NRX3A_MOUSE
ID NRX3A_MOUSE Reviewed; 1571 AA.
AC Q6P9K9; E9PW93; E9Q466; Q8CCT8;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Neurexin-3;
DE AltName: Full=Neurexin III-alpha;
DE AltName: Full=Neurexin-3-alpha;
DE Flags: Precursor;
GN Name=Nrxn3;
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] (ISOFORM 2A).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A).
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=19926856; DOI=10.1073/pnas.0809510106;
RA Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B.,
RA Cera M.R., Mascia L., Bussolino F., Arese M.;
RT "The synaptic proteins neurexins and neuroligins are widely expressed in
RT the vascular system and contribute to its functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Neuronal cell surface protein that may be involved in cell
CC recognition and cell adhesion. May mediate intracellular signaling (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: The laminin G-like domain 2 binds to NXPH1. Specific isoforms
CC bind to alpha-dystroglycan. The cytoplasmic C-terminal region binds to
CC CASK (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6P9K9; O14522: PTPRT; Xeno; NbExp=2; IntAct=EBI-7281557, EBI-728180;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Comment=A number of isoforms, alpha-type and beta-type are produced
CC by alternative promoter usage. Beta-type isoforms differ from
CC alpha-type isoforms in their N-terminus.;
CC Name=1a;
CC IsoId=Q6P9K9-1; Sequence=Displayed;
CC Name=2a;
CC IsoId=Q6P9K9-2; Sequence=VSP_041710, VSP_041711, VSP_041712;
CC Name=1b;
CC IsoId=Q8C985-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain and arteries (at protein level).
CC {ECO:0000269|PubMed:19926856}.
CC -!- MISCELLANEOUS: [Isoform 2a]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH60719.1; Type=Miscellaneous discrepancy; Note=Contains an insert which is not supported by any other transcript and which does not match with the genome.; Evidence={ECO:0000305};
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DR EMBL; AK032126; BAC27716.1; -; mRNA.
DR EMBL; AC115709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC115910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC155274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC171335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01025627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR974428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR974583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT009725; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU041252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060719; AAH60719.1; ALT_SEQ; mRNA.
DR CCDS; CCDS49134.1; -. [Q6P9K9-2]
DR CCDS; CCDS56856.1; -. [Q6P9K9-1]
DR RefSeq; NP_001185516.2; NM_001198587.3. [Q6P9K9-1]
DR RefSeq; NP_766132.2; NM_172544.3. [Q6P9K9-2]
DR RefSeq; XP_006515620.1; XM_006515557.1. [Q6P9K9-1]
DR PDB; 3MW4; X-ray; 2.00 A; A/B/C=1090-1293.
DR PDBsum; 3MW4; -.
DR AlphaFoldDB; Q6P9K9; -.
DR SMR; Q6P9K9; -.
DR BioGRID; 201853; 1.
DR IntAct; Q6P9K9; 2.
DR MINT; Q6P9K9; -.
DR STRING; 10090.ENSMUSP00000129678; -.
DR GlyConnect; 2541; 3 N-Linked glycans (3 sites).
DR GlyGen; Q6P9K9; 6 sites, 3 N-linked glycans (3 sites).
DR iPTMnet; Q6P9K9; -.
DR PhosphoSitePlus; Q6P9K9; -.
DR MaxQB; Q6P9K9; -.
DR PaxDb; Q6P9K9; -.
DR PeptideAtlas; Q6P9K9; -.
DR PRIDE; Q6P9K9; -.
DR ProteomicsDB; 293974; -. [Q6P9K9-1]
DR ProteomicsDB; 293975; -. [Q6P9K9-2]
DR Antibodypedia; 106; 252 antibodies from 31 providers.
DR DNASU; 18191; -.
