NXF1_MOUSE
ID NXF1_MOUSE Reviewed; 618 AA.
AC Q99JX7; O88985; Q3TJA5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Nuclear RNA export factor 1;
DE AltName: Full=Tip-associated protein;
DE AltName: Full=Tip-associating protein;
DE AltName: Full=mRNA export factor TAP;
GN Name=Nxf1; Synonyms=Tap;
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 [MRNA].
RC TISSUE=Heart ventricle;
RA Tannoch V.J., Cormier-Regard S., Claycomb W.C.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP INTERACTION WITH ALYREF/THOC4.
RX PubMed=10786854; DOI=10.1017/s1355838200000078;
RA Stutz F., Bachi A., Doerks T., Braun I.C., Seraphin B., Wilm M., Bork P.,
RA Izaurralde E.;
RT "REF, an evolutionarily conserved family of hnRNP-like proteins, interacts
RT with TAP/Mex67p and participates in mRNA nuclear export.";
RL RNA 6:638-650(2000).
RN [6]
RP INTERACTION WITH THE EXON JUNCTION COMPLEX.
RX PubMed=12093754; DOI=10.1093/emboj/cdf345;
RA Lejeune F., Ishigaki Y., Li X., Maquat L.E.;
RT "The exon junction complex is detected on CBP80-bound but not eIF4E-bound
RT mRNA in mammalian cells: dynamics of mRNP remodeling.";
RL EMBO J. 21:3536-3545(2002).
RN [7]
RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16800626; DOI=10.1021/bi060474w;
RA Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G.,
RA Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C.,
RA Bigelow D.J.;
RT "Endogenously nitrated proteins in mouse brain: links to neurodegenerative
RT disease.";
RL Biochemistry 45:8009-8022(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Involved in the nuclear export of mRNA species bearing
CC retroviral constitutive transport elements (CTE) and in the export of
CC mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-
CC NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction
CC with ALYREF/THOC4 and THOC5 components of the TREX complex.
CC ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1
CC heterodimer for export. Also involved in nuclear export of m6A-
CC containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-
CC containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear
CC export. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- SUBUNIT: Heterodimer (via NTF2 domain) with NXT1 (By similarity). The
CC formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated
CC nuclear mRNA export (By similarity). Forms a complex with
CC RANBP2/NUP358, NXT1 and RANGAP1 (By similarity). Associates with the
CC exon junction complex (EJC) (PubMed:12093754). Associates with the
CC transcription/export (TREX) complex (By similarity). Found in a mRNA
CC complex with UPF3A and UPF3B (By similarity). Found in a post-splicing
CC complex with RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1 (By similarity).
CC Interacts (via N-terminus) with DHX9 (via N-terminus); this interaction
CC is direct and negatively regulates NXF1-mediated nuclear export of
CC constitutive transport element (CTE)-containing cellular mRNAs (By
CC similarity). Interacts with FYTTD1/UIF (By similarity). Interacts with
CC EIF4A3 (By similarity). Interacts with NUP42 (By similarity). Interacts
CC with ALYREF/THOC4 (PubMed:10786854). Interacts with CHTOP (By
CC similarity). Interacts with FRG1 (via N-terminus) (By similarity).
CC Interacts with LUZP4 (By similarity). Interacts with FMR1; the
CC interaction occurs in a mRNA-dependent and polyribosomes-independent
CC manner in the nucleus (By similarity). Interacts with CPSF6 (via N-
CC terminus); this interaction is direct (By similarity). Interacts with
CC RBM15 (By similarity). Interacts with RBM15B (By similarity). Interacts
CC with MCM3AP; this interaction is not mediated by RNA (By similarity).
CC Interacts with DDX3X (via C-terminus); this interaction may be partly
CC involved in DDX3X nuclear export and in NXF1 localization to stress
CC granules. Interacts with PABPC1/PABP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBU9, ECO:0000269|PubMed:10786854,
CC ECO:0000269|PubMed:12093754}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex
CC {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope
CC {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q9UBU9}. Note=Localized predominantly in the
CC nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the
CC nuclear pore complex. Shuttles between the nucleus and the cytoplasm.
CC Travels to the cytoplasm as part of the exon junction complex (EJC)
CC bound to mRNA. The association with the TREX complex seems to occur in
CC regions surrounding nuclear speckles known as perispeckles. Nucleus;
CC nuclear rim. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- DOMAIN: The minimal CTE binding domain consists of an RNP-type RNA
CC binding domain (RBD) and leucine-rich repeats.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The nucleoporin binding domain consists of a NTF2 domain (also
CC called NTF2-like domain) and a TAP-C domain (also called UBA-like
CC domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2
CC and the other in the TAP-C domain) which contribute to nucleoporin
CC association and act synergistically to export cellular mRNAs.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The NTF2 domain is functional only in the presence of NXT1 and
CC is essential for the export of mRNA from the nucleus. It inhibits RNA
CC binding activity through an intramolecular interaction with the N-
CC terminal RNA binding domain (RBD); the inhibition is removed by an
CC association with the TREX complex, specifically involving ALYREF/THOC4
CC and THOC5. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The TAP-C domain mediates direct interactions with nucleoporin-
CC FG-repeats and is necessary and sufficient for localization of NXF1 to
CC the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has
CC a critical role in the interaction with nucleoporins.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The leucine-rich repeats are essential for the export of mRNA
CC from the nucleus. {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
CC {ECO:0000250|UniProtKB:Q9UBU9}.
CC -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
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DR EMBL; AF093140; AAC63368.1; -; mRNA.
DR EMBL; AK133883; BAE21911.1; -; mRNA.
DR EMBL; AK167518; BAE39590.1; -; mRNA.
