CNTN6_MOUSE
ID CNTN6_MOUSE Reviewed; 1028 AA.
AC Q9JMB8; Q8C6X1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Contactin-6;
DE AltName: Full=Neural recognition molecule NB-3;
DE Short=mNB-3;
DE Flags: Precursor;
GN Name=Cntn6;
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 [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=129/SvJ; TISSUE=Brain;
RX PubMed=10717476; DOI=10.1016/s0378-1119(00)00031-7;
RA Lee S., Takeda Y., Kawano H., Hosoya H., Nomoto M., Fujimoto D.,
RA Takahashi N., Watanabe K.;
RT "Expression and regulation of a gene encoding neural recognition molecule
RT NB-3 of the contactin/F3 subgroup in mouse brain.";
RL Gene 245:253-266(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12884264; DOI=10.1002/neu.10222;
RA Takeda Y., Akasaka K., Lee S., Kobayashi S., Kawano H., Murayama S.,
RA Takahashi N., Hashimoto K., Kano M., Asano M., Sudo K., Iwakura Y.,
RA Watanabe K.;
RT "Impaired motor coordination in mice lacking neural recognition molecule
RT NB-3 of the contactin/F3 subgroup.";
RL J. Neurobiol. 56:252-265(2003).
RN [5]
RP INTERACTION WITH PTPRG.
RX PubMed=20133774; DOI=10.1073/pnas.0911235107;
RA Bouyain S., Watkins D.J.;
RT "The protein tyrosine phosphatases PTPRZ and PTPRG bind to distinct members
RT of the contactin family of neural recognition molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:2443-2448(2010).
CC -!- FUNCTION: Contactins mediate cell surface interactions during nervous
CC system development. Participates in oligodendrocytes generation by
CC acting as a ligand of NOTCH1. Its association with NOTCH1 promotes
CC NOTCH1 activation through the released notch intracellular domain
CC (NICD) and subsequent translocation to the nucleus (By similarity).
CC Involved in motor coordination. {ECO:0000250,
CC ECO:0000269|PubMed:12884264}.
CC -!- SUBUNIT: Interacts with PTPRG. {ECO:0000269|PubMed:20133774}.
CC -!- INTERACTION:
CC Q9JMB8; P70232: Chl1; NbExp=5; IntAct=EBI-7703151, EBI-7703109;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JMB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JMB8-2; Sequence=VSP_011968;
CC -!- TISSUE SPECIFICITY: Expressed in brain. In brain, it is preferentially
CC expressed in the accessory olfactory bulb, layers II/III and V of the
CC cerebral cortex, piriform cortex, anterior thalamic nuclei, locus
CC coeruleus of the pons and mesencephalic trigeminal nucleus and in
CC Purkinje cells of the cerebellum. {ECO:0000269|PubMed:10717476}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed after birth, reaching a maximum
CC at the postnatal day 7, and declines thereafter in the cerebrum,
CC whereas it increases in the cerebellum to adulthood.
CC {ECO:0000269|PubMed:10717476}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, the formation and
CC organization of all nuclei and layers throughout the brains are
CC apparently normal. They are however slow to learn to stay on the
CC rotating rod in the rotorod test during repeated trials, and display
CC dysfunction of equilibrium and vestibular senses in the wire hang and
CC horizontal rod-walking tests. {ECO:0000269|PubMed:12884264}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB032602; BAA92367.1; -; mRNA.
DR EMBL; AK052972; BAC35227.1; -; mRNA.
DR EMBL; BC076594; AAH76594.1; -; mRNA.
DR CCDS; CCDS20394.1; -. [Q9JMB8-1]
DR RefSeq; NP_059079.2; NM_017383.3. [Q9JMB8-1]
DR RefSeq; XP_006506444.1; XM_006506381.3. [Q9JMB8-1]
DR RefSeq; XP_006506445.1; XM_006506382.3. [Q9JMB8-1]
DR RefSeq; XP_006506446.1; XM_006506383.3. [Q9JMB8-1]
DR RefSeq; XP_006506447.1; XM_006506384.2. [Q9JMB8-2]
DR RefSeq; XP_017177167.1; XM_017321678.1. [Q9JMB8-1]
DR RefSeq; XP_017177168.1; XM_017321679.1. [Q9JMB8-1]
DR PDB; 5E55; X-ray; 2.70 A; A/B=597-900.
DR PDB; 5E5U; X-ray; 2.00 A; B/D=119-316.
DR PDBsum; 5E55; -.
DR PDBsum; 5E5U; -.
DR AlphaFoldDB; Q9JMB8; -.
DR SMR; Q9JMB8; -.
DR BioGRID; 207499; 1.
DR IntAct; Q9JMB8; 1.
DR MINT; Q9JMB8; -.
DR STRING; 10090.ENSMUSP00000086623; -.
DR GlyConnect; 2229; 1 N-Linked glycan (1 site).
DR GlyGen; Q9JMB8; 13 sites, 1 N-linked glycan (1 site).
DR PhosphoSitePlus; Q9JMB8; -.
DR MaxQB; Q9JMB8; -.
DR PaxDb; Q9JMB8; -.
DR PRIDE; Q9JMB8; -.
DR ProteomicsDB; 283586; -. [Q9JMB8-1]
DR ProteomicsDB; 283587; -. [Q9JMB8-2]
DR Antibodypedia; 9868; 141 antibodies from 28 providers.
DR DNASU; 53870; -.
DR Ensembl; ENSMUST00000089215; ENSMUSP00000086623; ENSMUSG00000030092. [Q9JMB8-1]
DR Ensembl; ENSMUST00000162872; ENSMUSP00000124025; ENSMUSG00000030092. [Q9JMB8-1]
DR GeneID; 53870; -.
