NRX2A_RAT
ID NRX2A_RAT Reviewed; 1715 AA.
AC Q63374; Q63375;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Neurexin-2;
DE AltName: Full=Neurexin II-alpha;
DE AltName: Full=Neurexin-2-alpha;
DE Flags: Precursor;
GN Name=Nrxn2;
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] (ISOFORMS 1A AND 10A), VARIANT LEU-434, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=1621094; DOI=10.1126/science.1621094;
RA Ushkaryov Y.A., Petrenko A.G., Geppert M., Suedhof T.C.;
RT "Neurexins: synaptic cell surface proteins related to the alpha-latrotoxin
RT receptor and laminin.";
RL Science 257:50-56(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP ALTERNATIVE SPLICING.
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 [4]
RP 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 [5]
RP INTERACTION WITH PATJ.
RX PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
RN [6]
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.
CC -!- SUBUNIT: The laminin G-like domain 1 binds to NXPH1 (PubMed:9856994).
CC Interacts with PATJ (PubMed:9647694). Interacts with CBLN1, CBLN2 and,
CC less avidly, with CBLN4 (By similarity). Isoforms alpha 2C bind to
CC alpha-dystroglycan (PubMed:11470830). Interacts (via Laminin G-like 1
CC domain) with IGSF21 (Ig-like 1 domain) in a trans-interaction manner
CC (By similarity). {ECO:0000250|UniProtKB:E9Q7X7,
CC ECO:0000269|PubMed:11470830, ECO:0000269|PubMed:9647694,
CC ECO:0000269|PubMed:9856994}.
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=18;
CC Comment=Two isoform types, alpha-type and beta-type are produced by
CC alternative promoter usage. In addition there are at least five major
CC alternatively spliced sites, each of which may be spliced in up to
CC three different ways. Additional isoforms may derive from a minor
CC cytoplasmic splice site 6. Combinatorial splicing at each of these
CC six sites may lead to the generation of at least 216 isoforms but for
CC simplicity only individual splice events are explicitly described
CC below. Beta-type isoforms share the possibility of alternative
CC splicing at sites 4, 5 and 6. Experimental confirmation may be
CC lacking for some isoforms. {ECO:0000269|PubMed:1621094,
CC ECO:0000269|PubMed:7695896};
CC Name=1a; Synonyms=Alpha-1A2A3A4A5A;
CC IsoId=Q63374-1; Sequence=Displayed;
CC Name=2a; Synonyms=Alpha-1B;
CC IsoId=Q63374-2; Sequence=VSP_003509;
CC Name=3a; Synonyms=Alpha-1C;
CC IsoId=Q63374-3; Sequence=VSP_003510;
CC Name=4a; Synonyms=Alpha-2B;
CC IsoId=Q63374-4; Sequence=VSP_003512;
CC Name=5a; Synonyms=Alpha-2C;
CC IsoId=Q63374-5; Sequence=VSP_003511;
CC Name=6a; Synonyms=Alpha-3B;
CC IsoId=Q63374-6; Sequence=VSP_003514;
CC Name=7a; Synonyms=Alpha-3C;
CC IsoId=Q63374-7; Sequence=VSP_003513;
CC Name=8a; Synonyms=Alpha-4B;
CC IsoId=Q63374-8; Sequence=VSP_003515;
CC Name=9a; Synonyms=Alpha-5B;
CC IsoId=Q63374-9; Sequence=VSP_003516;
CC Name=10a; Synonyms=Alpha-6;
CC IsoId=Q63374-10; Sequence=VSP_003517;
CC Name=1b; Synonyms=Beta-4A5A;
CC IsoId=Q63376-1; Sequence=External;
CC Name=2b; Synonyms=Beta-4A5B;
CC IsoId=Q63376-2; Sequence=External;
CC Name=3b; Synonyms=Beta-4B5A;
CC IsoId=Q63376-3; Sequence=External;
CC Name=4b; Synonyms=Beta-4B5B;
CC IsoId=Q63376-4; Sequence=External;
CC Name=5b; Synonyms=Beta-4A5A6;
CC IsoId=Q63376-5; Sequence=External;
CC Name=6b; Synonyms=Beta-4A5B6;
CC IsoId=Q63376-6; Sequence=External;
CC Name=7b; Synonyms=Beta-4B5A6;
CC IsoId=Q63376-7; Sequence=External;
CC Name=8b; Synonyms=Beta-4B5B6;
CC IsoId=Q63376-8; Sequence=External;
CC -!- TISSUE SPECIFICITY: Brain (neuronal synapse).
