CSTN1_MOUSE
ID CSTN1_MOUSE Reviewed; 979 AA.
AC Q9EPL2; A2A800; B2KFP1; B2KFP2; Q69ZV9; Q7TS67; Q8K103;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Calsyntenin-1 {ECO:0000305};
DE AltName: Full=Alcadein-alpha {ECO:0000303|PubMed:17332754};
DE Short=Alc-alpha {ECO:0000303|PubMed:17332754};
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 {ECO:0000312|MGI:MGI:1929895}; Synonyms=Cs1, Cstn1, Kiaa0911;
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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP CLEAVAGE.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=11161476; DOI=10.1006/mcne.2000.0937;
RA Vogt L., Schrimpf S.P., Meskenaite V., Frischknecht R., Kinter J.,
RA Leone D.P., Ziegler U., Sonderegger P.;
RT "Calsyntenin-1, a proteolytically processed postsynaptic membrane protein
RT with a cytoplasmic calcium-binding domain.";
RL Mol. Cell. Neurosci. 17:151-166(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Olfactory epithelium, and Retina;
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 [5]
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 [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP APBA2.
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-like
RT protein-mediated stabilization of amyloid beta-protein precursor
RT metabolism.";
RL J. Biol. Chem. 278:49448-49458(2003).
RN [7]
RP PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=15037614; DOI=10.1074/jbc.m401925200;
RA Araki Y., Miyagi N., Kato N., Yoshida T., Wada S., Nishimura M., Komano H.,
RA 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 [8]
RP INTERACTION WITH KLC1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP MUTAGENESIS OF GLU-900; MET-901; ASP-902; TRP-903; ASP-904; ASP-905 AND
RP TRP-972.
RX PubMed=16760430; DOI=10.1091/mbc.e06-02-0112;
RA Konecna A., Frischknecht R., Kinter J., Ludwig A., Steuble M.,
RA Meskenaite V., Indermuehle M., Engel M., Cen C., Mateos J.-M., Streit P.,
RA Sonderegger P.;
RT "Calsyntenin-1 docks vesicular cargo to kinesin-1.";
RL Mol. Biol. Cell 17:3651-3663(2006).
RN [9]
RP FUNCTION, INTERACTION WITH KLC1 AND APBB1, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=17332754; DOI=10.1038/sj.emboj.7601609;
RA Araki Y., Kawano T., Taru H., Saito Y., Wada S., Miyamoto K., Kobayashi H.,
RA Ishikawa H.O., Ohsugi Y., Yamamoto T., Matsuno K., Kinjo M., Suzuki T.;
RT "The novel cargo Alcadein induces vesicle association of kinesin-1 motor
RT components and activates axonal transport.";
RL EMBO J. 26:1475-1486(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Induces KLC1 association with vesicles and functions as a
CC cargo in axonal anterograde transport. Complex formation with APBA2 and
CC APP, stabilizes APP metabolism and enhances APBA2-mediated suppression
CC of beta-APP40 secretion, due to the retardation of intracellular APP
CC maturation. In complex with APBA2 and C99, a C-terminal APP fragment,
CC abolishes C99 interaction with PSEN1 and thus APP C99 cleavage by
CC gamma-secretase, most probably through stabilization of the direct
CC interaction between APBA2 and APP. As intracellular fragment AlcICD,
CC suppresses APBB1-dependent transactivation stimulated by APP C-terminal
CC intracellular fragment (AICD), most probably by competing with AICD for
CC APBB1-binding. May modulate calcium-mediated postsynaptic signals.
CC {ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:17332754}.
CC -!- SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex with
CC APBA2 and APP. The CTF1 chain interacts with PSEN1. The intracellular
CC fragment AlcICD interacts with APBB1; this interaction stabilizes
CC AlcICD metabolism. Interacts with KLC1 and APBB1.
CC {ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:16760430,
CC ECO:0000269|PubMed:17332754}.
CC -!- INTERACTION:
CC Q9EPL2; Q8CD76: Klc1; NbExp=3; IntAct=EBI-2013142, EBI-6271950;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC I membrane protein. Golgi apparatus membrane. Cell projection, neuron
CC projection {ECO:0000269|PubMed:12972431, ECO:0000269|PubMed:17332754}.
CC Postsynaptic cell membrane; Single-pass type I membrane protein.
CC Nucleus {ECO:0000250}. Vesicle {ECO:0000269|PubMed:17332754}.
