PCD16_HUMAN
ID PCD16_HUMAN Reviewed; 3298 AA.
AC Q96JQ0; O15098;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protocadherin-16;
DE AltName: Full=Cadherin-19;
DE AltName: Full=Cadherin-25;
DE AltName: Full=Fibroblast cadherin-1;
DE AltName: Full=Protein dachsous homolog 1;
DE Flags: Precursor;
GN Name=DCHS1; Synonyms=CDH19, CDH25, FIB1, KIAA1773, PCDH16;
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].
RC TISSUE=Brain;
RX PubMed=11597768; DOI=10.1016/s0169-328x(01)00218-2;
RA Nakajima D., Nakayama M., Kikuno R., Hirosawa M., Nagase T., Ohara O.;
RT "Identification of three novel non-classical cadherin genes through
RT comprehensive analysis of large cDNAs.";
RL Brain Res. Mol. Brain Res. 94:85-95(2001).
RN [2]
RP SEQUENCE REVISION.
RA Nakajima D., Nakayama M., Kikuno R., Nagase T., Ohara O.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 434-570, AND TISSUE SPECIFICITY.
RX PubMed=9199196; DOI=10.1006/bbrc.1997.6707;
RA Matsuyoshi N., Imamura S.;
RT "Multiple cadherins are expressed in human fibroblasts.";
RL Biochem. Biophys. Res. Commun. 235:355-358(1997).
RN [4]
RP FUNCTION, INVOLVEMENT IN MVP2, VARIANT LEU-197, VARIANTS MVP2 CYS-2330 AND
RP HIS-2513, CHARACTERIZATION OF VARIANT LEU-197, AND CHARACTERIZATION OF
RP VARIANTS MVP2 CYS-2330 AND HIS-2513.
RX PubMed=26258302; DOI=10.1038/nature14670;
RA Durst R., Sauls K., Peal D.S., deVlaming A., Toomer K., Leyne M.,
RA Salani M., Talkowski M.E., Brand H., Perrocheau M., Simpson C., Jett C.,
RA Stone M.R., Charles F., Chiang C., Lynch S.N., Bouatia-Naji N.,
RA Delling F.N., Freed L.A., Tribouilloy C., Le Tourneau T., LeMarec H.,
RA Fernandez-Friera L., Solis J., Trujillano D., Ossowski S., Estivill X.,
RA Dina C., Bruneval P., Chester A., Schott J.J., Irvine K.D., Mao Y.,
RA Wessels A., Motiwala T., Puceat M., Tsukasaki Y., Menick D.R.,
RA Kasiganesan H., Nie X., Broome A.M., Williams K., Johnson A.,
RA Markwald R.R., Jeunemaitre X., Hagege A., Levine R.A., Milan D.J.,
RA Norris R.A., Slaugenhaupt S.A.;
RT "Mutations in DCHS1 cause mitral valve prolapse.";
RL Nature 525:109-113(2015).
RN [5]
RP VARIANT [LARGE SCALE ANALYSIS] TRP-1583.
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).
RN [6]
RP VARIANT VMLDS1 ILE-2370.
RX PubMed=24056717; DOI=10.1038/ng.2765;
RA Cappello S., Gray M.J., Badouel C., Lange S., Einsiedler M., Srour M.,
RA Chitayat D., Hamdan F.F., Jenkins Z.A., Morgan T., Preitner N., Uster T.,
RA Thomas J., Shannon P., Morrison V., Di Donato N., Van Maldergem L.,
RA Neuhann T., Newbury-Ecob R., Swinkells M., Terhal P., Wilson L.C.,
RA Zwijnenburg P.J., Sutherland-Smith A.J., Black M.A., Markie D.,
RA Michaud J.L., Simpson M.A., Mansour S., McNeill H., Goetz M.,
RA Robertson S.P.;
RT "Mutations in genes encoding the cadherin receptor-ligand pair DCHS1 and
RT FAT4 disrupt cerebral cortical development.";
RL Nat. Genet. 45:1300-1308(2013).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions
CC in neuroprogenitor cell proliferation and differentiation. In the
CC heart, has a critical role for proper morphogenesis of the mitral
CC valve, acting in the regulation of cell migration involved in valve
CC formation (PubMed:26258302). {ECO:0000269|PubMed:26258302}.
