CAD23_RAT
ID CAD23_RAT Reviewed; 3317 AA.
AC P58365;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Cadherin-23;
DE AltName: Full=Otocadherin;
DE Flags: Precursor;
GN Name=Cdh23;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
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).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells. CDH23 is required for establishing and/or maintaining
CC the proper organization of the stereocilia bundle of hair cells in the
CC cochlea and the vestibule during late embryonic/early postnatal
CC development. It is part of the functional network formed by USH1C,
CC USH1G, CDH23 and MYO7A that mediates mechanotransduction in cochlear
CC hair cells. Required for normal hearing.
CC {ECO:0000250|UniProtKB:Q9H251}.
CC -!- SUBUNIT: antiparallel heterodimer with PCDH15 (By similarity).
CC Interacts with USH1C and USH1G (By similarity).
CC {ECO:0000250|UniProtKB:Q99PF4, ECO:0000250|UniProtKB:Q9H251}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9H251};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain.
CC {ECO:0000250|UniProtKB:P12830}.
CC -!- DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent heterophilic
CC interaction with PCDH15. {ECO:0000250|UniProtKB:Q99PF4}.
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; AB053447; BAB61904.1; -; mRNA.
DR RefSeq; NP_446096.1; NM_053644.1.
DR SMR; P58365; -.
DR STRING; 10116.ENSRNOP00000048338; -.
DR GlyGen; P58365; 42 sites.
DR iPTMnet; P58365; -.
DR PhosphoSitePlus; P58365; -.
DR PaxDb; P58365; -.
DR PRIDE; P58365; -.
DR GeneID; 114102; -.
DR KEGG; rno:114102; -.
DR UCSC; RGD:619760; rat.
DR CTD; 64072; -.
DR RGD; 619760; Cdh23.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P58365; -.
DR OrthoDB; 17702at2759; -.
DR PhylomeDB; P58365; -.
DR PRO; PR:P58365; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0098683; C:cochlear hair cell ribbon synapse; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0060091; C:kinocilium; ISO:RGD.
DR GO; GO:0001917; C:photoreceptor inner segment; ISO:RGD.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032420; C:stereocilium; ISO:RGD.
DR GO; GO:0032426; C:stereocilium tip; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0008344; P:adult locomotory behavior; ISO:RGD.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISO:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0050957; P:equilibrioception; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0042491; P:inner ear auditory receptor cell differentiation; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISO:RGD.
DR GO; GO:0048563; P:post-embryonic animal organ morphogenesis; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0060013; P:righting reflex; ISO:RGD.
DR GO; GO:0050953; P:sensory perception of light stimulus; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR033030; CDH23.
DR PANTHER; PTHR24025:SF18; PTHR24025:SF18; 2.
DR Pfam; PF00028; Cadherin; 25.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 26.
DR SUPFAM; SSF49313; SSF49313; 27.
DR PROSITE; PS00232; CADHERIN_1; 17.