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; M96376; AAA41706.1; -; mRNA.
DR EMBL; M96376; AAA41707.1; -; mRNA.
DR EMBL; AABR03000676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03002856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03004066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03004601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03004809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03005995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03006603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03006786; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03008290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03009435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C40228; C40228.
DR RefSeq; NP_446298.1; NM_053846.1.
DR AlphaFoldDB; Q63374; -.
DR SMR; Q63374; -.
DR BioGRID; 250509; 4.
DR IntAct; Q63374; 6.
DR MINT; Q63374; -.
DR STRING; 10116.ENSRNOP00000063600; -.
DR GlyGen; Q63374; 4 sites.
DR iPTMnet; Q63374; -.
DR PhosphoSitePlus; Q63374; -.
DR PaxDb; Q63374; -.
DR PRIDE; Q63374; -.
DR GeneID; 116595; -.
DR KEGG; rno:116595; -.
DR CTD; 9379; -.
DR RGD; 620211; Nrxn2.
DR eggNOG; KOG3514; Eukaryota.
DR InParanoid; Q63374; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005246; F:calcium channel regulator activity; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0097109; F:neuroligin family protein binding; ISS:BHF-UCL.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; ISS:BHF-UCL.
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; ISS:BHF-UCL.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:BHF-UCL.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; ISS:BHF-UCL.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL.
DR GO; GO:0042297; P:vocal learning; ISO:RGD.
DR GO; GO:0071625; P:vocalization behavior; ISO:RGD.
DR CDD; cd00110; LamG; 6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Calcium; Cell adhesion;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000250"
FT CHAIN 30..1715
FT /note="Neurexin-2"
FT /id="PRO_0000019496"
FT TOPO_DOM 30..1639
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1640..1660
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1661..1715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..206
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 202..242
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 289..486
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 493..686
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 690..727
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 732..907
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 921..1096
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1099..1136
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1140..1348
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 1461..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1529..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1682..1715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 206..219
FT /evidence="ECO:0000250"
FT DISULFID 213..229
FT /evidence="ECO:0000250"
FT DISULFID 231..241
FT /evidence="ECO:0000250"
FT DISULFID 450..486
FT /evidence="ECO:0000250"
FT DISULFID 657..686
FT /evidence="ECO:0000250"
FT DISULFID 694..705
FT /evidence="ECO:0000250"
FT DISULFID 699..714
FT /evidence="ECO:0000250"
FT DISULFID 716..726
FT /evidence="ECO:0000250"
FT DISULFID 1068..1096
FT /evidence="ECO:0000250"
FT DISULFID 1103..1114
FT /evidence="ECO:0000250"
FT DISULFID 1108..1123
FT /evidence="ECO:0000250"
FT DISULFID 1125..1135
FT /evidence="ECO:0000250"
FT VAR_SEQ 250..283
FT /note="Missing (in isoform 3a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003510"
