PCD16_MOUSE
ID PCD16_MOUSE Reviewed; 3291 AA.
AC E9PVD3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protocadherin-16;
DE AltName: Full=Protein Dchs1;
DE AltName: Full=Protein dachsous homolog 1;
DE Flags: Precursor;
GN Name=Dchs1;
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 [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 [2]
RP SUBCELLULAR LOCATION, AND HETEROPHILIC INTERACTION WITH FAT4.
RX PubMed=19506035; DOI=10.1083/jcb.200811030;
RA Ishiuchi T., Misaki K., Yonemura S., Takeichi M., Tanoue T.;
RT "Mammalian Fat and Dachsous cadherins regulate apical membrane organization
RT in the embryonic cerebral cortex.";
RL J. Cell Biol. 185:959-967(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3048, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Spleen;
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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=21303848; DOI=10.1242/dev.057166;
RA Mao Y., Mulvaney J., Zakaria S., Yu T., Morgan K.M., Allen S., Basson M.A.,
RA Francis-West P., Irvine K.D.;
RT "Characterization of a Dchs1 mutant mouse reveals requirements for Dchs1-
RT Fat4 signaling during mammalian development.";
RL Development 138:947-957(2011).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
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).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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).
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:24056717,
CC ECO:0000269|PubMed:26258302}.
CC -!- SUBUNIT: Heterophilic interaction with FAT4; this interaction affects
CC their respective protein levels.
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:0000269|PubMed:19506035}.
CC -!- TISSUE SPECIFICITY: Expressed in the epicardium and atrioventricular
CC sulcus (at protein level). {ECO:0000269|PubMed:26258302}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all layers of the developing brain,
CC with expression being most prominent at the ventricular margin.
CC Expressed throughout cardiac development in the endothelial cells and
CC interstitial cells of the developing valves (at protein level).
CC Expression is observed in the endocardium and mesenchyme of the
CC superior and inferior cushions at day 11.5 dpc. At days 13.5 dpc and
CC 15.5 dpc, expression is observed in the forming anterior and posterior
CC mitral leaflets (PubMed:26258302). {ECO:0000269|PubMed:24056717,
CC ECO:0000269|PubMed:26258302}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit postnatal lethality,
CC growth retardation, small lungs, abnormal cochlea morphology, abnormal
CC kidney morphology, cardiovascular abnormalities and skeletal
CC abnormalities. DCHS1 and FAT4 single mutants and DCHS1/FAT4 double
CC mutants have similar phenotypes. Heterozygous mice lacking one DCHS1
CC allele exhibit mitral valve prolapse with posterior leaflet elongation,
CC leaflet thickening, and myxomatous degeneration with increased
CC proteoglycan accumulation in both mitral leaflets (PubMed:26258302).
CC {ECO:0000269|PubMed:21303848, ECO:0000269|PubMed:26258302}.
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DR EMBL; AC121823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52351.1; -.
DR RefSeq; NP_001156415.1; NM_001162943.1.
DR SMR; E9PVD3; -.
DR BioGRID; 231434; 2.
DR IntAct; E9PVD3; 1.
DR STRING; 10090.ENSMUSP00000077574; -.
DR GlyConnect; 2648; 3 N-Linked glycans (2 sites).
DR GlyGen; E9PVD3; 4 sites, 3 N-linked glycans (2 sites).
DR iPTMnet; E9PVD3; -.
DR PhosphoSitePlus; E9PVD3; -.
DR jPOST; E9PVD3; -.
DR MaxQB; E9PVD3; -.
DR PaxDb; E9PVD3; -.
DR PeptideAtlas; E9PVD3; -.
DR PRIDE; E9PVD3; -.
DR ProteomicsDB; 294341; -.
DR Antibodypedia; 64000; 67 antibodies from 16 providers.
DR Ensembl; ENSMUST00000078482; ENSMUSP00000077574; ENSMUSG00000036862.
DR GeneID; 233651; -.
DR KEGG; mmu:233651; -.
DR UCSC; uc009izh.2; mouse.
DR CTD; 8642; -.
DR MGI; MGI:2685011; Dchs1.
DR VEuPathDB; HostDB:ENSMUSG00000036862; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161822; -.
DR HOGENOM; CLU_000265_2_0_1; -.
DR InParanoid; E9PVD3; -.
DR OMA; RVMAYDP; -.
DR OrthoDB; 34489at2759; -.
DR PhylomeDB; E9PVD3; -.
DR TreeFam; TF316403; -.
DR BioGRID-ORCS; 233651; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Dchs1; mouse.
DR PRO; PR:E9PVD3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PVD3; protein.
DR Bgee; ENSMUSG00000036862; Expressed in internal carotid artery and 138 other tissues.