CC -!- SUBUNIT: Heterophilic interaction with FAT4; this interaction affects
CC their respective protein levels. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and
CC DCHS1 accumulated at the cell-cell boundaries located apical to the
CC adherens junction. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in fibroblasts but not in melanocytes or
CC keratinocytes. {ECO:0000269|PubMed:9199196}.
CC -!- DISEASE: Van Maldergem syndrome 1 (VMLDS1) [MIM:601390]: An autosomal
CC recessive disorder characterized by intellectual disability, typical
CC craniofacial features, auditory malformations resulting in hearing
CC loss, and skeletal and limb malformations. Some patients have renal
CC hypoplasia. Brain MRI typically shows periventricular nodular
CC heterotopia. {ECO:0000269|PubMed:24056717}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- DISEASE: Mitral valve prolapse 2 (MVP2) [MIM:607829]: A form of mitral
CC valve prolapse, a valvular heart disease characterized by abnormally
CC elongated and thickened mitral valve leaflets, that typically show
CC myxomatous degeneration with increased leaflet compliance. It is
CC associated with mitral regurgitation. Myxomatous mitral valves have an
CC abnormal layered architecture characterized by loose collagen in
CC fibrosa, expanded spongiosa strongly positive for proteoglycans, and
CC disrupted elastin in atrialis. In classic mitral valve prolapse,
CC leaflets are at least 5 mm thick, whereas in the non-classic form, they
CC are less than 5 mm thick. Severe classic mitral valve prolapse is
CC strongly associated with arrhythmias, endocarditis, heart failure, and
CC need for valve surgery. MVP2 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:26258302}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB61903.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB053446; BAB61903.2; ALT_INIT; mRNA.
DR EMBL; AB000895; BAA21133.1; -; mRNA.
DR CCDS; CCDS7771.1; -.
DR PIR; PC4297; PC4297.
DR RefSeq; NP_003728.1; NM_003737.3.
DR SMR; Q96JQ0; -.
DR BioGRID; 114194; 15.
DR IntAct; Q96JQ0; 6.
DR MINT; Q96JQ0; -.
DR STRING; 9606.ENSP00000299441; -.
DR GlyGen; Q96JQ0; 14 sites.
DR iPTMnet; Q96JQ0; -.
DR PhosphoSitePlus; Q96JQ0; -.
DR BioMuta; DCHS1; -.
DR DMDM; 20139065; -.
DR jPOST; Q96JQ0; -.
DR MassIVE; Q96JQ0; -.
DR PaxDb; Q96JQ0; -.
DR PeptideAtlas; Q96JQ0; -.
DR PRIDE; Q96JQ0; -.
DR ProteomicsDB; 77003; -.
DR Antibodypedia; 64000; 67 antibodies from 16 providers.
DR DNASU; 8642; -.
DR Ensembl; ENST00000299441.5; ENSP00000299441.3; ENSG00000166341.9.
DR GeneID; 8642; -.
DR KEGG; hsa:8642; -.
DR MANE-Select; ENST00000299441.5; ENSP00000299441.3; NM_003737.4; NP_003728.1.
DR UCSC; uc001mem.3; human.
DR CTD; 8642; -.
DR DisGeNET; 8642; -.
DR GeneCards; DCHS1; -.
DR HGNC; HGNC:13681; DCHS1.
DR HPA; ENSG00000166341; Low tissue specificity.
DR MalaCards; DCHS1; -.
DR MIM; 601390; phenotype.
DR MIM; 603057; gene.
DR MIM; 607829; phenotype.
DR neXtProt; NX_Q96JQ0; -.
DR OpenTargets; ENSG00000166341; -.
