ID NRX3A_RAT Reviewed; 1578 AA.
AC Q07310; Q07280; Q07311; Q07312; Q07313; Q07314;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=Neurexin-3;
DE AltName: Full=Neurexin III-alpha;
DE AltName: Full=Neurexin-3-alpha;
DE Flags: Precursor;
GN Name=Nrxn3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8341647; DOI=10.1073/pnas.90.14.6410;
RA Ushkaryov Y.A., Suedhof T.C.;
RT "Neurexin III alpha: extensive alternative splicing generates membrane-
RT bound and soluble forms.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6410-6414(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=7695896; DOI=10.1016/0896-6273(95)90306-2;
RA Ullrich B., Ushkaryov Y.A., Suedhof T.C.;
RT "Cartography of neurexins: more than 1000 isoforms generated by alternative
RT splicing and expressed in distinct subsets of neurons.";
RL Neuron 14:497-507(1995).
RN [3]
RP PROTEIN SEQUENCE OF N-TERMINUS, AND INTERACTION WITH NXPH1.
RX PubMed=9856994; DOI=10.1074/jbc.273.52.34716;
RA Missler M., Hammer R.E., Suedhof T.C.;
RT "Neurexophilin binding to alpha-neurexins. A single LNS domain functions as
RT an independently folding ligand-binding unit.";
RL J. Biol. Chem. 273:34716-34723(1998).
RN [4]
RP INTERACTION WITH CASK.
RX PubMed=8786425; DOI=10.1523/jneurosci.16-08-02488.1996;
RA Hata Y., Butz S., Suedhof T.C.;
RT "CASK: a novel dlg/PSD95 homolog with an N-terminal calmodulin-dependent
RT protein kinase domain identified by interaction with neurexins.";
RL J. Neurosci. 16:2488-2494(1996).
RN [5]
RP INTERACTION WITH ALPHA-DYSTROGLYCAN.
RX PubMed=11470830; DOI=10.1083/jcb.200105003;
RA Sugita S., Saito F., Tang J., Satz J., Campbell K., Suedhof T.C.;
RT "A stoichiometric complex of neurexins and dystroglycan in brain.";
RL J. Cell Biol. 154:435-445(2001).
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|UniProtKB:Q9CS84}.
CC -!- SUBUNIT: The laminin G-like domain 2 binds to NXPH1 (PubMed:9856994).
CC Isoform 8/alpha-4B binds to alpha-dystroglycan (PubMed:11470830). The
CC cytoplasmic C-terminal region binds to CASK (PubMed:8786425). Specific
CC isoforms bind neuroligins NLGN1, NLGN2 and NLGN3 (By similarity).
CC Interacts with CLSTN3 (By similarity). {ECO:0000250|UniProtKB:Q63376,
CC ECO:0000269|PubMed:11470830, ECO:0000269|PubMed:8786425,
CC ECO:0000269|PubMed:9856994}.
CC -!- SUBCELLULAR LOCATION: Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9CS84}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=19;
CC Comment=There are five major alternatively spliced sites, each of
CC which may be spliced in up to twelve different ways. Combinatorial
CC splicing at each of these five sites may lead to the generation of at
CC least 288 isoforms but for simplicity only individual splice events
CC are explicitly described below. Isoforms Alpha 5A to isoform Alpha 5H
CC lack the transmembrane domain. Experimental confirmation may be
CC lacking for some isoforms.;
CC Name=1; Synonyms=Alpha-5I;
CC IsoId=Q07310-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha-1B;
CC IsoId=Q07310-2; Sequence=VSP_003524;
CC Name=3; Synonyms=Alpha-1C;
CC IsoId=Q07310-3; Sequence=VSP_003521;
CC Name=4; Synonyms=Alpha-1D;
CC IsoId=Q07310-4; Sequence=VSP_003521, VSP_003524;
CC Name=5; Synonyms=Alpha-1E;
CC IsoId=Q07310-5; Sequence=VSP_003523;
CC Name=6; Synonyms=Alpha-1F;
CC IsoId=Q07310-6; Sequence=VSP_003522;
CC Name=7; Synonyms=Alpha-3B;
CC IsoId=Q07310-7; Sequence=VSP_003525;
CC Name=8; Synonyms=Alpha-4B;
CC IsoId=Q07310-8; Sequence=VSP_003526;
CC Name=9; Synonyms=Alpha-5A;
CC IsoId=Q07310-9; Sequence=VSP_003528, VSP_003529;
CC Name=10; Synonyms=Alpha-5B;
CC IsoId=Q07310-10; Sequence=VSP_003527, VSP_003528, VSP_003529;
CC Name=11; Synonyms=Alpha-5C;
CC IsoId=Q07310-11; Sequence=VSP_003528, VSP_003530;
CC Name=12; Synonyms=Alpha-5D;
CC IsoId=Q07310-12; Sequence=VSP_003527, VSP_003528, VSP_003530;
CC Name=13; Synonyms=Alpha-5E;
CC IsoId=Q07310-13; Sequence=VSP_003528, VSP_003531;
CC Name=14; Synonyms=Alpha-5F;
CC IsoId=Q07310-14; Sequence=VSP_003527, VSP_003528, VSP_003531;
CC Name=15; Synonyms=Alpha-5G;
CC IsoId=Q07310-15; Sequence=VSP_003528, VSP_003532;
CC Name=16; Synonyms=Alpha-5H;
CC IsoId=Q07310-16; Sequence=VSP_003527, VSP_003528, VSP_003532;
CC Name=17; Synonyms=Alpha-5J;
CC IsoId=Q07310-17; Sequence=VSP_003527;
CC Name=18; Synonyms=Alpha-5K;
CC IsoId=Q07310-18; Sequence=VSP_003528;
CC Name=19; Synonyms=Alpha-5L;
CC IsoId=Q07310-19; Sequence=VSP_003527, VSP_003528;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- PTM: O-glycosylated; contains heparan sulfate. Heparan sulfate
CC attachment is required for synapse development by mediating
CC interactions with neuroligins. {ECO:0000250|UniProtKB:Q6P9K9}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; L14851; AAA02853.1; -; mRNA.
