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Contactin-2 (Axonal glycoprotein TAG-1) (Axonin-1) (Transient axonal glycoprotein 1) (TAX-1)

 CNTN2_HUMAN             Reviewed;        1040 AA.
Q02246; P78432; Q5T054;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
28-FEB-2018, entry version 178.
RecName: Full=Contactin-2;
AltName: Full=Axonal glycoprotein TAG-1;
AltName: Full=Axonin-1;
AltName: Full=Transient axonal glycoprotein 1;
Short=TAX-1;
Flags: Precursor;
Name=CNTN2; Synonyms=AXT, TAG1, TAX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8425542; DOI=10.1111/j.1432-1033.1993.tb19902.x;
Hasler T.H., Rader C., Stoeckli E.T., Zuellig R.A., Sonderegger P.;
"cDNA cloning, structural features, and eucaryotic expression of human
TAG-1/axonin-1.";
Eur. J. Biochem. 211:329-339(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8307567; DOI=10.1016/S0888-7543(05)80357-X;
Tsiotra C.P., Karagogeos D., Theodorakis K., Michaelidis M.T.,
Modi W.S., Furley J.A., Jessel M.T., Papamatheakis J.;
"Isolation of the cDNA and chromosomal localization of the gene (TAX1)
encoding the human axonal glycoprotein TAG-1.";
Genomics 18:562-567(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8586412; DOI=10.1006/geno.1995.9892;
Kozlov S.V., Giger R.J., Hasler T., Korvatska E., Schorderet D.F.,
Sonderegger P.;
"The human TAX1 gene encoding the axon-associated cell adhesion
molecule TAG-1/axonin-1: genomic structure and basic promoter.";
Genomics 30:141-148(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
TISSUE=Placenta;
Tsiotra C.P., Theodorakis C., Michaelidis M.T., Mamalaki C.,
Karagogeus D., Papamatheakis J.;
"Molecular structure and functional studies of the TAX-1 promoter.";
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 31-45.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-904.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
INVOLVEMENT IN FAME5, AND FUNCTION.
PubMed=23518707; DOI=10.1093/brain/awt068;
Stogmann E., Reinthaler E., Eltawil S., El Etribi M.A., Hemeda M.,
El Nahhas N., Gaber A.M., Fouad A., Edris S., Benet-Pages A.,
Eck S.H., Pataraia E., Mei D., Brice A., Lesage S., Guerrini R.,
Zimprich F., Strom T.M., Zimprich A.;
"Autosomal recessive cortical myoclonic tremor and epilepsy:
association with a mutation in the potassium channel associated gene
CNTN2.";
Brain 136:1155-1160(2013).
[9]
X-RAY CRYSTALLOGRAPHY (3.07 ANGSTROMS) OF 34-414, AND DISULFIDE BONDS.
PubMed=17766378; DOI=10.1110/ps.072802707;
Mortl M., Sonderegger P., Diederichs K., Welte W.;
"The crystal structure of the ligand-binding module of human TAG-1
suggests a new mode of homophilic interaction.";
Protein Sci. 16:2174-2183(2007).
-!- FUNCTION: In conjunction with another transmembrane protein,
CNTNAP2, contributes to the organization of axonal domains at
nodes of Ranvier by maintaining voltage-gated potassium channels
at the juxtaparanodal region. May be involved in cell adhesion.
{ECO:0000269|PubMed:23518707}.
-!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
Note=Attached to the neuronal membrane by a GPI-anchor and is also
released from neurons.
-!- DISEASE: Epilepsy, familial adult myoclonic, 5 (FAME5)
[MIM:615400]: A form of cortical myoclonic tremor with epilepsy, a
syndrome characterized by cortical myoclonus and variable
occurrence of epileptic seizures. Usually, myoclonic tremor is the
presenting symptom, characterized by tremulous finger movements
and myoclonic jerks of the limbs increased by action and posture.
In a minority of patients, seizures are the presenting symptom;
both complex partial as well as generalized tonic clonic seizures
are described. Some patients exhibit mild cognitive impairment.
