NXF1_DROME
ID NXF1_DROME Reviewed; 672 AA.
AC Q9U1H9; Q9NFQ2; Q9NFQ3; Q9VZ65; Q9VZ68;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Nuclear RNA export factor 1 {ECO:0000305|PubMed:11780634};
DE AltName: Full=Protein small bristles {ECO:0000303|PubMed:11780634};
DE AltName: Full=Protein tip-associating {ECO:0000312|FlyBase:FBgn0003321};
GN Name=sbr {ECO:0000303|PubMed:11780634, ECO:0000312|FlyBase:FBgn0003321};
GN Synonyms=nxf1 {ECO:0000303|PubMed:11780633};
GN ORFNames=CG1664 {ECO:0000312|FlyBase:FBgn0003321};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=11780634;
RA Wilkie G.S., Zimyanin V., Kirby R., Korey C., Francis-Lang H.,
RA Van Vactor D., Davis I.;
RT "Small bristles, the Drosophila ortholog of NXF-1, is essential for mRNA
RT export throughout development.";
RL RNA 7:1781-1792(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R;
RX PubMed=11779805; DOI=10.1093/genetics/159.4.1659;
RA Korey C., Wilkie G., Davis I., Van Vactor D.;
RT "small bristles is required for the morphogenesis of multiple tissues
RT during Drosophila development.";
RL Genetics 159:1659-1670(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE, FUNCTION, AND INTERACTION WITH NXT1.
RC TISSUE=Embryo;
RX PubMed=11780633;
RA Herold A., Klymenko T., Izaurralde E.;
RT "NXF1/p15 heterodimers are essential for mRNA nuclear export in
RT Drosophila.";
RL RNA 7:1768-1780(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-672.
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [7]
RP IDENTIFICATION IN A COMPLEX WITH NUP358; RANGAP AND NXT1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14729961; DOI=10.1128/mcb.24.3.1155-1167.2004;
RA Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R.,
RA Bork P., Ellenberg J., Izaurralde E.;
RT "RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the
RT nuclear pore complex and functions in nuclear mRNA export.";
RL Mol. Cell. Biol. 24:1155-1167(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [9]
RP INTERACTION WITH ZC3H3.
RX PubMed=19364924; DOI=10.1083/jcb.200811072;
RA Hurt J.A., Obar R.A., Zhai B., Farny N.G., Gygi S.P., Silver P.A.;
RT "A conserved CCCH-type zinc finger protein regulates mRNA nuclear
RT adenylation and export.";
RL J. Cell Biol. 185:265-277(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH ORC3 AND HPR1.
RX PubMed=27016737; DOI=10.1093/nar/gkw192;
RA Kopytova D., Popova V., Kurshakova M., Shidlovskii Y., Nabirochkina E.,
RA Brechalov A., Georgiev G., Georgieva S.;
RT "ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association
RT with mRNP and mRNA export in Drosophila.";
RL Nucleic Acids Res. 44:4920-4933(2016).
RN [11]
RP INTERACTION WITH NXT1.
RX PubMed=31570835; DOI=10.1038/s41556-019-0396-0;
RA Zhao K., Cheng S., Miao N., Xu P., Lu X., Zhang Y., Wang M., Ouyang X.,
RA Yuan X., Liu W., Lu X., Zhou P., Gu J., Zhang Y., Qiu D., Jin Z., Su C.,
RA Peng C., Wang J.H., Dong M.Q., Wan Y., Ma J., Cheng H., Huang Y., Yu Y.;
RT "A Pandas complex adapted for piRNA-guided transcriptional silencing and
RT heterochromatin formation.";
RL Nat. Cell Biol. 21:1261-1272(2019).
RN [12]
RP FUNCTION, AND INTERACTION WITH NUP58 AND NUP54.