DR ExpressionAtlas; E9PVD3; baseline and differential.
DR Genevisible; E9PVD3; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
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: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:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0003273; P:cell migration involved in endocardial cushion formation; ISO:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
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; IMP:MGI.
DR GO; GO:0072137; P:condensed mesenchymal cell proliferation; IMP:MGI.
DR GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IC:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:UniProtKB.
DR GO; GO:0035329; P:hippo signaling; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0003192; P:mitral valve formation; ISO:MGI.
DR GO; GO:0003183; P:mitral valve morphogenesis; IMP:MGI.
DR GO; GO:0072006; P:nephron development; IGI:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0043931; P:ossification involved in bone maturation; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:MGI.
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; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..3291
FT /note="Protocadherin-16"
FT /id="PRO_0000429045"
FT TOPO_DOM 36..2933
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 2934..2954
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2955..3291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 37..137
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..249
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 250..356
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 369..466
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 476..572
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 573..679
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 680..784
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 785..888
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 889..994
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 995..1105
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1100..1205
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1218..1317
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1326..1429
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1430..1539
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1539..1642
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1643..1744
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1745..1848
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1849..1953
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1976..2061
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2062..2164
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2165..2270
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2270..2369
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2370..2475
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2476..2595
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2596..2699
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2700..2806
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2807..2926
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 2867..2886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2978..3033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3051..3081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3226..3291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3232..3255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3048
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 3291 AA; 346384 MW; 0C0C1E720AE82BE3 CRC64;