DR Orphanet; 314679; Cerebrofacioarticular syndrome.
DR Orphanet; 741; Familial mitral valve prolapse.
DR PharmGKB; PA33000; -.
DR VEuPathDB; HostDB:ENSG00000166341; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161822; -.
DR HOGENOM; CLU_000265_2_0_1; -.
DR InParanoid; Q96JQ0; -.
DR OMA; RVMAYDP; -.
DR OrthoDB; 34489at2759; -.
DR PhylomeDB; Q96JQ0; -.
DR TreeFam; TF316403; -.
DR PathwayCommons; Q96JQ0; -.
DR SignaLink; Q96JQ0; -.
DR BioGRID-ORCS; 8642; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; DCHS1; human.
DR GeneWiki; DCHS1; -.
DR GenomeRNAi; 8642; -.
DR Pharos; Q96JQ0; Tbio.
DR PRO; PR:Q96JQ0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96JQ0; protein.
DR Bgee; ENSG00000166341; Expressed in tendon of biceps brachii and 184 other tissues.
DR Genevisible; Q96JQ0; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0072137; P:condensed mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0003192; P:mitral valve formation; IMP:UniProtKB.
DR GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; PTHR24027; 8.
DR Pfam; PF00028; Cadherin; 23.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 27.
DR SUPFAM; SSF49313; SSF49313; 27.
DR PROSITE; PS00232; CADHERIN_1; 18.
DR PROSITE; PS50268; CADHERIN_2; 27.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Deafness; Disease variant;
KW Glycoprotein; Intellectual disability; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..3298
FT /note="Protocadherin-16"
FT /id="PRO_0000004000"
FT TOPO_DOM 43..2940
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2941..2961
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2962..3298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..143
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 144..255
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 256..362
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 367..472
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 474..578
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 579..685
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 686..790
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 791..894
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 895..1000
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1001..1111
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1112..1211
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1218..1324
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1333..1436
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1437..1546
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1547..1649
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1650..1751
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1752..1855
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1856..1960
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1965..2068
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2069..2171