RX PubMed=33856346; DOI=10.7554/elife.66321;
RA Munafo M., Lawless V.R., Passera A., MacMillan S., Borneloev S.,
RA Haussmann I.U., Soller M., Hannon G.J., Czech B.;
RT "Channel Nuclear Pore Complex subunits are required for transposon
RT silencing in Drosophila.";
RL Elife 10:0-0(2021).
CC -!- FUNCTION: Mediates the export of the majority of mRNAs from the nucleus
CC to the cytoplasm (PubMed:11779805, PubMed:11780633, PubMed:11780634,
CC PubMed:27016737). In ovarian follicle cells, plays a role in
CC transposable element silencing regulation by enabling the nuclear
CC export of flamenco (flam) transcripts and subsequent piRNA biogenesis
CC (PubMed:33856346). {ECO:0000269|PubMed:11779805,
CC ECO:0000269|PubMed:11780633, ECO:0000269|PubMed:11780634,
CC ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:33856346}.
CC -!- SUBUNIT: Interacts with Nxt1 (PubMed:11780633, PubMed:31570835).
CC Interacts with ZC3H3 (PubMed:19364924). Forms a complex with
CC Nup358/RanBP2, RanGAP and Nxt1 (PubMed:14729961). Interacts with Nup54
CC and Nup58 (PubMed:33856346). Interacts with Orc3 and Hpr1
CC (PubMed:27016737). {ECO:0000269|PubMed:11780633,
CC ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:19364924,
CC ECO:0000269|PubMed:27016737, ECO:0000269|PubMed:31570835,
CC ECO:0000269|PubMed:33856346}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:14729961}. Cytoplasm {ECO:0000269|PubMed:14729961}.
CC Nucleus envelope {ECO:0000269|PubMed:14729961}. Note=Localized 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 {ECO:0000269|PubMed:14729961}.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout embryonic development.
CC {ECO:0000269|PubMed:11779805}.
CC -!- DOMAIN: The leucine-rich repeats and the NTF2-domain are essential for
CC the export of mRNA from the nucleus.
CC -!- DOMAIN: The C-terminal fragment, containing the TAP domain (also called
CC UBA-like domain) and part of the NTF2-like domain, named the NPC-
CC binding domain, mediates direct interactions with nucleoporin-FG-
CC repeats and is necessary and sufficient for localization of NXF1 to the
CC nuclear rim.
CC -!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
CC -!- MISCELLANEOUS: Mutations affect the morphogenesis of embryonic neurons,
CC embryonic muscle and adult sensory bristles. This is thought to be due
CC to reduced rate of protein synthesis as the mRNA is not efficiently
CC being exported out of the nucleus.
CC -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL39560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB75848.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ251947; CAB64382.2; -; mRNA.
DR EMBL; AJ272389; CAB75848.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ272390; CAB75849.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AJ318090; CAC41645.1; -; mRNA.
DR EMBL; AE014298; AAF47959.3; -; Genomic_DNA.
DR EMBL; AY069415; AAL39560.1; ALT_INIT; mRNA.
DR RefSeq; NP_524660.1; NM_079921.3.
DR PDB; 6IHJ; X-ray; 2.70 A; A/C=359-544.
DR PDBsum; 6IHJ; -.
DR AlphaFoldDB; Q9U1H9; -.
DR SMR; Q9U1H9; -.
DR BioGRID; 68734; 21.
DR DIP; DIP-21726N; -.
DR IntAct; Q9U1H9; 4.
DR STRING; 7227.FBpp0073267; -.
DR iPTMnet; Q9U1H9; -.
DR PaxDb; Q9U1H9; -.
DR PRIDE; Q9U1H9; -.
DR EnsemblMetazoa; FBtr0073411; FBpp0073267; FBgn0003321.
DR GeneID; 43944; -.
DR KEGG; dme:Dmel_CG1664; -.
DR CTD; 43944; -.
DR FlyBase; FBgn0003321; sbr.
DR VEuPathDB; VectorBase:FBgn0003321; -.
DR eggNOG; KOG3763; Eukaryota.
