NUP98_MOUSE
ID NUP98_MOUSE Reviewed; 1816 AA.
AC Q6PFD9; Q68G59;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nuclear pore complex protein Nup98-Nup96;
DE EC=3.4.21.- {ECO:0000250|UniProtKB:P52948};
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup98;
DE AltName: Full=98 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup98;
DE Short=Nup98;
DE Contains:
DE RecName: Full=Nuclear pore complex protein Nup96;
DE AltName: Full=96 kDa nucleoporin;
DE AltName: Full=Nucleoporin Nup96;
DE Short=Nup96;
DE Flags: Precursor;
GN Name=Nup98;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-888 AND SER-1027, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653; THR-670 AND SER-888, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-612; SER-618;
RP SER-623; SER-653; SER-680; SER-888; SER-1027; SER-1059; SER-1063; SER-1328
RP AND THR-1771, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 732-880 IN COMPLEX WITH YEAST
RP NUP82 AND NUP159, INTERACTION WITH NUP88, MUTAGENESIS OF LYS-831, AND
RP SUBUNIT.
RX PubMed=22480613; DOI=10.1016/j.jmb.2012.03.024;
RA Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.;
RT "Molecular basis for the anchoring of proto-oncoprotein Nup98 to the
RT cytoplasmic face of the nuclear pore complex.";
RL J. Mol. Biol. 419:330-346(2012).
CC -!- FUNCTION: Plays a role in the nuclear pore complex (NPC) assembly
CC and/or maintenance. NUP98 and NUP96 are involved in the bidirectional
CC transport across the NPC. May anchor NUP153 and TPR to the NPC. In
CC cooperation with DHX9, plays a role in transcription and alternative
CC splicing activation of a subset of genes. Involved in the localization
CC of DHX9 in discrete intranuclear foci (GLFG-body).
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- SUBUNIT: Part of the nuclear pore complex (NPC). Interacts directly
CC with NUP96. Part of the Nup160 subcomplex in the nuclear pore which is
CC composed of NUP160, NUP133, NUP107 and NUP96; this complex plays a role
CC in RNA export and in tethering NUP98 and NUP153 to the nucleus.
CC Interacts with RAE1. Does not interact with TPR (By similarity).
CC Interacts directly with NUP88 and NUP214, subunits of the cytoplasmic
CC filaments of the NPC (PubMed:22480613). Interacts (via N-terminus) with
CC DHX9 (via DRBM, OB-fold and RGG domains); this interaction occurs in a
CC RNA-dependent manner and stimulates DHX9-mediated ATPase activity (By
CC similarity). {ECO:0000250|UniProtKB:P52948,
CC ECO:0000269|PubMed:22480613}.
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P52948};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P52948};
CC Nucleoplasmic side {ECO:0000250|UniProtKB:P52948}. Nucleus, nuclear
CC pore complex {ECO:0000250|UniProtKB:P52948}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:P52948}. Note=Localized to the nucleoplasmic
CC side of the nuclear pore complex (NPC), at or near the nucleoplasmic
CC basket. Dissociates from the dissasembled NPC structure early during
CC prophase of mitosis. Colocalized with NUP153 and TPR to the nuclear
CC basket of NPC. Colocalized with DHX9 in diffuse and discrete
CC intranuclear foci (GLFG-body). Remains localized to the nuclear
CC membrane after poliovirus (PV) infection.
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- DOMAIN: Contains G-L-F-G repeats. The FG repeat domains have a direct
CC role in the transport (By similarity). {ECO:0000250}.
CC -!- PTM: Autoproteolytically cleaved to yield Nup98 and Nup96 or Nup98
CC only, respectively. Cleaved Nup98 is necessary for the targeting of
CC Nup98 to the nuclear pore and the interaction with Nup96.
CC {ECO:0000250|UniProtKB:P52948}.
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50911.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH57608.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI12913.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AC118592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050911; AAH50911.1; ALT_SEQ; mRNA.
DR EMBL; BC057608; AAH57608.1; ALT_SEQ; mRNA.
DR EMBL; BC078630; AAH78630.1; -; mRNA.
DR EMBL; BC112912; AAI12913.1; ALT_SEQ; mRNA.
DR CCDS; CCDS85358.1; -.