DR Ensembl; ENSMUST00000057634; ENSMUSP00000050075; ENSMUSG00000066392. [Q6P9K9-2]
DR Ensembl; ENSMUST00000163134; ENSMUSP00000129678; ENSMUSG00000066392. [Q6P9K9-1]
DR Ensembl; ENSMUST00000167887; ENSMUSP00000127926; ENSMUSG00000066392. [Q6P9K9-2]
DR GeneID; 18191; -.
DR KEGG; mmu:18191; -.
DR UCSC; uc007okc.2; mouse. [Q6P9K9-2]
DR UCSC; uc033ger.1; mouse. [Q6P9K9-1]
DR CTD; 9369; -.
DR MGI; MGI:1096389; Nrxn3.
DR VEuPathDB; HostDB:ENSMUSG00000066392; -.
DR eggNOG; KOG3514; Eukaryota.
DR GeneTree; ENSGT00940000154618; -.
DR HOGENOM; CLU_001710_0_1_1; -.
DR InParanoid; Q6P9K9; -.
DR OMA; MFHNIPT; -.
DR OrthoDB; 35129at2759; -.
DR PhylomeDB; Q6P9K9; -.
DR TreeFam; TF321302; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 18191; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Nrxn3; mouse.
DR EvolutionaryTrace; Q6P9K9; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6P9K9; protein.
DR Bgee; ENSMUSG00000066392; Expressed in rostral migratory stream and 189 other tissues.
DR ExpressionAtlas; Q6P9K9; baseline and differential.
DR Genevisible; Q6P9K9; MM.
DR GO; GO:0098982; C:GABA-ergic synapse; IMP:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; ISA:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IMP:SynGO.
DR GO; GO:0035176; P:social behavior; ISO:MGI.
DR GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR GO; GO:0071625; P:vocalization behavior; ISO:MGI.
DR CDD; cd00110; LamG; 6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR InterPro; IPR027789; Syndecan/Neurexin_dom.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR Pfam; PF01034; Syndecan; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing; Calcium;
KW Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..1571
FT /note="Neurexin-3"
FT /id="PRO_0000412557"
FT TOPO_DOM 28..1496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1497..1517
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1518..1571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..202
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 198..235
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 258..440
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 447..639
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 643..680
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 685..857
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 871..1046
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1049..1086
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1090..1290
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1324..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1553..1571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 374
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 202..213
FT /evidence="ECO:0000250"
FT DISULFID 207..222
FT /evidence="ECO:0000250"
FT DISULFID 224..234
FT /evidence="ECO:0000250"
FT DISULFID 404..440
FT /evidence="ECO:0000250"
FT DISULFID 610..639
FT /evidence="ECO:0000250"
FT DISULFID 647..658
FT /evidence="ECO:0000250"
FT DISULFID 652..667
FT /evidence="ECO:0000250"
FT DISULFID 669..679
FT /evidence="ECO:0000250"
FT DISULFID 1018..1046
FT /evidence="ECO:0000250"
FT DISULFID 1053..1064
FT /evidence="ECO:0000250"
FT DISULFID 1058..1073
FT /evidence="ECO:0000250"
FT DISULFID 1075..1085