DR GeneTree; ENSGT00390000007539; -.
DR HOGENOM; CLU_011280_1_1_1; -.
DR InParanoid; Q9U1H9; -.
DR OMA; YGGHEAW; -.
DR OrthoDB; 1051093at2759; -.
DR PhylomeDB; Q9U1H9; -.
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 SignaLink; Q9U1H9; -.
DR BioGRID-ORCS; 43944; 1 hit in 3 CRISPR screens.
DR GenomeRNAi; 43944; -.
DR PRO; PR:Q9U1H9; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003321; Expressed in spermathecum and 20 other tissues.
DR ExpressionAtlas; Q9U1H9; baseline and differential.
DR Genevisible; Q9U1H9; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006406; P:mRNA export from nucleus; IMP:FlyBase.
DR GO; GO:0051168; P:nuclear export; IMP:FlyBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:FlyBase.
DR GO; GO:0046833; P:positive regulation of RNA export from nucleus; IMP:UniProtKB.
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; 2.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Leucine-rich repeat; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transport.
FT CHAIN 1..672
FT /note="Nuclear RNA export factor 1"
FT /id="PRO_0000220538"
FT DOMAIN 113..193
FT /note="RRM"
FT REPEAT 255..280
FT /note="LRR 1"
FT REPEAT 281..304
FT /note="LRR 2"
FT REPEAT 305..332
FT /note="LRR 3"
FT REPEAT 333..360
FT /note="LRR 4"
FT DOMAIN 375..529
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 618..672
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 561
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 292
FT /note="I -> V (in Ref. 2; CAB75848)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="K -> KR (in Ref. 2; CAB75849)"
FT /evidence="ECO:0000305"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 373..388
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 399..408
FT /evidence="ECO:0007829|PDB:6IHJ"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:6IHJ"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:6IHJ"
FT TURN 438..441
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 446..454
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 478..488
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 504..515
FT /evidence="ECO:0007829|PDB:6IHJ"
FT STRAND 517..531
FT /evidence="ECO:0007829|PDB:6IHJ"
FT HELIX 534..541
FT /evidence="ECO:0007829|PDB:6IHJ"
SQ SEQUENCE 672 AA; 76249 MW; FADEF8B6DA7B7F5F CRC64;
MPKRGGGSSQ RYNNNVGNGG GRYNAPEDFD DFDVEDRQRR KDRNKRRVSF KPSQCLHNKK
DIKLRPEDLR RWDEDDDMSD MTTAVKDRPT SRRRGSPIPR GKFGKLMPNS FGWYQVTLQN
AQIYEKETLL SALLAAMSPH VFIPQYWRVE RNCVIFFTDD YEAAERIQHL GKNGHLPDGY
RLMPRVRSGI PLVAIDDAFK EKMKVTMAKR YNIQTKALDL SRFHADPDLK QVFCPLFRQN
VMGAAIDIMC DNIPDLEALN LNDNSISSME AFKGVEKRLP NLKILYLGDN KIPSLAHLVV
LRNLSILELV LKNNPCRSRY KDSQQFISEV RRKFPKLVKL DGETLEPQIT FDLSEQGRLL
ETKASYLCDV AGAEVVRQFL DQYFRIFDSG NRQALLDAYH EKAMLSISMP SASQAGRLNS
FWKFNRNLRR LLNGEENRTR NLKYGRLACV STLDEWPKTQ HDRRTFTVDL TIYNTSMMVF
TVTGLFKELN DETNNPASME LYDVRHFART YVVVPQNNGF CIRNETIFIT NATHEQVREF
KRSQHQPAPG AMPSTSSAVT SPQAGAAAGL QGRLNALGVA TGPVAILSGD PLAATAPVNS
GSAAISTTAV APGAQDESTK MQMIEAMSAQ SQMNVIWSRK CLEETNWDFN HAAFVFEKLF
KENKIPPEAF MK