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2172..2277
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2278..2376
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2377..2482
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2483..2602
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2603..2706
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2707..2813
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2814..2933
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 2065..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2986..3040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3062..3082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3233..3298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3239..3262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PVD3"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 197
FT /note="P -> L (found in a MVP2 patient also carrying
FT pathogenic mutation H-2513; has no significant effect on
FT protein levels; dbSNP:rs145099391)"
FT /evidence="ECO:0000269|PubMed:26258302"
FT /id="VAR_075048"
FT VARIANT 1583
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs148882462)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036110"
FT VARIANT 1949
FT /note="T -> M (in dbSNP:rs4758443)"
FT /id="VAR_048577"
FT VARIANT 2172
FT /note="L -> Q (in dbSNP:rs56920123)"
FT /id="VAR_061074"
FT VARIANT 2330
FT /note="R -> C (in MVP2; loss-of-function mutation; results
FT in reduced protein levels; results in increased protein
FT degradation; dbSNP:rs768737101)"
FT /evidence="ECO:0000269|PubMed:26258302"
FT /id="VAR_075049"
FT VARIANT 2331
FT /note="V -> I (in dbSNP:rs7924553)"
FT /id="VAR_048578"
FT VARIANT 2359
FT /note="R -> C (in dbSNP:rs2659875)"
FT /id="VAR_048579"
FT VARIANT 2370
FT /note="N -> I (in VMLDS1; dbSNP:rs483352919)"
FT /evidence="ECO:0000269|PubMed:24056717"
FT /id="VAR_070928"
FT VARIANT 2513
FT /note="R -> H (in MVP2; the patient also carries L-197;
FT loss-of-function mutation; results in reduced protein
FT levels; results in increased protein degradation;
FT dbSNP:rs201457110)"
FT /evidence="ECO:0000269|PubMed:26258302"
FT /id="VAR_075050"
SQ SEQUENCE 3298 AA; 346181 MW; 6EE8D28BEF0795DB CRC64;
MQKELGIVPS CPGMKSPRPH LLLPLLLLLL LLLGAGVPGA WGQAGSLDLQ IDEEQPAGTL
IGDISAGLPA GTAAPLMYFI SAQEGSGVGT DLAIDEHSGV VRTARVLDRE QRDRYRFTAV
TPDGATVEVT VRVADINDHA PAFPQARAAL QVPEHTAFGT RYPLEPARDA DAGRLGTQGY
ALSGDGAGET FRLETRPGPD GTPVPELVVT GELDRENRSH YMLQLEAYDG GSPPRRAQAL
LDVTLLDIND HAPAFNQSRY HAVVSESLAP GSPVLQVFAS DADAGVNGAV TYEINRRQSE
GDGPFSIDAH TGLLQLERPL DFEQRRVHEL VVQARDGGAH PELGSAFVTV HVRDANDNQP
SMTVIFLSAD GSPQVSEAAP PGQLVARISV SDPDDGDFAH VNVSLEGGEG HFALSTQDSV
IYLVCVARRL DREERDAYNL RVTATDSGSP PLRAEAAFVL HVTDVNDNAP AFDRQLYRPE
PLPEVALPGS FVVRVTARDP DQGTNGQVTY SLAPGAHTHW FSIDPTSGII TTAASLDYEL
EPQPQLIVVA TDGGLPPLAS SATVSVALQD VNDNEPQFQR TFYNASLPEG TQPGTCFLQV
TATDADSGPF GLLSYSLGAG LGSSGSPPFR IDAHSGDVCT TRTLDRDQGP SSFDFTVTAV