DR RefSeq; NP_001274093.1; NM_001287164.1.
DR RefSeq; NP_001274094.1; NM_001287165.1.
DR RefSeq; NP_075355.1; NM_022979.2.
DR PDB; 3TKN; X-ray; 3.40 A; C/F/I=732-880.
DR PDB; 7BYF; X-ray; 2.50 A; B/E=157-213.
DR PDBsum; 3TKN; -.
DR PDBsum; 7BYF; -.
DR AlphaFoldDB; Q6PFD9; -.
DR SMR; Q6PFD9; -.
DR BioGRID; 234738; 66.
DR ComplexPortal; CPX-4474; Nuclear pore complex.
DR IntAct; Q6PFD9; 59.
DR MINT; Q6PFD9; -.
DR STRING; 10090.ENSMUSP00000068530; -.
DR MEROPS; S59.001; -.
DR iPTMnet; Q6PFD9; -.
DR PhosphoSitePlus; Q6PFD9; -.
DR SwissPalm; Q6PFD9; -.
DR EPD; Q6PFD9; -.
DR jPOST; Q6PFD9; -.
DR MaxQB; Q6PFD9; -.
DR PaxDb; Q6PFD9; -.
DR PeptideAtlas; Q6PFD9; -.
DR PRIDE; Q6PFD9; -.
DR ProteomicsDB; 287864; -.
DR DNASU; 269966; -.
DR GeneID; 269966; -.
DR KEGG; mmu:269966; -.
DR UCSC; uc009iqx.2; mouse.
DR CTD; 4928; -.
DR MGI; MGI:109404; Nup98.
DR eggNOG; KOG0845; Eukaryota.
DR InParanoid; Q6PFD9; -.
DR OrthoDB; 93359at2759; -.
DR TreeFam; TF343335; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
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-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
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-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 Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 269966; 8 hits in 42 CRISPR screens.
DR ChiTaRS; Nup98; mouse.
DR PRO; PR:Q6PFD9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6PFD9; protein.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; ISO:MGI.
DR GO; GO:0005643; C:nuclear pore; ISO:MGI.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISO:MGI.
DR GO; GO:0031080; C:nuclear pore outer ring; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISO:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0051292; P:nuclear pore complex assembly; ISO:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR InterPro; IPR021967; Nup98_C.
DR PANTHER; PTHR23198; PTHR23198; 1.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 1.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF12110; Nup96; 1.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Autocatalytic cleavage; Hydrolase;
KW Isopeptide bond; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protease; Protein transport; Reference proteome; Repeat;
KW Serine protease; Translocation; Transport; Ubl conjugation.
FT CHAIN 1..880
FT /note="Nuclear pore complex protein Nup98"
FT /id="PRO_0000421837"
FT CHAIN 881..1816
FT /note="Nuclear pore complex protein Nup96"
FT /id="PRO_0000421838"
FT DOMAIN 738..880
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..156
FT /note="FG repeats 1"
FT REGION 157..213
FT /note="GLEBS; interaction with RAE1"
FT /evidence="ECO:0000250"
FT REGION 214..480
FT /note="FG repeats 2"
FT REGION 512..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 881
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT SITE 880..881
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 603
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 670
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 934
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1069
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1771
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 563
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT CROSSLNK 603
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT CROSSLNK 665
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P52948"
FT MUTAGEN 831
FT /note="K->A: Reduces interaction with NUP88."