DR KEGG; mmu:53870; -.
DR UCSC; uc009dco.1; mouse. [Q9JMB8-1]
DR CTD; 27255; -.
DR MGI; MGI:1858223; Cntn6.
DR VEuPathDB; HostDB:ENSMUSG00000030092; -.
DR eggNOG; KOG3513; Eukaryota.
DR GeneTree; ENSGT00940000160606; -.
DR InParanoid; Q9JMB8; -.
DR OMA; LINTCAG; -.
DR OrthoDB; 655902at2759; -.
DR PhylomeDB; Q9JMB8; -.
DR TreeFam; TF351103; -.
DR BioGRID-ORCS; 53870; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Cntn6; mouse.
DR PRO; PR:Q9JMB8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9JMB8; protein.
DR Bgee; ENSMUSG00000030092; Expressed in trigeminal nucleus and 141 other tissues.
DR ExpressionAtlas; Q9JMB8; baseline and differential.
DR Genevisible; Q9JMB8; MM.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEP:MGI.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 6.
DR SUPFAM; SSF48726; SSF48726; 6.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Notch signaling pathway; Phosphoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..999
FT /note="Contactin-6"
FT /id="PRO_0000014729"
FT PROPEP 1000..1028
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014730"
FT DOMAIN 32..117
FT /note="Ig-like C2-type 1"
FT DOMAIN 122..208
FT /note="Ig-like C2-type 2"
FT DOMAIN 227..308
FT /note="Ig-like C2-type 3"
FT DOMAIN 318..402
FT /note="Ig-like C2-type 4"
FT DOMAIN 408..502
FT /note="Ig-like C2-type 5"
FT DOMAIN 500..587
FT /note="Ig-like C2-type 6"
FT DOMAIN 600..698
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 703..800
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 805..901
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 902..996
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOD_RES 882
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQ52"
FT LIPID 999
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 659
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 144..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 249..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 339..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 431..479
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 521..577
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 62..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10717476"
FT /id="VSP_011968"
FT CONFLICT 262
FT /note="K -> R (in Ref. 1; BAA92367)"
FT /evidence="ECO:0000305"
FT CONFLICT 892
FT /note="L -> P (in Ref. 1; BAA92367)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="L -> V (in Ref. 1; BAA92367)"
FT /evidence="ECO:0000305"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 153..159
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:5E5U"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:5E5U"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:5E5U"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:5E5U"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:5E5U"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 304..315
FT /evidence="ECO:0007829|PDB:5E5U"
FT STRAND 602..609
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 611..619
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 647..654
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 659..663
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 670..678
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 683..686
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 705..709
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 716..722
FT /evidence="ECO:0007829|PDB:5E55"
FT HELIX 726..728
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 731..733
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 735..742
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 749..755
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 773..782
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 793..796
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 810..812
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 814..817
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 819..822
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 837..845
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 850..858
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 863..866
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 874..883
FT /evidence="ECO:0007829|PDB:5E55"
FT STRAND 894..897
FT /evidence="ECO:0007829|PDB:5E55"
SQ SEQUENCE 1028 AA; 113761 MW; B233ED300881B101 CRC64;
MRLLWKLVIL LPLINSCAGE GRFSRPIFIQ EPQDVIFPLD LSRSEIILTC TANGYPSPHY
RWKQNGTDID FGMTYHYRLD GGSLAISSPR TDQDIGIYQC LATNPVGTIL SRKAKLQFAY
IEDFETKTRS TVSVREGQGV VLLCGPPPHF GELSYAWTFN DSPLYVQEDK RRFVSQDTGN
LYFAKVEPSD VGNYTCFVTN KEAHRSVQGP PTPLVLRTDG VMGEYEPKIE VRFPETIQAA
KDSSIKLECF ALGNPVPDIS WKRLDGSPMP GKIKYSKSQA ILEIPKFQQE DEGFYECIAG
NLRGRNLAKG QLIFYAPPEW EQKIQNTYLS IYDSLFWECK ASGNPNPSYT WLKNGQRLNT
EERIQIENGT LIITMLNISD SGIYQCAAEN KYQTIYANAE LRVLASAPDF SKNPIKKISV
VQVGGDISIE CKPNAFPKAS ISWKRGTENL KQSKRVLFLE DGSLKICNVT RADAGSYTCV
ATNQFGNGKS SGGLVVKERT IITVPPSKMD VTVGESIVLP CQVSHDPTME VLFVWYFNGD
IIDLKKGVAH FERIGGESVG DLMIRNIQLG HSGKYLCTVQ TTLERLSAVA DIIVRGPPGP
PEDVKVEHIS STTSQLSWRP GPDNNSPIQI FTIQTRTPFS VGWQAVATVP EILNGQTYNA
TVVGLSPWVE YEFRVVAGNN IGIGEPSKPS ELLRTKASVP NVAPGNINGG GGSRSELVIT
WEAIPEELQN GEGFGYIVMF RPVGTTAWMK ERVALVESSK FIYRNESIMP LSPFEVKVGV
YNNEGEGSLS TVTIVYSGED EPQLAPRGTS VQSFSASEME VSWNAIAWNR NTGRVLGYEV
LYWTDNSKES MIGKIRVSGN VTTKNITGLR ANTIYFASVR AYNTAGTGPS SLPVNVTTKK
SPPSQPPANI AWKLSNSKLC LNWEHVKTME NESEVLGYKI LYRQNRQSKT HILETNNTSA
ELLVPFEEDY LIEIRTVSDG GDGSSSEEIR IPKMSSLSST GVQISKPSTQ SLSMVGVFYC
FAIHPLSR