MQKELSVALS CPGMKSLRTL LPLLVLLGAT VPGSWGQAGS LDLQIDEEQP AGTLIGDISA
GLPPGTAPPP MYFISAQEGS GVGTDLAIDE HSGVVRTARV LDRERRDRYR FTAVTPDGAT
VEVTVRVADI NDHAPAFPQA RAALQIPEHT ALGTRYPLEP ARDADAGRLG TQGYALSGDG
AGETFRLETR PGPGGAPVPE LVIAGELDRE NRSHYMLQLE AYDGGSPPRR AQALLDVTLL
DINDHAPAFN QSRYHAVVSE SLAPGSPVLQ VFASDADAGA NGAVTYEINR RQSEGDGPFS
IDAHTGFLRL ERPLDFEQRR VHELVVQARD GGAHPELGSA FVTVHVRDAN DNQPSMTVIF
LSADGSPRVS EAAPPGQLVA RISVSDPDDG DFAHVNVSLE GGEGHFALST QDSVIYLVCV
ARRLDREERD VYNLRVTATD SGSPPLRAEA AFVLHVTDVN DNAPAFDRQL YRPEPLPEVA
LPGSFVVRVT ARDPDQGTNG QITYSLAPGT HTHWFSIDPT SGIITTAATL DYELEPQPQL
IVVATDGGLP PLVSSATVSV ALQDVNDNEP QFQRTFYNAS LPEGTQPGTC FLQVTATDAD
SGPFGLLSYS LGAGLGASGS PPFRIDAHSG DVCTTRTLDR DQGPSSFDFT VTAIDGGGLK
SMVYVKVFVA DENDNPPQFY PREYAASLSA QSTPGTAVLR VHAHDPDQGP HGRLSYHILA
GNSPPLFALD AHSGLLTVAW PLGRRANSVV QLEIGAQDGG GLQAEPIARV NISIVPGTPT
PPIFEQLQYV FSVPEDVAPG TSVGIIQAHN PPGRLGPVTL TLSGGDPRGL FSLDSPSGLL
KTLRPLDREL LGPVLELEVR AGSGTPPVFA VARIRVLLDD VNDNSPAFPA PEDTVLLPQN
TAPGTPIYTL RALDPDSGAN SRITFNLLAG GDGLFTVDPT TGHVRLMGPL GPPGGPAHEL
EVEARDGGSP PRTSHFRLRV VIQDLGIHGL APRFDSPTYR VDLPSGTTTG TQILQVQAQA
PDGSPVTYHL AADGASSPFG LESQSGWLWV RTALDRESQE LYTLKVMAVS GSKAELGQQT
GTATVRVIIL NQNDHSPRLS EEPTFLAVAE NQPPGTSVGR VFATDRDSGP NGRLTYSLQQ
LSEDSKAFRI HPQTGEVTTL QTLDREQQSS FQLLVQVQDG GSPPRSATGT VHVAVLDLND
NSPTFLQASG AAGGGLPIQV PDRVPPGTLV TTLQAKDPDE GENGTILYTL TGPGSELFSL
HPHTGELHTA ASLVRAERPH YVLTLSAHDQ GSPPRSASLQ LLVQVLPSTR VVESPDLIEA
DSAATVPVVL TVTAAEGLRP GSLLGSVAPQ EPASVGVLTY TLVGGADPEG TFALDSASGR
LYLARPLDFE AGPAWRALTV RAEGPGGAGA RLLRVQVRVQ DENEHAPTFA RDPLALALPE
NPDPGATLYT FRASDADGPG PNSEVRYRLL RQEPPVPALR LDARTGALSA PRGLDRETTP
ALLLLVEATD RPANASRRRA ARVSARVFVT DENDNAPVFA SPSRVRLPED QPPGPAALHV
VARDPDLGEA ARVSYRLAAG GDGHFRLHAT TGALSVVRPL DREQRAEHVL TVVALDHGSP
PRSSTQLLTV SVVDVNDEAP AFPQQEYNVI LRENSPPGTS LLTLKATDPD LGANGQVTYG
GVSGESFSLD PNTGVLTTLR ALDREEQEEI YLTVYARDRG LPPLLTHITV RVTVEDENDH
TPTFGNTHLS LEVPEGQDPQ TLTTLRASDP DGGLNGQLQY RILDGDSSGA FALDLTSGEF
GTMRPLDREV EPAFQLQIEA RDGGQPALSA TLLVTVTVLD ANDHAPVFPV PSYSVEVPED
APVGTLLLQL QAHDPDDGDN GRVMYYLGAG TAGAFLLEPT SGELSTATAL DREHCASYAF
SVTAVDGAAA GPLSTTVPIT ITVRDVNDHA PAFPTSPLRL RLPRPGPSLN KPTLALATLR
AEDRDAGANA SILYRLAGTP PPGTTVDSYT GEIRVARSPV ALGPQDRVLF IVATDLGRPA
RSATGVVVVG IQGEPERGPR FPRTSSEAVL RENAPPGTPV ISPKAVHSGG SNGPITYSIL
SGNERGIFSI QPSTGAITVR SAEGLDFETS PRLRLVLQAE SGGAFAFSVL TLTLQDANDN
APRFLRPHYV AFLPESRPLE GPLLQVEADD LDQGSGGQIS YSLAASQPAR GLFHVDPATG
TITTTAILDR EIWAETRLVL MATDRGSPAL VGSATLTVMV IDTNDNRPTI PQPWELRVSE
DALLGSEIAQ VTGNDVDSGP VLWYVLSPSG PQDPFSIGRY GGRVSLTGPL DFEQCDHYHL
QLLAHDGPHE GHANLTVLVE DVNDNVPTFS QSLYQVMMLE HTPPGSAILS VSATDRDSGA
NGHISYHLAS PAEGFRVDPN NGTLFTTVGA MALGHEGPGV VDVVLEARDH GAPGRTAQAT
VHVQLKDQND HAPSFTLPHY RVAVSEDLPP GSTLLTLEAT DADGSRTHAT VDYSIISGNR
GRVFQLEPRL AEVGDGVGPG PQALGCLVLL EPLDFESLTQ YNLTVAAADR GQPPRSSAVP
VTVTVLDVND NPPVFTRASY RVTVPEDMPV GAELLHVEAS DADPGPHGLV HFTLSSGDPL
GLFELDENSG ALRLSRPLDC ETQAQHQLVV QAADPAGTHF SLVPVTVEVQ DVNDHGPAFP
LSLLSTSLAE NQPPGTLVTT LHAIDGDAGT FGRLRYSLLE AVPGPEGREA FSLNSSTGEL
RARVPFDYEH TGSFRLLVGA ADAGNLSASV TVSVLITGED EYDPVFLAPS FHFQVPEGAQ
RGHSLGHVQA TDEDGGADGL VLYSLATSSP YFGINQTTGA LYLRVDSRAP GSGTTTSGGG
GRTRREAPRE LRLEVVARGP LPGSRSATVP VTVDITHTAL GLAPDLNLLL VGAVAASLGV
VVVLALAALV LGLVRARSRK AEAAPGPMSQ TAPIASSSLQ KLGREPPSPP PSEHLYHQTL
PSYGGPGAGG PYPRGGSLDP SHSSGRGSAE AAEDDEIRMI NEFPRVASVA SSLAARGPDS
GIQQDADGLS DTSCEPPAPD TWYKGRKAGL LLPGAGATLY REEGPPATAT AFLGGCGLSP
APAGDYGFPA DGKPCVAGAL TAIVAGEEEL RGSYNWDYLL SWCPQFQPLA SVFTEIARLK
DEARPCPPAP RIDPPPLITA VAHPGAKSVP PKPASTAVAR AIFPPASHRS PISHEGSLSS
AAMSPSFSPS LSPLAARSPV VSPFGVAQGP SASALSTESG LEPPDDTELR I