FT /evidence="ECO:0000269|PubMed:22480613"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:7BYF"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:7BYF"
FT TURN 193..197
FT /evidence="ECO:0007829|PDB:7BYF"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:7BYF"
FT STRAND 741..745
FT /evidence="ECO:0007829|PDB:3TKN"
FT HELIX 749..752
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 763..769
FT /evidence="ECO:0007829|PDB:3TKN"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 773..780
FT /evidence="ECO:0007829|PDB:3TKN"
FT HELIX 788..790
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 792..795
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 798..807
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 813..815
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 819..823
FT /evidence="ECO:0007829|PDB:3TKN"
FT TURN 831..833
FT /evidence="ECO:0007829|PDB:3TKN"
FT HELIX 840..845
FT /evidence="ECO:0007829|PDB:3TKN"
FT HELIX 848..857
FT /evidence="ECO:0007829|PDB:3TKN"
FT TURN 858..860
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 862..867
FT /evidence="ECO:0007829|PDB:3TKN"
FT TURN 868..871
FT /evidence="ECO:0007829|PDB:3TKN"
FT STRAND 872..878
FT /evidence="ECO:0007829|PDB:3TKN"
SQ SEQUENCE 1816 AA; 197241 MW; CEB86B4A447E9750 CRC64;
MFNKSFGTPF GGSTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG
GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTASTGTS LFSSQNNAFA QNKPTGFGNF
GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST
NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG GGTTAGLFGS SPATSSATGL
FSSSTTNSAF SYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTPNTGF
SFGNTSTLGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQPNTGFGAV
GSTLFGNNKL TTFGTSTTSA PSFGTTSGGL FGNKPTLTLG TNTNTSNFGF GTNNSGSSIF
GSKPAAGTLG TGLGTGFGTA LGAGQASLFG NNQPKIGGPL GTGAFGAPGF NTSTAILGFG
APQAPVALTD PNASAAQQAV LQQHLNSLTY SPFGDSPLFR NPMSDPKKKE ERLKPTNPAA
QKALTTPTHY KLTPRPATRV RPKALQTTGT AKSHLFDGLD DDEPSLANGA FMPKKSIKKL
VLKNLNNSNL FSPVNHDSED LASPSEYPEN GERFSFLSKP VDENNQQDGE DDSLVSRFYT
NPIAKPIPQT PESVGNKNNS SSNVEDTIVA LNMRAALRNG LEGSSEETSF HDESLQDDRE
EIENNAYHIH PAGIVLTKVG YYTIPSMDDL AKITNEKGEC IVSDFTIGRK GYGSIYFEGD
VNLTNLNLDD IVHIRRKEVI VYVDDNQKPP VGEGLNRKAE VTLDGVWPTD KTSRCLIKSP
DRLADINYEG RLEAVSRKQG AQFKEYRPET GSWVFKVSHF SKYGLQDSDE EEEEHPPKTT
SKKLKTAPLP PAGQATTFQM TLNGKPAPPP QSQSPEVEQL GRVVELDSDM VDITQEPVPD
SVLEESVPED QEPVSASTHI ASSLGINPHV LQIMKASLLV DEEDVDAMDQ RFGHIPSKGE
TVQEICSPRL PISASHSSKS RSIVGGLLQS KFASGTFLSP SASVQECRTP RTSSRMNIPS
TSPWSVPLPL ATVFTVPSPA PEVQLKTVGI RRQPGLVPLE KSITYGKGKL LMDMALFMGR
SFRVGWGPNW TLANSGEQLH GSHELENHQV ADSMEYGFLP NPVAVKSLSE SPFKVHLEKL
GLRQRKLDED LQLYQTPLEL KLKHSTVHVD ELCPLIVPNP GVSVIHDYAD WVKDSPGDFL
ELPIVKHWSL TWTLCEALWG HLKELDGQLD EPSEYIQTLE RRRAFSRWLS HTAAPQIEEE
VSLTRRDSPV EAVFSYLTGS RISGACCLAQ QSGDHRLALL LSQLVGSQSV RELLTMQLAD
WHQLQADSFI HDERLRIFAL LAGKPVWQLS EQKQINVCSQ LDWKRTLAIH LWYLLPPTAS
ISRALSMYEE AFQNTPEGDK YACSPLPSYL EGCGCMVEEE KDSRRPLQDV CFHLLKLYSD
RHYELNQLLE PRSITADPLD YRLSWHLWEV LRALNYTHLS EQCEGVLQAS YAGQLESEGL
WEWAIFVFLH IDNSGMREKA VRELLTRHCQ LSETPESWAK EAFLTQKLCV PAEWIHEAKA
VRAHMESNKH LEALYLFKAG HWNRCHKLVI RHLASDAIIN ENYDYLKGFL EDLAPPERSS
LIQDWETSGL VYLDYIRVIE MLHRIQQVDC SGYELEHLHT KVTSLCNRIE QIPCYNAKDR
LAQSDMAKRV ANLLRVVLSL QHAPDATSNS TPDPQRVPLR LLAPHIGRLP MPEDYALEEL
RGLTQSYLRE LTVGSQ