CC Note=Neurite tips. Localized in the postsynaptic membrane of both
CC excitatory and inhibitory synapses. The AlcICD fragment is translocated
CC to the nucleus upon interaction with APBB1 (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9EPL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9EPL2-2; Sequence=VSP_032036;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain (at protein level),
CC with over 90% of the neurons expressing detectable amounts. In the
CC brain, relatively high levels in the cerebral cortex, striatum,
CC hippocampus and thalamus. Moderate levels in the cerebellum. Low levels
CC in the olfactory bulb, midbrain and pons (at protein level). Not
CC detected in Purkinje cells. Expressed at low levels in the lung (at
CC protein level). At the mRNA level, weakly detected in the kidney, lung,
CC skeletal muscle, heart and testis. Not expressed in the sciatic nerve
CC fiber. {ECO:0000269|PubMed:12498782, ECO:0000269|PubMed:12972431,
CC ECO:0000269|PubMed:16760430}.
CC -!- DEVELOPMENTAL STAGE: Expression in the brain gradually increases during
CC the first postnatal week, reaching a peak at P7. In the gray matter,
CC highly expressed in both developing and adult brain. In the white
CC matter, at P6 highly expressed in all major fiber tracts, including the
CC anterior commissure and the corpus callosum, as well as the external
CC and internal capsules, while in the adult, axonal expression in fiber
CC tracts is only faint (at protein level). {ECO:0000269|PubMed:16760430}.
CC -!- DOMAIN: The cytoplasmic domain is involved in interaction with APBA2,
CC 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 fragment
CC (CTF1). A secondary cleavage catalyzed by presenilin gamma-secretase
CC within the transmembrane domain releases the beta-Alc-alpha chain in
CC the extracellular milieu and produces an intracellular fragment
CC (AlcICD). Beta-Alc-alpha secretion is largely dependent upon PSEN1 and
CC PSEN2. This processing is strongly suppressed in the tripartite complex
CC formed with APBA2 and APP, which seems to prevent the association with
CC PSEN1. {ECO:0000269|PubMed:11161476, ECO:0000269|PubMed:15037614}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32337.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ289016; CAC17788.1; -; mRNA.
DR EMBL; AK173059; BAD32337.1; ALT_INIT; mRNA.
DR EMBL; AL607078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU207384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU210912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029027; AAH29027.1; -; mRNA.
DR EMBL; BC053843; AAH53843.1; -; mRNA.
DR CCDS; CCDS18963.1; -. [Q9EPL2-1]
DR CCDS; CCDS71522.1; -. [Q9EPL2-2]
DR RefSeq; NP_001277918.1; NM_001290989.1. [Q9EPL2-2]
DR RefSeq; NP_075538.1; NM_023051.5. [Q9EPL2-1]
DR PDB; 6F9I; X-ray; 3.99 A; C/X=965-979.
DR PDBsum; 6F9I; -.
DR AlphaFoldDB; Q9EPL2; -.
DR SMR; Q9EPL2; -.
DR BioGRID; 211147; 11.
DR ELM; Q9EPL2; -.
DR IntAct; Q9EPL2; 53.
DR MINT; Q9EPL2; -.
DR STRING; 10090.ENSMUSP00000036962; -.
DR GlyGen; Q9EPL2; 3 sites.
DR iPTMnet; Q9EPL2; -.
DR PhosphoSitePlus; Q9EPL2; -.
DR MaxQB; Q9EPL2; -.
DR PaxDb; Q9EPL2; -.
DR PeptideAtlas; Q9EPL2; -.
DR PRIDE; Q9EPL2; -.
DR ProteomicsDB; 277907; -. [Q9EPL2-1]
DR ProteomicsDB; 277908; -. [Q9EPL2-2]
DR Antibodypedia; 2632; 178 antibodies from 27 providers.
DR DNASU; 65945; -.
DR Ensembl; ENSMUST00000039144; ENSMUSP00000036962; ENSMUSG00000039953. [Q9EPL2-1]
DR Ensembl; ENSMUST00000105691; ENSMUSP00000101316; ENSMUSG00000039953. [Q9EPL2-2]
DR GeneID; 65945; -.
DR KEGG; mmu:65945; -.
DR UCSC; uc008vwo.2; mouse. [Q9EPL2-1]
DR UCSC; uc008vwp.2; mouse. [Q9EPL2-2]
DR CTD; 22883; -.
DR MGI; MGI:1929895; Clstn1.
DR VEuPathDB; HostDB:ENSMUSG00000039953; -.
DR eggNOG; KOG1834; Eukaryota.
DR GeneTree; ENSGT00950000183086; -.
DR HOGENOM; CLU_008904_0_0_1; -.
DR InParanoid; Q9EPL2; -.
DR OMA; CWQGSDN; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q9EPL2; -.
DR TreeFam; TF315946; -.
DR BioGRID-ORCS; 65945; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Clstn1; mouse.
DR PRO; PR:Q9EPL2; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9EPL2; protein.
DR Bgee; ENSMUSG00000039953; Expressed in floor plate of midbrain and 248 other tissues.
DR Genevisible; Q9EPL2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0099065; C:integral component of spine apparatus membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098845; C:postsynaptic endosome; IDA:SynGO.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0042988; F:X11-like protein binding; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:MGI.