DR PROSITE; PS50268; CADHERIN_2; 27.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Hearing; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..3317
FT /note="Cadherin-23"
FT /id="PRO_0000003826"
FT TOPO_DOM 24..3062
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3063..3083
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3084..3317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 133..236
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 237..348
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 349..458
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 459..559
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 560..669
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 670..782
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 777..888
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 889..993
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 994..1100
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1101..1206
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1208..1311
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1312..1416
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1418..1525
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1527..1632
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1633..1742
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1743..1849
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1850..1957
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1958..2067
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2068..2172
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2173..2291
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2295..2400
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2401..2507
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2508..2609
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2612..2720
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2727..2844
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2845..2973
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 999
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1016
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1649
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1816
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1855
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1900
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2012
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2048
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2894
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2939
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2979
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 3317 AA; 365455 MW; CEF397A066BF0986 CRC64;
MRHPPVTWCA MLWLLMLVSG SWGQVNRLPF FTNHFFDTYL LISEDTPVGS SVTQLLARDM
DNDPLVFGVS GEEASRFFAV EPDTGVVWLR QPLDRETKSE FTVEFSVSDH QGVITRKVNI
QVGDVNDNAP TFHNQPYSVR IPENTPVGTP IFIVNATDPD LGAGGSVLYS FQPPSQFFAI
DSARGIVTVI RELDYEVTQA YQLTVNATDQ DKTRPLSTLA NLAIIITDVQ DMDPIFINLP
YSTNIYEHSP PGTTVRVITA VDQDKGRPRG IGYTIVSGNT NSIFALDYIS GALTLNGLLD
RENPLYSHGF ILTVKGTELN DDRSPSDATV TTTFNILVID INDNAPEFNS SEYSVAITEL
AQVGFALPLF IQVVDKDEGL NSMFEVYLVG NNSHHFIISP TSVQGKADIR IRVAIPLDYE
