FT /note="Seven-bladed beta propeller"
FT /evidence="ECO:0000250"
FT REGION 236..1430
FT /note="46 X 2 AA repeats of F-G"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT REGION 423..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..2071
FT /note="11 X 5 AA approximate repeats"
FT REGION 491..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..762
FT /note="Leucine-zipper 1"
FT REGION 855..876
FT /note="Leucine-zipper 2"
FT REGION 1134..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1174..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1421..2079
FT /note="18 X 4 AA approximate repeats"
FT REGION 1439..2080
FT /note="11 X 3 AA approximate repeats"
FT REGION 1453..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1495..1575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1615..1636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1763..1814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1880..1899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 674..1217
FT /evidence="ECO:0000250"
FT COMPBIAS 491..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1618..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 416
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 437
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1027
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1062
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 1156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1162
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT MOD_RES 1980
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT CROSSLNK 1548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P35658"
FT CONFLICT 1973
FT /note="S -> G (in Ref. 1; BAC65471)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2085 AA; 212979 MW; C9998CC8BC27EE4A CRC64;
MGDEMDAMIP EREMKDFQFR ALKKVRIFDS PEELPKERSS VLTISNKYGM LFAGGTNGLN
VFPTKSLLIQ NKPGDDPNKI VDTIQGLNVP MKFPVHHLAL SCDSLTLSAC MMSSEYGSII
AFFDVRTFSN QAKPLKRPFT YHKVSNDASG MVNDMKWNPT VPSMVAVCLA DGSISVLQVT
DVVKVCATLP PSTGVTCVCW SPKGKQLAVG KQNGTVVQYL PTLQEKKVIP CPPFYESDHP
VRVLDVLWIG TYVFTIVYAG ADGTLETCPD VVMALLPKKE EKHPEIFVNF MEPCYSSCTE
RQHHYYLSYI EEWDLVLAAS AASTEVSILA RQNDQTNWES WLLEDSSRAE LPVTDKSDDS
LPMGVAIDYT NEVEVTINEE KTLPPAPVLL LLSTDGVLCP FYMINQNPGV RSLIKTLELI
STEGERQPKS SGSFPGTPSS PQAPQNLDAP ATASSPLPPV SAAPTSTFPM PSAAGSPSVF
SFGPSSFKSS ASVTGEPPLY PTGSDSSRAA PGSGTSTFSF APPSKGSLAS TPAVAPVATS
AAPFTFGFKP TLESTPMSST PNTGMKPSFP PSASSVKVNL NEKFTAVASS APVHSSTSTP
SVLPFSSSPK PTASGPLSHP TPLPASSSSM PLKSSVSPSP AAGRSTQTAP SSAPSTGQKS
PRVNPPVPKS GSSQAKALQP PVTEKQRPQW KDSDPVLAGI GEEIAHFQKE LEELKARTAK
ACLQVGTSEE MKMLRTESDD LHTFLFEIRE TTESLHGDIS TLKTTLLEGF AGVEEAREQH
GRNHDSGYLH LLYKRPLDPK SEAQLQEIRR LHQYVKFAVQ DVNDVLDLEW DRHLEQKKRQ
RRLIVPERET LFNTLANNRE IINQQRKRLN QLVDSLQQLR LYNHTAPWSL PSALSTQSNS
HSFDSDLECL LKTTIESHTK PSPRVPGKLS PAKQAQLRNF LAKRKTPPVR STAPASLSRS
AFLSQRYYED LDEGSSASSV AQPLEGEDAR PTCTSVAQPL EGEDAQPICK EEEAVVPVPR
HAPVVRTPSI QPSLLPQSMP FAKPHLIHSS SPAVMSSAVS TSATKVIPQG ADSTMLATKT
VKHGAPGPSH TVAAPQAAAA AALRRQMASQ APAMSTLTES TLKTVPQVVN VQELRSNPSP
PSAAMGSAVQ HSAAKTPHAV LTPVANSQAK QGSLINSFKP SGPTAASCQL SSGDKAVGQG
TAKTESAATS TPSAAGQLNK PFSFASPGTF TFGTITPTPS SSFTATPGAG PPTKEPTQLE
AFSFGGGGKP FSEAIPGNSP ATGATSAPST SVTAASLEDS APSSSKPAAP PETTVSSASS
KLETPPSKLG ELLFPSSLAG ETLGSFSGLR VGQAEDSTKP VSKASSTNLA GAQPAKPSGV
SFPNTSVLGK PVEPAVTSSV SPAPAAPASA LNVSTSSSSA TVFGSVPLTS AGPPGLISFG
GAALASSKAS FSFGNQQTSS STASSATPTS TSVAPSLPAS FPTLSFGGLL SSPSASSLPV
SSGKSTEEAA PPAVPDKSDS SEVSATTPSL PVQPQSTQAS LQTSDPVKKE PVLVQTTDSS
PSRPASSASF VASTESMPVT LGAPDSKIEA VSPASTFAGP GQAAVATAVL PGAGSAATEA
SGTPTTSTVS SSSPTSATET AVFGTATSGS SVFTQPPAAS SSSAFSQLSS NTATAPSATP
VFGQVAASIT STAAATPQAS SSGFGSPAFG ASAPGVFGQT AFGQTPAFGQ ATSSPASGFS
FSQPGFSSVP AFGQSVSSTP ASTSANVFGA TSSTSSPGSF SFGQASTNTG GTLFGQNNPP
AFGQSPGFGQ GSSVFGGTSA TTSTAAPSGF SFCQASGFGS SNTGSVFGQA ANTGGSVFGQ
SSTSSGGVFG SGNATRGGGF FSGLGGKPSQ DAANKNPFSS AGGGFGSTAA PNTSNLFGNS
GAKTFGGFGS SSFGEQKPAG TFSSGGGSVA SQGFGFSTPN KTGGFGAAPV FGSPPTFGGS
PGFGGVPAFG SAPAFTSPLG STGGKVFGEG TAAASAGGFG FGSSGNTASF GTLASQNAPT
FGSLSQQTSG FGTPSSGFAG FGSGTGAFTF GSSNSSVQGF GGWRS
