ID CSTN1_HUMAN Reviewed; 981 AA. AC O94985; A8K183; Q5SR52; Q5UE58; Q71MN0; Q8N4K9; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-FEB-2019, entry version 163. DE RecName: Full=Calsyntenin-1; DE AltName: Full=Alcadein-alpha; DE Short=Alc-alpha; DE AltName: Full=Alzheimer-related cadherin-like protein; DE AltName: Full=Non-classical cadherin XB31alpha; DE Contains: DE RecName: Full=Soluble Alc-alpha; DE Short=SAlc-alpha; DE Contains: DE RecName: Full=CTF1-alpha; DE AltName: Full=C-terminal fragment 1-alpha; DE Flags: Precursor; GN Name=CLSTN1; Synonyms=CS1, KIAA0911; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, RP INTERACTION WITH APBA2, AND MUTAGENESIS OF 913-ASN-PRO-914 AND RP TYR-918. RC TISSUE=Brain; RX PubMed=12972431; DOI=10.1074/jbc.M306024200; RA Araki Y., Tomita S., Yamaguchi H., Miyagi N., Sumioka A., Kirino Y., RA Suzuki T.; RT "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11- RT like protein-mediated stabilization of amyloid beta-protein precursor RT metabolism."; RL J. Biol. Chem. 278:49448-49458(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS RP ALA-474; CYS-524; ARG-583; HIS-857 AND SER-870. RC TISSUE=Hippocampus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 29-33 AND 826-833, AND PROTEOLYTIC CLEAVAGE. RX PubMed=15037614; DOI=10.1074/jbc.M401925200; RA Araki Y., Miyagi N., Kato N., Yoshida T., Wada S., Nishimura M., RA Komano H., Yamamoto T., De Strooper B., Yamamoto K., Suzuki T.; RT "Coordinated metabolism of Alcadein and amyloid beta-protein precursor RT regulates FE65-dependent gene transactivation."; RL J. Biol. Chem. 279:24343-24354(2004). RN [7] RP TISSUE SPECIFICITY. RX PubMed=12498782; DOI=10.1006/mcne.2002.1181; RA Hintsch G., Zurlinden A., Meskenaite V., Steuble M., Fink-Widmer K., RA Kinter J., Sonderegger P.; RT "The calsyntenins - a family of postsynaptic membrane proteins with RT distinct neuronal expression patterns."; RL Mol. Cell. Neurosci. 21:393-409(2002). RN [8] RP INTERACTION WITH KLC1, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=17332754; DOI=10.1038/sj.emboj.7601609; RA Araki Y., Kawano T., Taru H., Saito Y., Wada S., Miyamoto K., RA Kobayashi H., Ishikawa H.O., Ohsugi Y., Yamamoto T., Matsuno K., RA Kinjo M., Suzuki T.; RT "The novel cargo Alcadein induces vesicle association of kinesin-1 RT motor components and activates axonal transport."; RL EMBO J. 26:1475-1486(2007). CC -!- FUNCTION: Induces KLC1 association with vesicles and functions as CC a cargo in axonal anterograde transport. Complex formation with CC APBA2 and APP, stabilizes APP metabolism and enhances APBA2- CC mediated suppression of beta-APP40 secretion, due to the CC retardation of intracellular APP maturation. In complex with APBA2 CC and C99, a C-terminal APP fragment, abolishes C99 interaction with CC PSEN1 and thus APP C99 cleavage by gamma-secretase, most probably CC through stabilization of the direct interaction between APBA2 and CC APP. The intracellular fragment AlcICD suppresses APBB1-dependent CC transactivation stimulated by APP C-terminal intracellular CC fragment (AICD), most probably by competing with AICD for APBB1- CC binding. May modulate calcium-mediated postsynaptic signals (By CC similarity). {ECO:0000250, ECO:0000269|PubMed:12972431}. CC -!- SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex CC with APBA2 and APP. The CTF1 chain interacts with PSEN1. The CC intracellular fragment AlcICD interacts with APBB1; this CC interaction stabilizes AlcICD metabolism. Interacts with KLC1 and CC APBB1 (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q8CD76:Klc1 (xeno); NbExp=7; IntAct=EBI-522075, EBI-6271950; CC Q91YS4:Klc2 (xeno); NbExp=2; IntAct=EBI-16041593, EBI-6272135; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:17332754}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:17332754}. Golgi apparatus membrane CC {ECO:0000269|PubMed:17332754}. Cell projection CC {ECO:0000269|PubMed:17332754}. Cell junction, synapse, CC postsynaptic cell membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. Nucleus CC {ECO:0000269|PubMed:17332754}. Note=Neurite tips. Localized in the CC postsynaptic membrane of both excitatory and inhibitory synapses CC (By similarity). The AlcICD fragment is translocated to the CC nucleus upon interaction with APBB1. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=Alcalpha2; CC IsoId=O94985-1; Sequence=Displayed; CC Name=2; Synonyms=Alcalpha1; CC IsoId=O94985-2; Sequence=VSP_032035; CC -!- TISSUE SPECIFICITY: Expressed in the brain and, a lower level, in CC the heart, skeletal muscle, kidney and placenta. Accumulates in CC dystrophic neurites around the amyloid core of Alzheimer disease CC senile plaques (at protein level). {ECO:0000269|PubMed:12498782, CC ECO:0000269|PubMed:12972431}. CC -!- DOMAIN: The cytoplasmic domain is involved in interaction with CC APBA2, as well as the binding of synaptic Ca(2+). {ECO:0000250}. CC -!- PTM: Proteolytically processed under normal cellular conditions. A CC primary zeta-cleavage generates a large extracellular (soluble) N- CC terminal domain (sAlc) and a short C-terminal transmembrane CC fragment (CTF1). A secondary cleavage catalyzed by presenilin CC gamma-secretase within the transmembrane domain releases the beta- CC Alc-alpha chain in the extracellular milieu and produces an CC intracellular fragment (AlcICD). This processing is strongly CC suppressed in the tripartite complex formed with APBA2 and APP, CC which seems to prevent the association with PSEN1. CC {ECO:0000269|PubMed:15037614}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74934.2; Type=Erroneous initiation; 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; AF438482; AAQ04552.1; -; mRNA. DR EMBL; AY753301; AAV30551.1; -; mRNA. DR EMBL; AB020718; BAA74934.2; ALT_INIT; mRNA. DR EMBL; AK289798; BAF82487.1; -; mRNA. DR EMBL; AL691449; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL357140; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC033902; AAH33902.1; -; mRNA. DR CCDS; CCDS105.1; -. [O94985-2] DR CCDS; CCDS30580.1; -. [O94985-1] DR RefSeq; NP_001009566.1; NM_001009566.2. [O94985-1] DR RefSeq; NP_001289812.1; NM_001302883.1. DR RefSeq; NP_055759.3; NM_014944.4. [O94985-2] DR UniGene; Hs.29665; -. DR ProteinModelPortal; O94985; -. DR BioGrid; 116550; 31. DR DIP; DIP-31694N; -. DR ELM; O94985; -. DR IntAct; O94985; 14. DR MINT; O94985; -. DR STRING; 