CSTN3_HUMAN
ID CSTN3_HUMAN Reviewed; 956 AA.
AC Q9BQT9; D3DUT6; O94831; Q2T9J5; Q5UE57;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Calsyntenin-3;
DE AltName: Full=Alcadein-beta;
DE Short=Alc-beta;
DE Flags: Precursor;
GN Name=CLSTN3; Synonyms=CS3, KIAA0726;
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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEOLYTIC PROCESSING.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Blood, and Brain;
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 [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH 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 [8]
RP VARIANT [LARGE SCALE ANALYSIS] TYR-874.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May modulate calcium-mediated postsynaptic signals. Complex
CC formation with APBA2 and APP, stabilizes APP metabolism and enhances
CC APBA2-mediated suppression of beta-APP40 secretion, due to the
CC retardation of intracellular APP maturation. {ECO:0000250}.
CC -!- SUBUNIT: Directly interacts with APBA2. Forms a tripartite complex with
CC APBA2 and APP. Interacts with low affinity with KLC1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BQT9; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-11291074, EBI-2807956;
CC Q9BQT9; P21145: MAL; NbExp=3; IntAct=EBI-11291074, EBI-3932027;
CC Q9BQT9; Q16617: NKG7; NbExp=3; IntAct=EBI-11291074, EBI-3919611;
CC Q9BQT9; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-11291074, EBI-2804156;
CC Q9BQT9; Q9UHJ9-5: PGAP2; NbExp=3; IntAct=EBI-11291074, EBI-12092917;
CC Q9BQT9; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-11291074, EBI-12845616;
CC Q9BQT9; Q969K7: TMEM54; NbExp=3; IntAct=EBI-11291074, EBI-3922833;
CC Q9BQT9; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-11291074, EBI-12111910;
CC Q9BQT9; Q8N609: TRAM1L1; NbExp=3; IntAct=EBI-11291074, EBI-11996766;
CC Q9BQT9; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-11291074, EBI-10268111;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99JH7};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99JH7}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}. Postsynapse
CC {ECO:0000250|UniProtKB:Q99JH7}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q99JH7}. Note=Most prominent in the postsynaptic
CC specializations of asymmetric (type I) synapses with both axodendritic
CC and axospinous localization. {ECO:0000250|UniProtKB:Q99JH7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BQT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQT9-2; Sequence=VSP_043748;
CC -!- TISSUE SPECIFICITY: According to PubMed:12498782, expressed
CC predominantly in the brain and in kidney. Low levels in heart, skeletal
CC muscle, liver, placenta, pancreas and lung. According to
CC PubMed:12972431, predominant expression in brain, and only marginal in
CC kidney. In brain, present throughout all cortical layers, highest
CC levels in GABAergic neurons (based on morphology and distribution
CC pattern). {ECO:0000269|PubMed:12498782, ECO:0000269|PubMed:12972431}.
CC -!- DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain.
CC {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 gamma-secretase within the
CC transmembrane domain releases the beta-Alc-beta chain in the
CC extracellular milieu and produces an intracellular fragment (AlcICD).
CC This processing is strongly suppressed in the tripartite complex formed
CC with APBA2 and APP, which seems to prevent the association with gamma-
CC secretase (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34446.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ277460; CAC33084.1; -; mRNA.
DR EMBL; AY753302; AAV30552.1; -; mRNA.
DR EMBL; AB018269; BAA34446.2; ALT_INIT; mRNA.
DR EMBL; AC018653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88677.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88678.1; -; Genomic_DNA.
DR EMBL; CH471116; EAW88679.1; -; Genomic_DNA.
DR EMBL; BC104767; AAI04768.1; -; mRNA.
DR EMBL; BC111491; AAI11492.1; -; mRNA.
DR EMBL; BC112283; AAI12284.1; -; mRNA.
DR CCDS; CCDS8575.1; -. [Q9BQT9-1]
DR RefSeq; NP_055533.2; NM_014718.3. [Q9BQT9-1]
DR RefSeq; XP_006719226.1; XM_006719163.3. [Q9BQT9-2]
DR AlphaFoldDB; Q9BQT9; -.
DR BioGRID; 115094; 103.
DR IntAct; Q9BQT9; 15.
DR MINT; Q9BQT9; -.
DR STRING; 9606.ENSP00000266546; -.
DR GlyGen; Q9BQT9; 5 sites.
DR iPTMnet; Q9BQT9; -.
DR PhosphoSitePlus; Q9BQT9; -.
DR BioMuta; CLSTN3; -.
DR DMDM; 23396507; -.
DR EPD; Q9BQT9; -.
DR jPOST; Q9BQT9; -.
DR MassIVE; Q9BQT9; -.
DR MaxQB; Q9BQT9; -.
DR PaxDb; Q9BQT9; -.
DR PeptideAtlas; Q9BQT9; -.
DR PRIDE; Q9BQT9; -.
DR ProteomicsDB; 78722; -. [Q9BQT9-1]
DR ProteomicsDB; 78723; -. [Q9BQT9-2]
DR Antibodypedia; 42025; 34 antibodies from 14 providers.
DR DNASU; 9746; -.