DR GO; GO:0007268; P:chemical synaptic transmission; NAS: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; IDA:SynGO.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IGI:MGI.
DR GO; GO:0050806; P:positive regulation of synaptic transmission; IGI:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR GO; GO:0090128; P:regulation of synapse maturation; IDA:SynGO.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR026914; Calsyntenin.
DR InterPro; IPR045588; CLSTN_C.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR PANTHER; PTHR14139; PTHR14139; 1.
DR Pfam; PF00028; Cadherin; 1.
DR Pfam; PF19699; CLSTN_C; 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 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Golgi apparatus; Membrane; Nucleus;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..979
FT /note="Calsyntenin-1"
FT /id="PRO_0000004022"
FT CHAIN 29..825
FT /note="Soluble Alc-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000323599"
FT CHAIN 826..979
FT /note="CTF1-alpha"
FT /evidence="ECO:0000250"
FT /id="PRO_0000323600"
FT TOPO_DOM 29..859
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 881..979
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 38..164
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 165..265
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 915..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..958
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 824..825
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q6Q0N0"
FT SITE 853..854
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:Q6Q0N0"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 72..81
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032036"
FT MUTAGEN 900
FT /note="E->A: Marked reduction in KLC1-binding."
FT /evidence="ECO:0000269|PubMed:16760430"
FT MUTAGEN 901
FT /note="M->A: Almost completely abolishes KLC1-binding."
FT /evidence="ECO:0000269|PubMed:16760430"
FT MUTAGEN 902
FT /note="D->A: Marked reduction in KLC1-binding."
FT /evidence="ECO:0000269|PubMed:16760430"
FT MUTAGEN 903
FT /note="W->A: Marked reduction in KLC1-binding; when
FT associated with A-972. Marked alteration in anterograde
FT axonal transport."
FT /evidence="ECO:0000269|PubMed:16760430"
FT MUTAGEN 904
FT /note="D->A: Almost completely abolishes KLC1-binding."
FT /evidence="ECO:0000269|PubMed:16760430"
FT MUTAGEN 905
FT /note="D->A: Almost completely abolishes KLC1-binding."
FT /evidence="ECO:0000269|PubMed:16760430"
FT MUTAGEN 972
FT /note="W->A: Marked reduction in KLC1-binding; when
FT associated with A-903. Marked alteration in anterograde
FT axonal transport."
FT /evidence="ECO:0000269|PubMed:16760430"
SQ SEQUENCE 979 AA; 108900 MW; 898D62AE9C10A99C CRC64;
MLRRPAPALA PAVRLLLAGL LCGGGVWAAR VNKHKPWLEP TYHGIVTEND NTVLLDPPLI
ALDKDSPLRF AESFEVTVTK EGEICGFKIH GQNVPFDAVV VDKSTGEGII RSKEKLDCEL
QKDYTFTIQA YDCGKGPDGT GVKKSHKATV HIQVNDVNEY APVFKEKSYK AAVVEGKQHS
SILRVEAVDA DCSPQFSQIC SYEILTPDVP FTVDKDGYIK NTEKLNYGKE HQYKLTVTAY
DCGKKRATED VLVKISVKPT CSPGWQGWSS RIEYEPGTGA LAVFPSIHLE TCDEPVASVQ
ATVELETSHI GKGCDRDTYS EKSLHRLCGA AAGTSELLPS PSSSFNWTVG LPTDNGHDSD
QVFEFNGTQA VRIPDGVVTL DPKEPFTISV WMRHGPFGRK KETILCSSDK TDMNRHHYSL
YVHGCRLVFL LRQDPSEEKK YRPAEFHWKL NQVCDEDWHH FVLNVEVPSV TLYVDGIPHE
PFSVTEDYPL HPTKIETQLV VGACWQEYSG VESGNETEPA TMASAGGDLH MTQFFRGNLA
GLTVRSGKLA DKKVIDCLYT CKEGLDLQVP EDANRGVQIQ ASSSQAVLTL EGDNVGELDK
AMQHISYLNS RQFPTPGIRR LKITSTVKCF NEAACIEVPP VEGYVMVLQP EEPKISLSGV
HHFARAASEF ESAEGISLFP ELRIISTITR EVEPEADGSE DPTVQESLVS EEIVHDLDTC
EVTVEGDELN AEQESLEVDV TRLQQKGIEA SHSDLGVVFT GVETMASYEE VLHLLRYRNW
HTRSLLDRKF KLICSELNGR YLSNEFKVEV NVIHTANPVE HANHMAAQPQ FVHPEHRSFV
DLSGHNLANP HPFAVVPSTA TVVIVVCVSF LVFMIILGVF RIRAAHQRTM RDQDTGKENE
MDWDDSALTI TVNPMETYED QHSSEEEEEE EEEEESEDGE EEEDITSAES ESSEEEEGGP
GDGQNATRQL EWDDSTLSY
