SEZ6_HUMAN
ID SEZ6_HUMAN Reviewed; 994 AA.
AC Q53EL9; B6ZDN1; Q8N701; Q8NB57; Q8ND50; Q8TD25; Q96NI5; Q96NQ3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Seizure protein 6 homolog;
DE Short=SEZ-6;
DE Short=hSEZ-6;
DE Flags: Precursor;
GN Name=SEZ6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain, and Oligodendroglioma;
RA Huang X.H., Guo J.H., Yu L.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-806.
RC TISSUE=Brain, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-994 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
RN [7]
RP VARIANTS MET-300; VAL-330; ALA-592; ASN-736 AND VAL-756.
RX PubMed=17086543; DOI=10.1002/jnr.21103;
RA Yu Z.-L., Jiang J.-M., Wu D.-H., Xie H.-J., Jiang J.-J., Zhou L., Peng L.,
RA Bao G.-S.;
RT "Febrile seizures are associated with mutation of seizure-related (SEZ) 6,
RT a brain-specific gene.";
RL J. Neurosci. Res. 85:166-172(2007).
CC -!- FUNCTION: May play a role in cell-cell recognition and in neuronal
CC membrane signaling. Seems to be important for the achievement of the
CC necessary balance between dendrite elongation and branching during the
CC elaboration of a complex dendritic arbor. Involved in the development
CC of appropriate excitatory synaptic connectivity (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q53EL9; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-723710, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=Localized on dendrites and in the
CC synaptic and postsynaptic fraction. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q53EL9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53EL9-2; Sequence=VSP_034250;
CC Name=3;
CC IsoId=Q53EL9-3; Sequence=VSP_034253;
CC Name=4; Synonyms=SEZ6b;
CC IsoId=Q53EL9-4; Sequence=VSP_034251, VSP_034252;
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEZ6 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK71497.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAM22213.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB70826.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB70912.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY038048; AAK71497.1; ALT_FRAME; mRNA.
DR EMBL; AF502129; AAM22213.1; ALT_FRAME; mRNA.
DR EMBL; AF502130; AAM22214.1; -; mRNA.
DR EMBL; AK054913; BAB70826.1; ALT_INIT; mRNA.
DR EMBL; AK055383; BAB70912.1; ALT_INIT; mRNA.
DR EMBL; AK091522; BAC03684.1; -; mRNA.
DR EMBL; AK223620; BAD97340.1; -; mRNA.
DR EMBL; AC024267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834405; CAD39067.1; -; mRNA.
DR CCDS; CCDS45638.1; -. [Q53EL9-3]
DR CCDS; CCDS45639.1; -. [Q53EL9-1]
DR RefSeq; NP_001092105.1; NM_001098635.1. [Q53EL9-3]
DR RefSeq; NP_001277131.1; NM_001290202.1. [Q53EL9-2]
DR RefSeq; NP_849191.3; NM_178860.4. [Q53EL9-1]
DR AlphaFoldDB; Q53EL9; -.
DR SMR; Q53EL9; -.
DR BioGRID; 125899; 12.
DR IntAct; Q53EL9; 3.
DR MINT; Q53EL9; -.
DR STRING; 9606.ENSP00000312942; -.
DR GlyGen; Q53EL9; 4 sites.
DR iPTMnet; Q53EL9; -.
DR PhosphoSitePlus; Q53EL9; -.
DR BioMuta; SEZ6; -.
DR DMDM; 190410975; -.
DR MassIVE; Q53EL9; -.
DR PaxDb; Q53EL9; -.
DR PeptideAtlas; Q53EL9; -.
DR PRIDE; Q53EL9; -.
DR ProteomicsDB; 62438; -. [Q53EL9-1]
DR ProteomicsDB; 62439; -. [Q53EL9-2]
DR ProteomicsDB; 62440; -. [Q53EL9-3]
DR ProteomicsDB; 62441; -. [Q53EL9-4]
DR Antibodypedia; 2178; 41 antibodies from 14 providers.
DR DNASU; 124925; -.