{ECO:0000269|PubMed:23518707}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
family. {ECO:0000305}.
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EMBL; X68274; CAA48335.1; -; mRNA.
EMBL; X67734; CAA47963.1; -; mRNA.
EMBL; X84420; CAA59137.1; -; Genomic_DNA.
EMBL; AL583832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X92681; CAA63365.1; -; Genomic_DNA.
CCDS; CCDS1449.1; -.
PIR; S35508; A49356.
RefSeq; NP_001333012.1; NM_001346083.1.
RefSeq; NP_005067.1; NM_005076.4.
UniGene; Hs.519220; -.
PDB; 2OM5; X-ray; 3.07 A; A=34-414.
PDBsum; 2OM5; -.
ProteinModelPortal; Q02246; -.
SMR; Q02246; -.
BioGrid; 112763; 7.
IntAct; Q02246; 2.
MINT; Q02246; -.
STRING; 9606.ENSP00000330633; -.
TCDB; 8.A.23.1.3; the basigin (basigin) family.
iPTMnet; Q02246; -.
PhosphoSitePlus; Q02246; -.
BioMuta; CNTN2; -.
DMDM; 399092; -.
PaxDb; Q02246; -.
PeptideAtlas; Q02246; -.
PRIDE; Q02246; -.
Ensembl; ENST00000331830; ENSP00000330633; ENSG00000184144.
Ensembl; ENST00000638378; ENSP00000492617; ENSG00000184144.
Ensembl; ENST00000639302; ENSP00000491671; ENSG00000184144.
Ensembl; ENST00000640326; ENSP00000492495; ENSG00000184144.
GeneID; 6900; -.
KEGG; hsa:6900; -.
UCSC; uc001hbr.4; human.
CTD; 6900; -.
DisGeNET; 6900; -.
EuPathDB; HostDB:ENSG00000184144.9; -.
GeneCards; CNTN2; -.
HGNC; HGNC:2172; CNTN2.
HPA; HPA001397; -.
HPA; HPA012497; -.
MalaCards; CNTN2; -.
MIM; 190197; gene.
MIM; 615400; phenotype.
neXtProt; NX_Q02246; -.
OpenTargets; ENSG00000184144; -.
Orphanet; 86814; Benign adult familial myoclonic epilepsy.
PharmGKB; PA26686; -.
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00760000118840; -.
HOGENOM; HOG000059617; -.
HOVERGEN; HBG051047; -.
InParanoid; Q02246; -.
KO; K06760; -.
OMA; ECFAFGN; -.
OrthoDB; EOG091G00X7; -.
PhylomeDB; Q02246; -.
TreeFam; TF351103; -.
Reactome; R-HSA-373760; L1CAM interactions.
Reactome; R-HSA-419037; NCAM1 interactions.
Reactome; R-HSA-447038; NrCAM interactions.
ChiTaRS; CNTN2; human.
EvolutionaryTrace; Q02246; -.
GeneWiki; CNTN2; -.
GenomeRNAi; 6900; -.
PRO; PR:Q02246; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000184144; -.
CleanEx; HS_CNTN2; -.
ExpressionAtlas; Q02246; baseline and differential.
Genevisible; Q02246; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
GO; GO:0043209; C:myelin sheath; ISS:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0033268; C:node of Ranvier; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0045202; C:synapse; ISS:BHF-UCL.
GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; TAS:BHF-UCL.
GO; GO:0043621; F:protein self-association; IEA:Ensembl.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IEA:Ensembl.
GO; GO:0045163; P:clustering of voltage-gated potassium channels; ISS:BHF-UCL.
GO; GO:0071206; P:establishment of protein localization to juxtaparanode region of axon; IEA:Ensembl.
GO; GO:0007612; P:learning; IEA:Ensembl.
GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0060168; P:positive regulation of adenosine receptor signaling pathway; IEA:Ensembl.
GO; GO:0010954; P:positive regulation of protein processing; IEA:Ensembl.