DR Ensembl; ENST00000266546.11; ENSP00000266546.6; ENSG00000139182.15. [Q9BQT9-1]
DR Ensembl; ENST00000672495.1; ENSP00000500510.1; ENSG00000288427.1. [Q9BQT9-1]
DR GeneID; 9746; -.
DR KEGG; hsa:9746; -.
DR MANE-Select; ENST00000266546.11; ENSP00000266546.6; NM_014718.4; NP_055533.2.
DR UCSC; uc001qsr.4; human. [Q9BQT9-1]
DR CTD; 9746; -.
DR DisGeNET; 9746; -.
DR GeneCards; CLSTN3; -.
DR HGNC; HGNC:18371; CLSTN3.
DR HPA; ENSG00000139182; Low tissue specificity.
DR MIM; 611324; gene.
DR neXtProt; NX_Q9BQT9; -.
DR OpenTargets; ENSG00000139182; -.
DR PharmGKB; PA38320; -.
DR VEuPathDB; HostDB:ENSG00000139182; -.
DR eggNOG; KOG1834; Eukaryota.
DR GeneTree; ENSGT00950000183086; -.
DR HOGENOM; CLU_008904_0_0_1; -.
DR InParanoid; Q9BQT9; -.
DR OMA; YTVQCAM; -.
DR OrthoDB; 302557at2759; -.
DR PhylomeDB; Q9BQT9; -.
DR TreeFam; TF315946; -.
DR PathwayCommons; Q9BQT9; -.
DR SignaLink; Q9BQT9; -.
DR BioGRID-ORCS; 9746; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; CLSTN3; human.
DR GenomeRNAi; 9746; -.
DR Pharos; Q9BQT9; Tbio.
DR PRO; PR:Q9BQT9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BQT9; protein.
DR Bgee; ENSG00000139182; Expressed in cerebellum and 102 other tissues.
DR ExpressionAtlas; Q9BQT9; baseline and differential.
DR Genevisible; Q9BQT9; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR GO; GO:0042988; F:X11-like protein binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; 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:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
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 Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..956
FT /note="Calsyntenin-3"
FT /id="PRO_0000004026"
FT TOPO_DOM 20..847
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..868
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 869..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..145
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 146..246
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 916..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..21
FT /note="MTLLLLPLLLASLLASCSCNK -> MVLGCELSGSTRVVVGVEALLTGASSP
FT LPGVGP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15037614,
FT ECO:0000303|PubMed:9872452"
FT /id="VSP_043748"
FT VARIANT 209
FT /note="S -> G (in dbSNP:rs7302230)"
FT /id="VAR_048583"
FT VARIANT 874
FT /note="H -> Y (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036114"
SQ SEQUENCE 956 AA; 106098 MW; 5BE96722C604B173 CRC64;
MTLLLLPLLL ASLLASCSCN KANKHKPWIE AEYQGIVMEN DNTVLLNPPL FALDKDAPLR
YAGEICGFRL HGSGVPFEAV ILDKATGEGL IRAKEPVDCE AQKEHTFTIQ AYDCGEGPDG
ANTKKSHKAT VHVRVNDVNE FAPVFVERLY RAAVTEGKLY DRILRVEAID GDCSPQYSQI
CYYEILTPNT PFLIDNDGNI ENTEKLQYSG ERLYKFTVTA YDCGKKRAAD DAEVEIQVKP
TCKPSWQGWN KRIEYAPGAG SLALFPGIRL ETCDEPLWNI QATIELQTSH VAKGCDRDNY
SERALRKLCG AATGEVDLLP MPGPNANWTA GLSVHYSQDS SLIYWFNGTQ AVQVPLGGPS
GLGSGPQDSL SDHFTLSFWM KHGVTPNKGK KEEETIVCNT VQNEDGFSHY SLTVHGCRIA
FLYWPLLESA RPVKFLWKLE QVCDDEWHHY ALNLEFPTVT LYTDGISFDP ALIHDNGLIH
PPRREPALMI GACWTEEKNK EKEKGDNSTD TTQGDPLSIH HYFHGYLAGF SVRSGRLESR
EVIECLYACR EGLDYRDFES LGKGMKVHVN PSQSLLTLEG DDVETFNHAL QHVAYMNTLR
FATPGVRPLR LTTAVKCFSE ESCVSIPEVE GYVVVLQPDA PQILLSGTAH FARPAVDFEG
TNGVPLFPDL QITCSISHQV EAKKDESWQG TVTDTRMSDE IVHNLDGCEI SLVGDDLDPE
RESLLLDTTS LQQRGLELTN TSAYLTIAGV ESITVYEEIL RQARYRLRHG AALYTRKFRL
SCSEMNGRYS SNEFIVEVNV LHSMNRVAHP SHVLSSQQFL HRGHQPPPEM AGHSLASSHR
NSMIPSAATL IIVVCVGFLV LMVVLGLVRI HSLHRRVSGA GGPPGASSDP KDPDLFWDDS
ALTIIVNPME SYQNRQSCVT GAVGGQQEDE DSSDSEVADS PSSDERRIIE TPPHRY