DR Ensembl; ENST00000317338.17; ENSP00000312942.11; ENSG00000063015.21. [Q53EL9-1]
DR Ensembl; ENST00000360295.13; ENSP00000353440.9; ENSG00000063015.21. [Q53EL9-3]
DR GeneID; 124925; -.
DR KEGG; hsa:124925; -.
DR MANE-Select; ENST00000317338.17; ENSP00000312942.11; NM_178860.5; NP_849191.3.
DR UCSC; uc002hdp.3; human. [Q53EL9-1]
DR CTD; 124925; -.
DR DisGeNET; 124925; -.
DR GeneCards; SEZ6; -.
DR HGNC; HGNC:15955; SEZ6.
DR HPA; ENSG00000063015; Tissue enhanced (brain, pituitary gland, retina).
DR MIM; 616666; gene.
DR neXtProt; NX_Q53EL9; -.
DR OpenTargets; ENSG00000063015; -.
DR PharmGKB; PA38065; -.
DR VEuPathDB; HostDB:ENSG00000063015; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156995; -.
DR InParanoid; Q53EL9; -.
DR OrthoDB; 126806at2759; -.
DR PhylomeDB; Q53EL9; -.
DR TreeFam; TF330037; -.
DR PathwayCommons; Q53EL9; -.
DR SignaLink; Q53EL9; -.
DR BioGRID-ORCS; 124925; 13 hits in 1067 CRISPR screens.
DR ChiTaRS; SEZ6; human.
DR GeneWiki; SEZ6; -.
DR GenomeRNAi; 124925; -.
DR Pharos; Q53EL9; Tdark.
DR PRO; PR:Q53EL9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q53EL9; protein.
DR Bgee; ENSG00000063015; Expressed in cortical plate and 143 other tissues.
DR ExpressionAtlas; Q53EL9; baseline and differential.
DR Genevisible; Q53EL9; HS.
DR GO; GO:0097440; C:apical dendrite; IEA:Ensembl.
DR GO; GO:0043198; C:dendritic shaft; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0021680; P:cerebellar Purkinje cell layer development; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0050773; P:regulation of dendrite development; IBA:GO_Central.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IBA:GO_Central.
DR GO; GO:0060074; P:synapse maturation; IBA:GO_Central.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00041; CUB; 2.
DR Gene3D; 2.60.120.290; -; 2.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00084; Sushi; 5.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00042; CUB; 2.
DR SUPFAM; SSF49854; SSF49854; 3.
DR SUPFAM; SSF57535; SSF57535; 5.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS50923; SUSHI; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..994
FT /note="Seizure protein 6 homolog"
FT /id="PRO_0000341346"
FT TOPO_DOM 20..925
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 926..946
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 947..994
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 355..414
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 416..527
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 530..591
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 593..704
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 708..767
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 769..832
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 836..897
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 28..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 38..47
FT /note="O-glycosylated at two sites"
FT REGION 59..63
FT /note="O-glycosylated at two sites"
FT REGION 88..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 357..397
FT /evidence="ECO:0000250"
FT DISULFID 383..412
FT /evidence="ECO:0000250"
FT DISULFID 416..443
FT /evidence="ECO:0000250"
FT DISULFID 532..574
FT /evidence="ECO:0000250"
FT DISULFID 559..589
FT /evidence="ECO:0000250"
FT DISULFID 593..619