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..373
FT /note="Missing (in isoform 2a)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041710"
FT VAR_SEQ 1047
FT /note="E -> EVALTKADLQ (in isoform 2a)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041711"
FT VAR_SEQ 1364..1470
FT /note="Missing (in isoform 2a)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_041712"
FT CONFLICT 390
FT /note="A -> T (in Ref. 1; BAC27716)"
FT /evidence="ECO:0000305"
FT STRAND 1091..1104
FT /evidence="ECO:0007829|PDB:3MW4"
FT HELIX 1107..1109
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1113..1123
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1127..1137
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1143..1149
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1152..1162
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1164..1167
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1175..1177
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1179..1186
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1189..1194
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1200..1202
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1245..1252
FT /evidence="ECO:0007829|PDB:3MW4"
FT HELIX 1253..1255
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1261..1268
FT /evidence="ECO:0007829|PDB:3MW4"
FT HELIX 1273..1278
FT /evidence="ECO:0007829|PDB:3MW4"
FT STRAND 1284..1293
FT /evidence="ECO:0007829|PDB:3MW4"
SQ SEQUENCE 1571 AA; 173428 MW; 98F989F5DD2B71AB CRC64;
MSFTLHSVFF TLKVSIFLGS LVGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETTVLS NKQVNDSSWH FLMVSRDRVR
TGLVIDGEGQ SGELRPQRPY MDVVSDLFLG GVPADIRPSA LTLDGVQSMP GFKGLMLDLK
YGNSEPRLLG SQSVQLEAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GTLCSEDVSQ
GPGLSHLMMS EQAREENVAT FRGSEYLCYD LSQNPIQSSS DEITLSFKTW QRNGLILHTG
KSADYVNLAL KDGAVSLVIN LGSGAFEAIV EPVNGKFNDN AWHDVKVTRN LRQVTISVDG
ILTTTGYTQE DYTMLGSDDF FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDIRLELS
RLARIGDTKM KIYGEVVFKC ENVATLDPIN FETPEAYISL PKWNTKRMGS ISFDFRTTEP
NGLILFTHGK PQERKDVRSQ KNTKVDFFAV ELLDGNLYLL LDMGSGTIKV KATQKKANDG
EWYHVDIQRD GRSGTISVNS RRTPFTASGE SEILDLEGDM YLGGLPENRA GLILPTELWT
AMLNYGYVGC IRDLFIDGRS KNIRQLAEMQ NAAGVKSSCS RMSAKQCDSY PCKNNAVCKD
GWNRFICDCT GTGYWGRTCE REASILSYDG SMYMKVIMPM VMHTEAEDVS FRFMSQRAYG
LLVATTSRDS ADTLRLELDG GRVKLMVNLD CIRINCNSSK GPETLYAGQK LNDNEWHTVR
VVRRGKSLKL TVDDDVAEGT MVGDHTRLEF HNIETGIMTE KRYISVVPSS FIGHLQSLMF
NGLLYIDLCK NGDIDYCELK ARFGLRNIIA DPVTFKTKSS YLTLATLQAY TSMHLFFQFK
TTSADGFILF NSGDGNDFIA VELVKGYIHY VFDLGNGPNV IKGNSDRPLN DNQWHNVVIT
RDSSNTHSLK VDTKVVTQVI NGAKNLDLKG DLYMAGLAQG MYSNLPKLVA SRDGFQGCLA
SVDLNGRLPD LINDALHRSG QIERGCEGPS TTCQEDSCAN QGVCMQQWEG FTCDCSMTSY
SGNQCNDPGA TYIFGKSGGL ILYTWPANDR PSTRSDRLAV GFSTTVKDGI LVRIDSAPGL
GDFLQLHIEQ GKIGVVFNIG TVDISIKEER TPVNDGKYHV VRFTRNGGNA TLQVDNWPVN
EHYPTGNTDN ERLQMVKQKI PFKYNRPVEE WLQEKGRQLT IFNTQAQIAI GGKDKGRLFQ
GQLSGLYYDG LKVLNMAAEN NPNIKINGSV RLVGEVPSVS GTTQTTSMPP EMSTTVMETT
TTMATTTTRK NRSTASIQPT SDDLVSSAEC SSDDEDFVEC EPSTDKSLST SIFEGGYKAH
APKWESKDFR PNKVSETSRT TTTSLSPELI RFTASSSSGM VPKLPAGKMN NRDLKPQPDI
VLLPLPTAYE LDSTKLKSPL ITSPMFRNVP TANPTEPGIR RVPGASEVIR ESSSTTGMVV
GIVAAAALCI LILLYAMYKY RNRDEGSYQV DETRNYISNS AQSNGTLMKE KQASSKSGHK
KQKNKDKEYY V