GO; GO:0097090; P:presynaptic membrane organization; IMP:UniProtKB.
GO; GO:0071205; P:protein localization to juxtaparanode region of axon; ISS:BHF-UCL.
GO; GO:0031623; P:receptor internalization; IEA:Ensembl.
GO; GO:0048710; P:regulation of astrocyte differentiation; IEA:Ensembl.
GO; GO:0031133; P:regulation of axon diameter; IEA:Ensembl.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 10.
InterPro; IPR032991; Contactin-2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
PANTHER; PTHR43905:SF1; PTHR43905:SF1; 1.
Pfam; PF00041; fn3; 3.
Pfam; PF07679; I-set; 2.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 6.
SMART; SM00408; IGc2; 5.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 3.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
1: Evidence at protein level;
3D-structure; Cell adhesion; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Epilepsy; Glycoprotein;
GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
Polymorphism; Reference proteome; Repeat; Signal.
SIGNAL 1 30 {ECO:0000269|PubMed:15340161}.
CHAIN 31 1012 Contactin-2.
/FTId=PRO_0000014695.
PROPEP 1013 1040 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000014696.
DOMAIN 43 128 Ig-like C2-type 1.
DOMAIN 133 222 Ig-like C2-type 2.
DOMAIN 239 322 Ig-like C2-type 3.
DOMAIN 327 411 Ig-like C2-type 4.
DOMAIN 417 504 Ig-like C2-type 5.
DOMAIN 509 603 Ig-like C2-type 6.
DOMAIN 610 708 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 713 810 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 815 910 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 915 1006 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 794 796 Cell attachment site. {ECO:0000250}.
COMPBIAS 606 612 Gly/Pro-rich.
LIPID 1012 1012 GPI-anchor amidated asparagine.
{ECO:0000255}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 477 477 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 525 525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 830 830 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 904 904 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 918 918 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 940 940 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 61 111 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17766378}.
DISULFID 155 207 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17766378}.
DISULFID 261 306 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17766378}.
DISULFID 348 395 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:17766378}.
VARIANT 145 145 A -> T (in dbSNP:rs2275697).
/FTId=VAR_021918.
VARIANT 366 366 P -> L (in dbSNP:rs2229866).
/FTId=VAR_029129.
VARIANT 657 657 R -> W (in dbSNP:rs2305276).
/FTId=VAR_021919.
VARIANT 1024 1024 V -> I (in dbSNP:rs17416074).
/FTId=VAR_049867.
STRAND 35 41 {ECO:0000244|PDB:2OM5}.
STRAND 46 51 {ECO:0000244|PDB:2OM5}.
STRAND 55 59 {ECO:0000244|PDB:2OM5}.
STRAND 62 67 {ECO:0000244|PDB:2OM5}.
STRAND 70 75 {ECO:0000244|PDB:2OM5}.
STRAND 87 91 {ECO:0000244|PDB:2OM5}.
STRAND 94 99 {ECO:0000244|PDB:2OM5}.
HELIX 102 105 {ECO:0000244|PDB:2OM5}.
STRAND 107 115 {ECO:0000244|PDB:2OM5}.
STRAND 118 121 {ECO:0000244|PDB:2OM5}.
STRAND 125 132 {ECO:0000244|PDB:2OM5}.
STRAND 151 153 {ECO:0000244|PDB:2OM5}.
STRAND 160 162 {ECO:0000244|PDB:2OM5}.
STRAND 165 172 {ECO:0000244|PDB:2OM5}.
STRAND 180 185 {ECO:0000244|PDB:2OM5}.
STRAND 187 189 {ECO:0000244|PDB:2OM5}.
STRAND 192 196 {ECO:0000244|PDB:2OM5}.
STRAND 203 213 {ECO:0000244|PDB:2OM5}.
STRAND 216 221 {ECO:0000244|PDB:2OM5}.
STRAND 225 227 {ECO:0000244|PDB:2OM5}.
STRAND 229 231 {ECO:0000244|PDB:2OM5}.
STRAND 237 243 {ECO:0000244|PDB:2OM5}.