DR EMBL; L14851; AAA02854.1; -; mRNA.
DR EMBL; L14851; AAA02855.1; -; mRNA.
DR EMBL; L14851; AAA02856.1; -; mRNA.
DR EMBL; L14851; AAA02857.1; -; mRNA.
DR EMBL; L14851; AAA02858.1; -; mRNA.
DR PIR; I48216; I48216.
DR RefSeq; NP_446269.2; NM_053817.2.
DR AlphaFoldDB; Q07310; -.
DR SMR; Q07310; -.
DR BioGRID; 250475; 3.
DR ELM; Q07310; -.
DR IntAct; Q07310; 1.
DR MINT; Q07310; -.
DR STRING; 10116.ENSRNOP00000060600; -.
DR GlyCosmos; Q07310; 7 sites, No reported glycans.
DR GlyGen; Q07310; 8 sites.
DR iPTMnet; Q07310; -.
DR PhosphoSitePlus; Q07310; -.
DR PaxDb; 10116-ENSRNOP00000060655; -.
DR GeneID; 116508; -.
DR KEGG; rno:116508; -.
DR UCSC; RGD:620212; rat. [Q07310-1]
DR AGR; RGD:620212; -.
DR CTD; 9369; -.
DR RGD; 620212; Nrxn3.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; Q07310; -.
DR OrthoDB; 2999458at2759; -.
DR PhylomeDB; Q07310; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR GO; GO:0007612; P:learning; ISO:RGD.
DR GO; GO:0099645; P:neurotransmitter receptor localization to postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0007269; P:neurotransmitter secretion; ISO:RGD.
DR GO; GO:0097107; P:postsynaptic density assembly; ISO:RGD.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISO:RGD.
DR GO; GO:0099537; P:trans-synaptic signaling; ISO:RGD.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00110; LamG; 6.
DR Gene3D; 2.60.120.200; -; 6.
DR Gene3D; 2.10.25.10; Laminin; 3.
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 PANTHER; PTHR15036:SF57; NEUREXIN-3; 1.
DR PANTHER; PTHR15036; PIKACHURIN-LIKE PROTEIN; 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; Concanavalin A-like lectins/glucanases; 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 Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Heparan sulfate; Membrane; Metal-binding;
KW Proteoglycan; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:9856994"
FT CHAIN 28..1578
FT /note="Neurexin-3"
FT /id="PRO_0000019500"
FT TOPO_DOM 28..1503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1504..1524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1525..1578
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 260..444
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 451..643
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 647..684
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 689..861
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 875..1050
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1053..1090
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1094..1294
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1328..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 308
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q28146"
FT BINDING 325
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q28146"
FT BINDING 378
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q28146"
FT BINDING 736
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q28146"
FT BINDING 753
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q28146"
FT BINDING 811
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q28146"
FT BINDING 1146
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT BINDING 1163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT BINDING 1245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
FT BINDING 1247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9CS84"
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 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1351
FT /note="O-linked (Xyl...) (heparan sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:Q8C985"
FT CARBOHYD 1500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 202..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 207..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 224..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 408..444
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 614..643
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 651..662