TVDRYDFDLF ANESVPDHVG YAKVKITLIN ENDNRPIFSQ PLYNVSLYEN ITVGTSVLTV
LATDNDVGTF GEVNYFFSDD PDRFSLDKDT GLIMLIARLD YELIQRFTLT VIARDGGGEE
TTGRVRINVL DVNDNVPTFQ KDAYVGALRE NEPSVTQLVR LRATDEDSPP NNLITYSIVN
ASAFGSYFDI SVYEGYGVIS VSRPLDYEQI PNGLIYLTVM AKDAGNPPLY STVPVTIEVF
DENDNPPTFS KPAYFVSVVE NIMAGATVLF LNATDLDRSR EYGQESIIYS LEGSSQFRIN
ARSGEITTTS LLDRETKAEY ILIVRAVDGG VGHNQKTGIA TVNVTLLDIN DNHPTWKDAP
YYINLVEMTP PDSDVTTVVA VDPDLGKNGT LVYSIQPPNK FYSLNSTTGK IRTTHVMLDR
ENPDPVEAEL MRKIIVSVTD CGRPPLKATS SATVFVNLLD LNDNDPTFQN LPFVAEVLEG
TPAGVSVYQV VAIDLDEGLN GLVSYRMQVG MPRMDFVINS TSGVVTTTAE LDRERIAEYQ
LRVVASDAGT PTKSSTSTLT IRVLDVNDET PTFFPAVYNV SVSEDVPREF RVVWLNCTDN
DVGLNAELSY FITAGNVDGK FSVGYRDAVV RTVVGLDRET TAAYTLVLEA IDNVPVGKRR
TGTATVFVTV LDVNDNRPIF LQSSYEASVP EDIPEGHSIV QLKATDADEG EFGRVWYRIL
HGNHGNNFRL HVSSGLLVRG PRPLDRERNS SHVLMAEAYN HDLGPMRSSV RVIVYVEDVN
DEAPVFTQQQ YNRLGLRETA GIGTSVIVVR ATDRDTGDGG LVNYRILSGA EGKFEIDEST
GLIVTVDYLD YETKTSYLMN VSATDGAPPF NQGFCSVYVT LLNELDEAVQ FSNASYEAVI
MENLALGTEI VRVQAYSIDN LNQITYRFDA YTSAQAKALF KIDAITGVIT VKGLVDREKG
DFYTLTVVAD DGGPKVDSTV KVYVTVLDEN DNSPRFDFTS DSAISVPEDC PVGQRVATVK
ARDPDAGSNG QVVFSLASGN IAGAFEIITS NDSIGEVFVA KPLDREELDH YILKIVASDR
GTPPRKKDHI LQVTILDVND NPPVIESPFG YNVSVNENVG GGTSVVQVRA TDRDIGINSV
LSYYITEGNE DMTFRMDRIS GEIATRPAPP DRERQNFYHL VVTVEDEGTP TLSATTHVYV
TIVDENDNAP VFQQPHYEVV LDEGPDTVNT SLITVQALDL DEGPNGTVTY AIVAGNIINT
FRINRRTGVI TAAKELDYEI SHGRYTLIVT ATDQCPILSH RLTSTTTVLV NVNDINDNVP
TFPRDYEGPF DVTEGQPGPR VWTFLAHDRD SGPNGQVEYS VVDGDPLGEF VISPVEGVLR
VRKDVELDRE TIAFYNLTIC ARDRGVPPLS STMLVGIRVL DINDNDPVLL NLPMNITISE
NSPVSSFVAH VLASDADSGC NALLTFNITA GNRERAFFIN ATTGIVTVNR PLDRERIPEY
RLTVSVKDNP ENPRIARKDF DLLLVSLADE NDNHPLFTEG TYQAEVMENS PAGTPLTVLN
GPILALDADE DVYAVVTYQL LGTHSDLFVI DNSTGVVTVR SGVIIDREAF SPPFLELLLL
AEDVGQLNGT AYLFITILDD NDNWPTFSPP AYTVHLLENC PPGFSVLQIT ATDEDSGLNG
ELVYRIEAGA QDRFLIHPVT GVIRVGNATI DREEQESYRL TVVATDRGTV PLSGTATVTI
LIDDINDSRP EFLNPIQTVS VLESTEPGTV IANVTAIDLD LNPKLEYHIL SIVAKDDTDR
LVPDQEDAFA VNINTGSVIV KSPLNRELVA TYEVTLSVID NASDLPERSV SVPNAKLTVN
ILDVNDNTPQ FKPFGITYYT ERVLEGATPG TTLIAVAAVD PDKGLNGLIT YTLLDLIPPG
YVQLEDSSAG KVIANRTVDY EEVHWLNFTV RASDNGSPPR AAEIPVYLEI VDINDNNPIF
DQLSYQEAVF EDVAVGTVIL RVTATDADSG NFALIEYSLV DGEGKFAINP NTGDIYVLSS
LDREKKDHYI LTALAKDNPG DVASNRRENS VQVVIRVLDV NDCRPQFSKP QFSTSVYENE
PAGTSVITML ATDQDEGSNG QLTYSLEGPG MEAFSVDMDS GLVTTQRPLQ SYERFNLTVV
ATDGGEPPLW GTTMLLVEVI DVNDNRPVFV RPPNGTILHI KEEIPLRSNV YEVYATDKDE
GLNGAVRYSF LKSTGNRDWE YFTIDPISGL IQTAQRLDRE KQAVYSLILV ASDLGQPVPY
ETMQPLQVAL EDIDDNEPLF VRPPKGSPQY QLLTVPEHSP RGTLVGNVTG AVDADEGPNA
IVYYFIAAGN EDKNFHLQPD GRLLVLRDLD RETEAIFSFI VKASSNRSWT PPRGPSPALD
LLTDLTLQEV RVVLEDINDQ PPRFTKAEYT AGVATDAKVG SELIQVLALD ADIGNNSLVF
YGILAIHYFR ALANDSEDVG QVFTMGSVDG ILRTFDLFMA YSPGYFVVDI VARDLAGHND
TAIIGIYILR DDQRVKIVIN EIPDRVRGFE EEFIRLLSNI TGAIVNTDDV QFHVDMKGRV
NFAQTELLIH VVNRDTNRIL DVDRVIQMID ENKEQLRNLF RNYNVLDVQP AISVQLPDDM
SALQMAIIVL AILLFLAAML FVLMNWYYRT IHKRKLKAIV AGSAGNRGFI DIMDMPNTNK
YSFDGANPVW LDPFCRNLEL AAQAEHEDDL PENLSEIADL WNSPTRTHGT FGREPAAVKP
EDDRYLRAAI QEYDNIAKLG QIIREGPIKL IHTDLEEEPG DHSPGQGSLR FRHKPPTELK
GPDGIHIVHG STGTLLATDL NSLPEDDQKG LDRSLETLTA SEATAFERNA RTESAKSTPL
HKLRDVIMES PLEITEL