DGGGLKSMVY VKVFLSDEND NPPQFYPREY AASISAQSPP GTAVLRLRAH DPDQGSHGRL
SYHILAGNSP PLFTLDEQSG LLTVAWPLAR RANSVVQLEI GAEDGGGLQA EPSARVDISI
VPGTPTPPIF EQLQYVFSVP EDVAPGTSVG IVQAHNPPGR LAPVTLSLSG GDPRGLFSLD
AVSGLLQTLR PLDRELLGPV LELEVRAGSG VPPAFAVARV RVLLDDVNDN SPAFPAPEDT
VLLPPNTAPG TPIYTLRALD PDSGVNSRVT FTLLAGGGGA FTVDPTTGHV RLMRPLGPSG
GPAHELELEA RDGGSPPRTS HFRLRVVVQD VGTRGLAPRF NSPTYRVDLP SGTTAGTQVL
QVQAQAPDGG PITYHLAAEG ASSPFGLEPQ SGWLWVRAAL DREAQELYIL KVMAVSGSKA
ELGQQTGTAT VRVSILNQNE HSPRLSEDPT FLAVAENQPP GTSVGRVFAT DRDSGPNGRL
TYSLQQLSED SKAFRIHPQT GEVTTLQTLD REQQSSYQLL VQVQDGGSPP RSTTGTVHVA
VLDLNDNSPT FLQASGAAGG GLPIQVPDRV PPGTLVTTLQ AKDPDEGENG TILYTLTGPG
SELFSLHPHS GELLTAAPLI RAERPHYVLT LSAHDQGSPP RSASLQLLVQ VLPSARLAEP
PPDLAERDPA APVPVVLTVT AAEGLRPGSL LGSVAAPEPA GVGALTYTLV GGADPEGTFA
LDAASGRLYL ARPLDFEAGP PWRALTVRAE GPGGAGARLL RVQVQVQDEN EHAPAFARDP
LALALPENPE PGAALYTFRA SDADGPGPNS DVRYRLLRQE PPVPALRLDA RTGALSAPRG
LDRETTPALL LLVEATDRPA NASRRRAARV SARVFVTDEN DNAPVFASPS RVRLPEDQPP
GPAALHVVAR DPDLGEAARV SYRLASGGDG HFRLHSSTGA LSVVRPLDRE QRAEHVLTVV
ASDHGSPPRS ATQVLTVSVA DVNDEAPTFQ QQEYSVLLRE NNPPGTSLLT LRATDPDVGA
NGQVTYGGVS SESFSLDPDT GVLTTLRALD REEQEEINLT VYAQDRGSPP QLTHVTVRVA
VEDENDHAPT FGSAHLSLEV PEGQDPQTLT MLRASDPDVG ANGQLQYRIL DGDPSGAFVL
DLASGEFGTM RPLDREVEPA FQLRIEARDG GQPALSATLL LTVTVLDAND HAPAFPVPAY
SVEVPEDVPA GTLLLQLQAH DPDAGANGHV TYYLGAGTAG AFLLEPSSGE LRTAAALDRE
QCPSYTFSVS AVDGAAAGPL STTVSVTITV RDVNDHAPTF PTSPLRLRLP RPGPSFSTPT
LALATLRAED RDAGANASIL YRLAGTPPPG TTVDSYTGEI RVARSPVALG PRDRVLFIVA
TDLGRPARSA TGVIIVGLQG EAERGPRFPR ASSEATIREN APPGTPIVSP RAVHAGGTNG
PITYSILSGN EKGTFSIQPS TGAITVRSAE GLDFEVSPRL RLVLQAESGG AFAFTVLTLT
LQDANDNAPR FLRPHYVAFL PESRPLEGPL LQVEADDLDQ GSGGQISYSL AASQPARGLF
HVDPTTGTIT TTAILDREIW AETRLVLMAT DRGSPALVGS ATLTVMVIDT NDNRPTIPQP
WELRVSEDAL LGSEIAQVTG NDVDSGPVLW YVLSPSGPQD PFSVGRYGGR VSLTGPLDFE
QCDRYQLQLL AHDGPHEGRA NLTVLVEDVN DNAPAFSQSL YQVMLLEHTP PGSAILSVSA
TDRDSGANGH ISYHLASPAD GFSVDPNNGT LFTIVGTVAL GHDGSGAVDV VLEARDHGAP
GRAARATVHV QLQDQNDHAP SFTLSHYRVA VTEDLPPGST LLTLEATDAD GSRSHAAVDY
SIISGNWGRV FQLEPRLAEA GESAGPGPRA LGCLVLLEPL DFESLTQYNL TVAAADRGQP
PQSSVVPVTV TVLDVNDNPP VFTRASYRVT VPEDTPVGAE LLHVEASDAD PGPHGLVRFT
VSSGDPSGLF ELDESSGTLR LAHALDCETQ ARHQLVVQAA DPAGAHFALA PVTIEVQDVN
DHGPAFPLNL LSTSVAENQP PGTLVTTLHA IDGDAGAFGR LRYSLLEAGP GPEGREAFAL
NSSTGELRAR VPFDYEHTES FRLLVGAADA GNLSASVTVS VLVTGEDEYD PVFLAPAFHF
QVPEGARRGH SLGHVQATDE DGGADGLVLY SLATSSPYFG INQTTGALYL RVDSRAPGSG
TATSGGGGRT RREAPRELRL EVIARGPLPG SRSATVPVTV DITHTALGLA PDLNLLLVGA
VAASLGVVVV LALAALVLGL VRARSRKAEA APGPMSQAAP LASDSLQKLG REPPSPPPSE
HLYHQTLPSY GGPGAGGPYP RGGSLDPSHS SGRGSAEAAE DDEIRMINEF PRVASVASSL
AARGPDSGIQ QDADGLSDTS CEPPAPDTWY KGRKAGLLLP GAGATLYREE GPPATATAFL
GGCGLSPAPT GDYGFPADGK PCVAGALTAI VAGEEELRGS YNWDYLLSWC PQFQPLASVF
TEIARLKDEA RPCPPAPRID PPPLITAVAH PGAKSVPPKP ANTAAARAIF PPASHRSPIS
HEGSLSSAAM SPSFSPSLSP LAARSPVVSP FGVAQGPSAS ALSAESGLEP PDDTELHI