FT /evidence="ECO:0000250"
FT DISULFID 710..752
FT /evidence="ECO:0000250"
FT DISULFID 738..765
FT /evidence="ECO:0000250"
FT DISULFID 771..813
FT /evidence="ECO:0000250"
FT DISULFID 799..830
FT /evidence="ECO:0000250"
FT DISULFID 838..880
FT /evidence="ECO:0000250"
FT DISULFID 866..895
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034250"
FT VAR_SEQ 493..508
FT /note="LPIEGLLSSGKHFFVE -> PPPPPPLQPHYHRVSV (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034251"
FT VAR_SEQ 509..994
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034252"
FT VAR_SEQ 985..994
FT /note="SLSFAGDERI -> ETREYEVSI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_034253"
FT VARIANT 300
FT /note="V -> M (in dbSNP:rs1428430471)"
FT /evidence="ECO:0000269|PubMed:17086543"
FT /id="VAR_044048"
FT VARIANT 330
FT /note="A -> V (in dbSNP:rs754657367)"
FT /evidence="ECO:0000269|PubMed:17086543"
FT /id="VAR_044049"
FT VARIANT 546
FT /note="T -> A (in dbSNP:rs1976165)"
FT /id="VAR_044050"
FT VARIANT 592
FT /note="V -> A (in dbSNP:rs1397876475)"
FT /evidence="ECO:0000269|PubMed:17086543"
FT /id="VAR_044051"
FT VARIANT 736
FT /note="Y -> N"
FT /evidence="ECO:0000269|PubMed:17086543"
FT /id="VAR_044052"
FT VARIANT 756
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:17086543"
FT /id="VAR_044053"
FT VARIANT 806
FT /note="M -> T (in dbSNP:rs12941884)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_044054"
FT CONFLICT 78
FT /note="Q -> H (in Ref. 1; AAM22213/AAM22214/AAK71497)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> S (in Ref. 1; AAM22213/AAM22214/AAK71497)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="S -> SPD (in Ref. 1; AAM22213/AAM22214/AAK71497)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="Q -> K (in Ref. 1; AAM22213/AAK71497)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="F -> L (in Ref. 3; BAD97340)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..417
FT /note="AACG -> GECP (in Ref. 1; AAM22213/AAK71497)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="G -> P (in Ref. 1; AAM22213/AAK71497)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="D -> G (in Ref. 2; BAB70912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 994 AA; 107425 MW; BF715A8EEA4101C6 CRC64;
MRPVALLLLP SLLALLAHGL SLEAPTVGKG QAPGIEETDG ELTAAPTPEQ PERGVHFVTT
APTLKLLNHH PLLEEFLQEG LEKGDEELRP ALPFQPDPPA PFTPSPLPRL ANQDSRPVFT
SPTPAMAAVP TQPQSKEGPW SPESESPMLR ITAPLPPGPS MAVPTLGPGE IASTTPPSRA
WTPTQEGPGD MGRPWVAEVV SQGAGIGIQG TITSSTASGD DEETTTTTTI ITTTITTVQT
PGPCSWNFSG PEGSLDSPTD LSSPTDVGLD CFFYISVYPG YGVEIKVQNI SLREGETVTV
EGLGGPDPLP LANQSFLLRG QVIRSPTHQA ALRFQSLPPP AGPGTFHFHY QAYLLSCHFP
RRPAYGDVTV TSLHPGGSAR FHCATGYQLK GARHLTCLNA TQPFWDSKEP VCIAACGGVI
RNATTGRIVS PGFPGNYSNN LTCHWLLEAP EGQRLHLHFE KVSLAEDDDR LIIRNGDNVE
APPVYDSYEV EYLPIEGLLS SGKHFFVELS TDSSGAAAGM ALRYEAFQQG HCYEPFVKYG
NFSSSTPTYP VGTTVEFSCD PGYTLEQGSI IIECVDPHDP QWNETEPACR AVCSGEITDS
AGVVLSPNWP EPYGRGQDCI WGVHVEEDKR IMLDIRVLRI GPGDVLTFYD GDDLTARVLG
QYSGPRSHFK LFTSMADVTI QFQSDPGTSV LGYQQGFVIH FFEVPRNDTC PELPEIPNGW
KSPSQPELVH GTVVTYQCYP GYQVVGSSVL MCQWDLTWSE DLPSCQRVTS CHDPGDVEHS
RRLISSPKFP VGATVQYICD QGFVLMGSSI LTCHDRQAGS PKWSDRAPKC LLEQLKPCHG
LSAPENGARS PEKQLHPAGA TIHFSCAPGY VLKGQASIKC VPGHPSHWSD PPPICRAASL
DGFYNSRSLD VAKAPAASST LDAAHIAAAI FLPLVAMVLL VGGVYFYFSR LQGKSSLQLP
RPRPRPYNRI TIESAFDNPT YETGSLSFAG DERI
