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 27-MAR-2024, entry version 141. 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}; 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; 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; 13. DR IntAct; Q53EL9; 3. DR MINT; Q53EL9; -. DR STRING; 9606.ENSP00000312942; -. DR GlyCosmos; Q53EL9; 4 sites, No reported glycans. DR GlyGen; Q53EL9; 7 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q53EL9; -. DR PhosphoSitePlus; Q53EL9; -. DR BioMuta; SEZ6; -. DR DMDM; 190410975; -. DR MassIVE; Q53EL9; -. DR PaxDb; 9606-ENSP00000312942; -. DR PeptideAtlas; Q53EL9; -. DR ProteomicsDB; 62438; -. [Q53EL9-1] DR ProteomicsDB; 62439; -. [Q53EL9-2] DR ProteomicsDB; 62440; -. [Q53EL9-3] DR ProteomicsDB; 62441; -. [Q53EL9-4] DR Antibodypedia; 2178; 147 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 AGR; HGNC:15955; -. DR CTD; 124925; -. DR DisGeNET; 124925; -. DR GeneCards; SEZ6; -. DR HGNC; HGNC:15955; SEZ6. DR HPA; ENSG00000063015; Tissue enriched (brain). 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; 5350762at2759; -. DR PhylomeDB; Q53EL9; -. DR TreeFam; TF330037; -. DR PathwayCommons; Q53EL9; -. DR SignaLink; Q53EL9; -. DR BioGRID-ORCS; 124925; 17 hits in 1145 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 cell types or tissues. DR ExpressionAtlas; Q53EL9; baseline and differential. 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: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; 2.10.70.10; Complement Module, domain 1; 5. DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 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 PANTHER; PTHR45656; PROTEIN CBR-CLEC-78; 1. DR PANTHER; PTHR45656:SF1; SEIZURE PROTEIN 6 HOMOLOG; 1. DR Pfam; PF00431; CUB; 2. DR Pfam; PF00084; Sushi; 5. DR SMART; SM00032; CCP; 5. DR SMART; SM00042; CUB; 2. DR SUPFAM; SSF57535; Complement control module/SCR domain; 5. DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3. DR PROSITE; PS01180; CUB; 2. DR PROSITE; PS50923; SUSHI; 5. DR Genevisible; Q53EL9; HS. 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 //