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 656..671
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 673..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1022..1050
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1057..1068
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1062..1077
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1079..1089
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 237..256
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_003522"
FT VAR_SEQ 237..242
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003521"
FT VAR_SEQ 243..256
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_003523"
FT VAR_SEQ 253..256
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_003524"
FT VAR_SEQ 754..763
FT /note="DCIRINCNSS -> G (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_003525"
FT VAR_SEQ 1210..1239
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_003526"
FT VAR_SEQ 1369..1371
FT /note="Missing (in isoform 10, isoform 12, isoform 14,
FT isoform 16, isoform 17 and isoform 19)"
FT /evidence="ECO:0000305"
FT /id="VSP_003527"
FT VAR_SEQ 1372..1478
FT /note="Missing (in isoform 9, isoform 10, isoform 11,
FT isoform 12, isoform 13, isoform 14, isoform 15, isoform 16,
FT isoform 18 and isoform 19)"
FT /evidence="ECO:0000305"
FT /id="VSP_003528"
FT VAR_SEQ 1479..1578
FT /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> VLERRII
FT LNLKTNAHPKSLQSKTC (in isoform 11 and isoform 12)"
FT /evidence="ECO:0000305"
FT /id="VSP_003530"
FT VAR_SEQ 1479..1578
FT /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> DILLKSF
FT (in isoform 13 and isoform 14)"
FT /evidence="ECO:0000305"
FT /id="VSP_003531"
FT VAR_SEQ 1479..1578
FT /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> ATTTTKK
FT SNFQECGNSICPRAFLHNFLL (in isoform 15 and isoform 16)"
FT /evidence="ECO:0000305"
FT /id="VSP_003532"
FT VAR_SEQ 1479..1578
FT /note="ANPTEPGIRRVPGASEVIRESNSTTGMVVGIVAAAALCILILLYAMYKYRNR
FT DEGSYQVDETRNYISNSAQSNGTLMKEKQASSKSGHKKQKNKDKEYYV -> ARSSNAA
FT RITPCRPYMDMATHLHIYPSHLHLLCSTLIDTPLPFPHPFFPMLPPSLALLKFMCCHPP
FT P (in isoform 9 and isoform 10)"
FT /evidence="ECO:0000305"
FT /id="VSP_003529"
SQ SEQUENCE 1578 AA; 173994 MW; 936CF8529143D0C7 CRC64;
MSFTLHSVFF TLKVSSFLGS LVGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETTVLS NKQVNDSSWH FLMVSRDRVR
TGLVIDGEGQ SGELRAQRPY MDVVSDLFLG GGPADIRPSA LTLDGVQNMP GFKGLMLDLK
YGNSEPRLLG SQSVQLEAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GTLCSEDVSQ
GPGLSHLMMS EQGRSKAREE NVATFRGSEY LSYDLSQNPI QSSSSEITLS FKTWQRNGLI
LHTGKSADYV NLALKDGAVS LVINLGSGAF EAIVEPVNGK FNDNAWHDVK VTRNLRQVTI
SVDGILTTTG YTQEDYTMLG SDDSSYVGPS PSTADLPGSP VSNNFMGCLK EVVYKNNDIR
LELSRLARIG ATKMKIYGEV VFKCENVATL DPINFETPEA YISLPKWNTK RMGSISFDFR
TTEPNGLILL THGKPQERKD VRSQKNTKVD FFAVELLDGN LYLLLDMGSG TIKVKATQKK
ANDGEWYHVD IQRDGRSGTI SVNSRRTPFT ASGQSEILDL EGDMYLGGLP ENRAGLILPT
ELWTAMLNYG YVGCIRDLFI DGRSKNIRQL AEMQNAAGVK SSCSRMSAKQ CDSYPCKNNA
VCKDGWNRFI CDCTGTGYWG RTCEREASIL SYDGSMYMKV IMPMVMHTEA EDVSFRFMSQ
RAYGLLVATT SRDSADTLRL ELDGGRVKLM VNLDCIRINC NSSKGPETLY AGQKLNDNEW
HTVRVVRRGK SLKLTVDDDV AEGTMVGDHT RLEFHNIETG IMTEKRYISV VPSSFIGHLQ
SLMFNGLLYI DLCKNGDIDY CELKARFGLR NIIADPVTFK TKSSYLTLAT LQAYTSMHLF
FQFKTTSADG FILFNSGDGN NFIAVELVKG YIHYVFDLGN GPNVIKGNSD RPLNDNQWHN
VVITRDNSNT HSLKVDTKVV TQVINGAKNL DLKGDLYMAG LAQGMYSNLP KLVASRDGFQ
GCLASVDLNG RLPDLINDAL HRSGQIDRGC EGPSTTCQED SCANQGVCMQ QWEGFTCDCS
MTSYSGNQCN DPGATYIFGK SGGLILYTWP ANDRPSTRSD RLAVGFSTTV KDGVLVRIDS
APGLGDFLQL HIEQGKIGVV FNIGTVDISI KEERTPVNDG KYHVVRFTRN GANATLQVDN
WPVNEHYPTG NTDNERRQMV KQKIPFKYNR PVEEWLQEKG RQLTIFNTQA QIAIGGKDKG
RLFQGQLSGL YYDGLKVLNM AAENNPNIKI NGSVRLVGEV PSVSGTTHTT SMPPEMSTTV
METTTTMATT TTRKNRSTAS IQPTSDDLVS SAECSSDDED FVECEPSTGR SDKSLSTSIF
EGGYKAHAPK WESKDFRPNK VSETSRTTTT SLSPELIRFT ASSSSGMVPK LPAGKMNNRD
LKPQPDIVLL PLPTAYELDS TKLKSPLITC PMFRNVPTAN PTEPGIRRVP GASEVIRESN
STTGMVVGIV AAAALCILIL LYAMYKYRNR DEGSYQVDET RNYISNSAQS NGTLMKEKQA
SSKSGHKKQK NKDKEYYV
//