DR EMBL; CH466612; EDL33363.1; -; Genomic_DNA.
DR EMBL; BC005594; AAH05594.1; -; mRNA.
DR CCDS; CCDS29543.1; -.
DR RefSeq; NP_058093.2; NM_016813.2.
DR AlphaFoldDB; Q99JX7; -.
DR BMRB; Q99JX7; -.
DR SMR; Q99JX7; -.
DR BioGRID; 207282; 20.
DR STRING; 10090.ENSMUSP00000010241; -.
DR iPTMnet; Q99JX7; -.
DR PhosphoSitePlus; Q99JX7; -.
DR EPD; Q99JX7; -.
DR jPOST; Q99JX7; -.
DR MaxQB; Q99JX7; -.
DR PaxDb; Q99JX7; -.
DR PeptideAtlas; Q99JX7; -.
DR PRIDE; Q99JX7; -.
DR ProteomicsDB; 291930; -.
DR Antibodypedia; 4277; 308 antibodies from 36 providers.
DR DNASU; 53319; -.
DR Ensembl; ENSMUST00000010241; ENSMUSP00000010241; ENSMUSG00000010097.
DR GeneID; 53319; -.
DR KEGG; mmu:53319; -.
DR UCSC; uc008gmr.1; mouse.
DR CTD; 10482; -.
DR MGI; MGI:1858330; Nxf1.
DR VEuPathDB; HostDB:ENSMUSG00000010097; -.
DR eggNOG; KOG3763; Eukaryota.
DR GeneTree; ENSGT00390000007539; -.
DR HOGENOM; CLU_011280_2_0_1; -.
DR InParanoid; Q99JX7; -.
DR OMA; YGGHEAW; -.
DR OrthoDB; 1051093at2759; -.
DR PhylomeDB; Q99JX7; -.
DR TreeFam; TF314566; -.
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 BioGRID-ORCS; 53319; 29 hits in 73 CRISPR screens.
DR ChiTaRS; Nxf1; mouse.
DR PRO; PR:Q99JX7; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q99JX7; protein.
DR Bgee; ENSMUSG00000010097; Expressed in undifferentiated genital tubercle and 262 other tissues.
DR ExpressionAtlas; Q99JX7; baseline and differential.
DR Genevisible; Q99JX7; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:MGI.
DR GO; GO:0005643; C:nuclear pore; IDA:MGI.
DR GO; GO:0042272; C:nuclear RNA export factor complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0000346; C:transcription export complex; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:MGI.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IPI:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006405; P:RNA export from nucleus; IDA:MGI.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd14342; UBA_TAP-C; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR030217; NXF_fam.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR005637; TAP_C_dom.
DR InterPro; IPR015245; Tap_RNA-bd.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10662; PTHR10662; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF09162; Tap-RNA_bind; 1.
DR Pfam; PF03943; TAP_C; 1.
DR SMART; SM00804; TAP_C; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Leucine-rich repeat; Methylation; mRNA transport;
KW Nitration; Nuclear pore complex; Nucleus; Protein transport;
KW Reference proteome; Repeat; RNA-binding; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT CHAIN 2..618
FT /note="Nuclear RNA export factor 1"
FT /id="PRO_0000220530"
FT DOMAIN 118..197
FT /note="RRM"
FT REPEAT 265..290
FT /note="LRR 1"
FT REPEAT 291..314
FT /note="LRR 2"
FT REPEAT 315..342
FT /note="LRR 3"
FT REPEAT 343..370
FT /note="LRR 4"
FT DOMAIN 385..535
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 564..618
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..197
FT /note="Interaction with ALYREF/THOC4 and LUZP4"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT REGION 2..117
FT /note="RNA-binding (RBD)"
FT /evidence="ECO:0000250"
FT REGION 2..59
FT /note="Minor non-specific RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 60..117
FT /note="Major non-specific RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 60..117
FT /note="RNA binding"
FT /evidence="ECO:0000250"
FT MOTIF 66..99
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 82..109
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBU9"
FT MOD_RES 41
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 41
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 125
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0007744|PubMed:16800626"
FT CONFLICT 79
FT /note="N -> D (in Ref. 1; AAC63368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 618 AA; 70300 MW; 0556EF8553B4055F CRC64;
MADEGKSYNE HDDRVSFPQR RKKGRGPFRW KCGEGNRRSG RGGSGVQSSR FEEDDGDVAM
NDPQDGPRVR YNPYTNRPNR RGDGWHDRDR IHITVRRDRA PAERGGAGTS QDGTTKNWFK
ITIPYGRKYD KTWLLSMIQS KCSVPFNPIE FHYENTRAHF FVEDATTASA LKGVNHKIQD
RENRRISIII NASAPPYTVQ NELKPEQIEQ LKLIMSKRYD GNQQALDLKG LRSDPDLVAQ
NIDVVLNRRS CMAATLRIIE ENIPELLSLN LSSNRLYKLD DMSSIVQKAP NLKTLNLSGN
ELKTERELDK IKGLKLEELW LDRNPMCDNF GDQSSYISAI RERFPKLLRL DGHELPPPIS
FDVEAPTMLP PCKGSYFGTE NLKSLVLRFL QQYYVIYDSG DRQGLLYAYH DGACCSLSIP
YNPQNPVRKN LAEYVKDSRN VKKLKEPTQR FRLLKHTRLN VVAFLNELPK TQHDVNAFVV
DISAQTSTLL CFSVNGVFKE VDGKSRDSLR AFTRTFIAVP ASNSGLCIVN DELFVRNASP
EEIQRAFAMS APTPSSSPVP TLSPEQQEML QAFSTQSGMN LEWSQKCLQD NNWDYTRSAQ
AFTLLKAKGE IPEVAFMK