STRAND 247 252 {ECO:0000244|PDB:2OM5}.
STRAND 257 260 {ECO:0000244|PDB:2OM5}.
STRAND 262 267 {ECO:0000244|PDB:2OM5}.
STRAND 270 275 {ECO:0000244|PDB:2OM5}.
STRAND 289 295 {ECO:0000244|PDB:2OM5}.
HELIX 298 300 {ECO:0000244|PDB:2OM5}.
STRAND 302 310 {ECO:0000244|PDB:2OM5}.
STRAND 313 324 {ECO:0000244|PDB:2OM5}.
STRAND 329 331 {ECO:0000244|PDB:2OM5}.
STRAND 336 339 {ECO:0000244|PDB:2OM5}.
STRAND 344 347 {ECO:0000244|PDB:2OM5}.
STRAND 352 354 {ECO:0000244|PDB:2OM5}.
STRAND 357 366 {ECO:0000244|PDB:2OM5}.
STRAND 373 376 {ECO:0000244|PDB:2OM5}.
STRAND 379 384 {ECO:0000244|PDB:2OM5}.
HELIX 387 389 {ECO:0000244|PDB:2OM5}.
STRAND 391 398 {ECO:0000244|PDB:2OM5}.
STRAND 403 413 {ECO:0000244|PDB:2OM5}.
SEQUENCE 1040 AA; 113393 MW; 254E78DD3C28EFB6 CRC64;
MGTATRRKPH LLLVAAVALV SSSAWSSALG SQTTFGPVFE DQPLSVLFPE ESTEEQVLLA
CRARASPPAT YRWKMNGTEM KLEPGSRHQL VGGNLVIMNP TKAQDAGVYQ CLASNPVGTV
VSREAILRFG FLQEFSKEER DPVKAHEGWG VMLPCNPPAH YPGLSYRWLL NEFPNFIPTD
GRHFVSQTTG NLYIARTNAS DLGNYSCLAT SHMDFSTKSV FSKFAQLNLA AEDTRLFAPS
IKARFPAETY ALVGQQVTLE CFAFGNPVPR IKWRKVDGSL SPQWTTAEPT LQIPSVSFED
EGTYECEAEN SKGRDTVQGR IIVQAQPEWL KVISDTEADI GSNLRWGCAA AGKPRPTVRW
LRNGEPLASQ NRVEVLAGDL RFSKLSLEDS GMYQCVAENK HGTIYASAEL AVQALAPDFR
LNPVRRLIPA ARGGEILIPC QPRAAPKAVV LWSKGTEILV NSSRVTVTPD GTLIIRNISR
SDEGKYTCFA ENFMGKANST GILSVRDATK ITLAPSSADI NLGDNLTLQC HASHDPTMDL
TFTWTLDDFP IDFDKPGGHY RRTNVKETIG DLTILNAQLR HGGKYTCMAQ TVVDSASKEA
TVLVRGPPGP PGGVVVRDIG DTTIQLSWSR GFDNHSPIAK YTLQARTPPA GKWKQVRTNP
ANIEGNAETA QVLGLTPWMD YEFRVIASNI LGTGEPSGPS SKIRTREAAP SVAPSGLSGG
GGAPGELIVN WTPMSREYQN GDGFGYLLSF RRQGSTHWQT ARVPGADAQY FVYSNESVRP
YTPFEVKIRS YNRRGDGPES LTALVYSAEE EPRVAPTKVW AKGVSSSEMN VTWEPVQQDM
NGILLGYEIR YWKAGDKEAA ADRVRTAGLD TSARVSGLHP NTKYHVTVRA YNRAGTGPAS
PSANATTMKP PPRRPPGNIS WTFSSSSLSI KWDPVVPFRN ESAVTGYKML YQNDLHLTPT
LHLTGKNWIE IPVPEDIGHA LVQIRTTGPG GDGIPAEVHI VRNGGTSMMV ENMAVRPAPH
PGTVISHSVA MLILIGSLEL


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