FT VAR_SEQ 250..259
FT /note="Missing (in isoform 2a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003509"
FT VAR_SEQ 385..399
FT /note="Missing (in isoform 5a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003511"
FT VAR_SEQ 393..399
FT /note="Missing (in isoform 4a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003512"
FT VAR_SEQ 797..806
FT /note="DCLRVGCAPS -> G (in isoform 7a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003513"
FT VAR_SEQ 807..809
FT /note="Missing (in isoform 6a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003514"
FT VAR_SEQ 1256..1285
FT /note="Missing (in isoform 8a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003515"
FT VAR_SEQ 1421..1614
FT /note="Missing (in isoform 9a)"
FT /evidence="ECO:0000305"
FT /id="VSP_003516"
FT VAR_SEQ 1667..1715
FT /note="DEGSYQVDQSRNYISNSAQSNGAVVKEKAPAAPKTPSKAKKNKDKEYYV ->
FT CRKSPREEKLLPGSAQGLGLDLAKACCVCRCRATCIAGKPLEERGGGRGEGERQMQIYI
FT KNK (in isoform 10a)"
FT /evidence="ECO:0000303|PubMed:1621094"
FT /id="VSP_003517"
FT VARIANT 434
FT /note="N -> L"
FT /evidence="ECO:0000269|PubMed:1621094"
FT CONFLICT 244
FT /note="G -> E (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="P -> E (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="D -> N (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="F -> S (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="D -> N (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="V -> I (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="G -> A (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="V -> L (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
FT CONFLICT 987
FT /note="G -> S (in Ref. 1; AAA41706/AAA41707)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1715 AA; 185169 MW; C4A7A4129F25736C CRC64;
MALGSRWRPP PQLPPLLLLL ALVAGVRGLE FGGGPGQWAR YARWAGAAST GELSFSLRTN
ATRALLLYLD DGGDCDFLEL LLVDGRLRLR FTLSCAEPAT LQLDTPVADD RWHMVLLTRD
ARRTALAVDG EARAAEVRSK RREMQVASDL FVGGIPPDVR LSALTLSTVK YEPPFRGLLA
NLKLGERPPA LLGSQGLRGA AADPLCAPAR NPCANGGLCT VLAPGEVGCD CSHTGFGGKF
CSEGEHPMEG PAHLTLNSPV GSLLFSEGGA GRGGAGDVHQ PTKGKEEFVA TFKGNEFFCY
DLSHNPIQSS TDEITLAFRT LQRNGLMLHT GKSADYVNLS LKSGAVWLVI NLGSGAFEAL
VEPVNGKFND NAWHDVRVTR NLRQHAGIGH AMVNKLHYLV TISVDGILTT TGYTQEDYTM
LGSDDFFYIG GSPNTADLPG SPVSNNFMGC LKDVVYKNND FKLELSRLAK EGDPKMKLQG
DLSFRCEDVA ALDPVTFESP EAFVALPRWS AKRTGSISLD FRTTEPNGLL LFSQGRRAGA
GVGSHSSSQR ADYFAMELLD GYLYLLLDMG SGGIKLRASS RKVNDGEWCH VDFQRDGRKG
SISVNSRSTP FLATGESEVL DLESELYLGG LPEGGRVDLP LPPEVWTAAL RAGYVGCVRD
LFIDGRSRDL RGLAEAQGAV GVAPFCSRET LKQCASAPCR NGGICREGWN RFVCDCIGTG
FLGRVCEREA TVLSYDGSMY MKIMLPNAMH TEAEDVSLRF MSQRAYGLMM ATTSRESADT
LRLELDGGQM KLTVNLDCLR VGCAPSAAGK GPETLFAGHK LNDNEWHTVR VVRRGKSLQL
SVDNVTVEGQ MAGAHTRLEF HNIETGIMTE RRFISVVPSN FIGHLSGLVF NGQPYMDQCK
DGDITYCELN ARFGLRAIVA DPVTFKSRSS YLALATLQAY ASMHLFFQFK TTAPDGLLLF
NSGNGNDFIV IELVKGYIHY VFDLGNGPSL MKGNSDKPVN DNQWHNVVVS RDPGNVHTLK
IDSRTVTQHS NGARNLDLKG ELYIGGLSKN MFSNLPKLVA SRDGFQGCLA SVDLNGRLPD
LIADALHRIG QVERGCDGPS TTCTEESCAN QGVCLQQWDG FTCDCTMTSY GGPVCNDPGT
TYIFGKGGAL ITYTWPPNDR PSTRMDRLAV GFSTHQRSAV LVRVDSASGL GDYLQLHIDQ
GTVGVIFNVG TDDITIDEPN AIVSDGKYHV VRFTRSGGNA TLQVDSWPVN ERYPAGNFDN
ERLAIARQRI PYRLGRVVDE WLLDKGRQLT IFNSQAAIKI GGRDQGRPFQ GQVSGLYYNG
LKVLALAAES DPNVRTEGHL RLVGEGPSVL LSAETTATTL LADMATTIME TTTTMATTTT
RRGRSPTMRD STTQNTDDLL VASAECPSDD EDLEECEPST GGELILPIIT EDSLDPPPVA
TRSPFVPPPP TFYPFLTGVG ATQDTLPPPA ARRPSSGGPC QAERDDSDCE EPVEASGFAS
GEVFDSSLPP TDDEDFYTTF PLVTDRTTLL SPRKPAPRPN LRTDGATGAP GVLLAPSAPA
PNLPAGKMNH RDPLQPLLEN PPLGPGVPTA FEPRRPPPLR PGVTSVPGFP RLPTANPTGP
GERGPPGAVE VIRESSSTTG MVVGIVAAAA LCILILLYAM YKYRNRDEGS YQVDQSRNYI
SNSAQSNGAV VKEKAPAAPK TPSKAKKNKD KEYYV