9606.ENSP00000366513; -. DR iPTMnet; O94985; -. DR PhosphoSitePlus; O94985; -. DR BioMuta; CLSTN1; -. DR jPOST; O94985; -. DR MaxQB; O94985; -. DR PaxDb; O94985; -. DR PeptideAtlas; O94985; -. DR PRIDE; O94985; -. DR ProteomicsDB; 50608; -. DR ProteomicsDB; 50609; -. [O94985-2] DR DNASU; 22883; -. DR Ensembl; ENST00000361311; ENSP00000354997; ENSG00000171603. [O94985-2] DR Ensembl; ENST00000377298; ENSP00000366513; ENSG00000171603. [O94985-1] DR GeneID; 22883; -. DR KEGG; hsa:22883; -. DR UCSC; uc001aqh.4; human. [O94985-1] DR CTD; 22883; -. DR DisGeNET; 22883; -. DR EuPathDB; HostDB:ENSG00000171603.16; -. DR GeneCards; CLSTN1; -. DR HGNC; HGNC:17447; CLSTN1. DR HPA; HPA012412; -. DR MIM; 611321; gene. DR neXtProt; NX_O94985; -. DR OpenTargets; ENSG00000171603; -. DR PharmGKB; PA38238; -. DR eggNOG; KOG1834; Eukaryota. DR eggNOG; ENOG410XT2J; LUCA. DR GeneTree; ENSGT00940000153693; -. DR HOGENOM; HOG000037537; -. DR HOVERGEN; HBG051146; -. DR InParanoid; O94985; -. DR KO; K22659; -. DR OMA; CDEPITS; -. DR OrthoDB; 302557at2759; -. DR PhylomeDB; O94985; -. DR TreeFam; TF315946; -. DR ChiTaRS; CLSTN1; human. DR GeneWiki; CLSTN1; -. DR GenomeRNAi; 22883; -. DR PMAP-CutDB; O94985; -. DR PRO; PR:O94985; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000171603; Expressed in 239 organ(s), highest expression level in postcentral gyrus. DR ExpressionAtlas; O94985; baseline and differential. DR Genevisible; O94985; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0009986; C:cell surface; IBA:GO_Central. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:Ensembl. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IEA:Ensembl. DR GO; GO:0099065; C:integral component of spine apparatus membrane; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0098845; C:postsynaptic endosome; IEA:Ensembl. DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central. DR GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0019894; F:kinesin binding; IPI:UniProtKB. DR GO; GO:0042988; F:X11-like protein binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:UniProtKB. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro. DR GO; GO:0098969; P:neurotransmitter receptor transport to postsynaptic membrane; IEA:Ensembl. DR GO; GO:0051965; P:positive regulation of synapse assembly; IBA:GO_Central. DR GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central. DR GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl. DR GO; GO:0090128; P:regulation of synapse maturation; IEA:Ensembl. DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IEA:Ensembl. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR026914; Calsyntenin. DR InterPro; IPR013320; ConA-like_dom_sf. DR PANTHER; PTHR14139; PTHR14139; 1. DR Pfam; PF00028; Cadherin; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 2. DR SUPFAM; SSF49313; SSF49313; 2. DR SUPFAM; SSF49899; SSF49899; 1. DR PROSITE; PS50268; CADHERIN_2; 2. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell adhesion; Cell junction; KW Cell membrane; Cell projection; Complete proteome; KW Direct protein sequencing; Endoplasmic reticulum; Glycoprotein; KW Golgi apparatus; Membrane; Nucleus; Polymorphism; KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; KW Synapse; Transmembrane; Transmembrane helix. FT SIGNAL 1 28 {ECO:0000269|PubMed:15037614}. FT CHAIN 29 981 Calsyntenin-1. FT /FTId=PRO_0000004021. FT CHAIN 29 825 Soluble Alc-alpha. FT /FTId=PRO_0000323597. FT CHAIN 826 981 CTF1-alpha. FT /FTId=PRO_0000323598. FT TOPO_DOM 29 859 Extracellular. {ECO:0000255}. FT TRANSMEM 860 880 Helical. {ECO:0000255}. FT TOPO_DOM 881 981 Cytoplasmic. {ECO:0000255}. FT DOMAIN 38 164 Cadherin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 165 265 Cadherin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT COMPBIAS 916 959 Glu-rich (highly acidic). FT SITE 824 825 Cleavage. {ECO:0000250|UniProtKB:Q6Q0N0}. FT SITE 853 854 Cleavage. {ECO:0000250|UniProtKB:Q6Q0N0}. FT CARBOHYD 346 346 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 366 366 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 515 515 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 72 81 Missing (in isoform 2). FT {ECO:0000303|PubMed:12972431, FT ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_032035. FT VARIANT 332 332 A -> T (in dbSNP:rs7550295). FT /FTId=VAR_048582. FT VARIANT 474 474 V -> A (in dbSNP:rs17853245). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_039552. FT VARIANT 524 524 S -> C (in dbSNP:rs17853244). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_039553. FT VARIANT 583 583 P -> R (in dbSNP:rs17853243). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_039554. FT VARIANT 857 857 P -> H (in dbSNP:rs17855572). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_039555. FT VARIANT 870 870 F -> S (in dbSNP:rs17855573). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_039556. FT MUTAGEN 913 914 NP->AA: Abolishes interaction with APBA2. FT {ECO:0000269|PubMed:12972431}. FT MUTAGEN 918 918 Y->A: No effect on APBA2-binding. FT {ECO:0000269|PubMed:12972431}. FT CONFLICT 102 102 D -> G (in Ref. 3; BAF82487). FT {ECO:0000305}. FT CONFLICT 553 553 K -> R (in Ref. 3; BAF82487). FT {ECO:0000305}. FT CONFLICT 886 887 HR -> ST (in Ref. 1; AAQ04552). FT {ECO:0000305}. SQ SEQUENCE 981 AA; 109793 MW; 01856284DEC3FC73 CRC64; MLRRPAPALA PAARLLLAGL LCGGGVWAAR VNKHKPWLEP TYHGIVTEND NTVLLDPPLI ALDKDAPLRF AESFEVTVTK EGEICGFKIH GQNVPFDAVV VDKSTGEGVI RSKEKLDCEL QKDYSFTIQA YDCGKGPDGT NVKKSHKATV HIQVNDVNEY APVFKEKSYK ATVIEGKQYD SILRVEAVDA DCSPQFSQIC SYEIITPDVP FTVDKDGYIK NTEKLNYGKE HQYKLTVTAY DCGKKRATED VLVKISIKPT CTPGWQGWNN RIEYEPGTGA LAVFPNIHLE TCDEPVASVQ ATVELETSHI GKGCDRDTYS EKSLHRLCGA AAGTAELLPS PSGSLNWTMG LPTDNGHDSD QVFEFNGTQA VRIPDGVVSV SPKEPFTISV WMRHGPFGRK KETILCSSDK TDMNRHHYSL YVHGCRLIFL FRQDPSEEKK YRPAEFHWKL NQVCDEEWHH YVLNVEFPSV TLYVDGTSHE PFSVTEDYPL HPSKIETQLV VGACWQEFSG VENDNETEPV TVASAGGDLH MTQFFRGNLA GLTLRSGKLA DKKVIDCLYT CKEGLDLQVL EDSGRGVQIQ AHPSQLVLTL EGEDLGELDK AMQHISYLNS RQFPTPGIRR LKITSTIKCF NEATCISVPP VDGYVMVLQP EEPKISLSGV HHFARAASEF ESSEGVFLFP ELRIISTITR EVEPEGDGAE DPTVQESLVS EEIVHDLDTC EVTVEGEELN HEQESLEVDM ARLQQKGIEV SSSELGMTFT GVDTMASYEE VLHLLRYRNW HARSLLDRKF KLICSELNGR YISNEFKVEV NVIHTANPME HANHMAAQPQ FVHPEHRSFV DLSGHNLANP HPFAVVPSTA TVVIVVCVSF LVFMIILGVF RIRAAHRRTM RDQDTGKENE MDWDDSALTI TVNPMETYED QHSSEEEEEE EEEEESEDGE EEDDITSAES ESSEEEEGEQ GDPQNATRQQ QLEWDDSTLS Y //