ID CADH3_CAEEL Reviewed; 3343 AA.
AC P34616;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 27-MAR-2024, entry version 176.
DE RecName: Full=Cadherin-3;
DE Flags: Precursor;
GN Name=cdh-3; ORFNames=ZK112.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=9012534; DOI=10.1242/dev.122.12.4149;
RA Pettitt J., Wood W.B., Plasterk R.H.;
RT "cdh-3, a gene encoding a member of the cadherin superfamily, functions in
RT epithelial cell morphogenesis in Caenorhabditis elegans.";
RL Development 122:4149-4157(1996).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15960981; DOI=10.1016/j.cell.2005.03.031;
RA Sherwood D.R., Butler J.A., Kramer J.M., Sternberg P.W.;
RT "FOS-1 promotes basement-membrane removal during anchor-cell invasion in C.
RT elegans.";
RL Cell 121:951-962(2005).
CC -!- FUNCTION: Cell adhesion protein involved in the control of epithelial
CC morphogenesis (PubMed:9012534). Together with metalloproteinase zmp-1
CC and hemicentin him-4, plays a role in anchor cell (AC) invasion during
CC postembryonic vulval development (PubMed:15960981).
CC {ECO:0000269|PubMed:15960981, ECO:0000269|PubMed:9012534}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15960981};
CC Single-pass type I membrane protein {ECO:0000305}. Basolateral cell
CC membrane {ECO:0000269|PubMed:15960981}. Cell junction
CC {ECO:0000250|UniProtKB:Q9BYE9}.
CC -!- TISSUE SPECIFICITY: Expressed in the anchor cell.
CC {ECO:0000269|PubMed:15960981}.
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. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: 2 percent of mutants have a delay in anchor cell
CC invasion. In 7 percent of zmp-1 and cdh-3 double mutants and in 25
CC percent of cdh-3, him-4 and zmp-1 triple mutants, anchor cell invasion
CC is delayed. {ECO:0000269|PubMed:15960981}.
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; FO080308; CCD62768.1; -; Genomic_DNA.
DR PIR; S44887; S44887.
DR RefSeq; NP_498687.2; NM_066286.4.
DR STRING; 6239.ZK112.7.1; -.
DR GlyCosmos; P34616; 46 sites, No reported glycans.
DR EPD; P34616; -.
DR PaxDb; 6239-ZK112-7; -.
DR PeptideAtlas; P34616; -.
DR EnsemblMetazoa; ZK112.7.1; ZK112.7.1; WBGene00000395.
DR GeneID; 176085; -.
DR KEGG; cel:CELE_ZK112.7; -.
DR UCSC; ZK112.7; c. elegans.
DR AGR; WB:WBGene00000395; -.
DR WormBase; ZK112.7; CE50490; WBGene00000395; cdh-3.
DR eggNOG; KOG1219; Eukaryota.
DR GeneTree; ENSGT00940000167267; -.
DR HOGENOM; CLU_225093_0_0_1; -.
DR InParanoid; P34616; -.
DR OrthoDB; 2882115at2759; -.
DR PhylomeDB; P34616; -.
DR PRO; PR:P34616; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000395; Expressed in pharyngeal muscle cell (C elegans) and 13 other cell types or tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; TAS:WormBase.
DR GO; GO:0034769; P:basement membrane disassembly; IGI:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; TAS:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR CDD; cd11304; Cadherin_repeat; 14.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 13.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF445; CADHERIN-87A; 1.
DR Pfam; PF00028; Cadherin; 7.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 13.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 14.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00232; CADHERIN_1; 8.
DR PROSITE; PS50268; CADHERIN_2; 11.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..3343
FT /note="Cadherin-3"
FT /id="PRO_0000004020"
FT TOPO_DOM 27..3228
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3229..3250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3251..3343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..117
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 118..229
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..330
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 632..738
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1279..1368
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1545..1648
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1676..1756
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1757..1857
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1954..2045
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2046..2145
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2146..2245
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3040..3205
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 3257..3277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 966
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 970
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 985
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1895
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 2053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2621
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2665
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2712
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2798
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2809
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2927
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3045
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3172..3205
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
SQ SEQUENCE 3343 AA; 375752 MW; 063E6F17FCC15D18 CRC64;
MTIRIFFSIF LLNHLIFFHL FNFTHQFSEE TIKFSVSEDA KLNTIIGHLE AEIGYTYRLS
RGNSKIKFDE QTLELSVSSP LDRESENAID MLIITSPPSI IHILIDVLDV NDNSPIFPID
VQRVEIPETA PIGWRVQISG ATDPDEGKNG TIGKYELVDS LATVDTMSPF GIVQSDGFLF
LEVTGKLDRE TRDLYSMRLT AIDQGVPELS SSCHLNILIL DINDNPPNFG IRSLTLNWNG
LPNTKLFSLN ATDLDSNENS LLTYRILPSG PTSEMFSISD ENILVTQNNT ECLQRCEFVV
EARDSGVPPL STTLNIVVNM EYGNEHEPNI NIRFYPSDYP FIIVQPEDVN GKTLAILSIT
DSDGPLGANS TIWIENGNEQ SIFSLISRQS INILTVKHVE NANQEQYILE FRANDGQSPA
DRITRKELKI FFKKYVKSTQ IHVERESHVT VEKDTVPGSF VAHVETNCTD MCSFELANSD
VFKIDPFNGI IVTSSILPEG VTSYHLPIRI HLPPPSTQLV EADVFVKVIQ ESVPKNLIRS
SESPIHLKRA YTFTTWQDVS LGTVIGRLPK AQIYSTIDTV SELGVFPDGS VFVGKTITSD
FVTLPVTLVN RNTTQTSIIT LIVKPLNQHS PICQITEIHV LENAPIGTIF GRIQARDEDS
GLSGVVSYKI LTKSDDYDGI FHLDSTSGSL RSLKAFDAEK KRSYTFEYEA KDLGTPSKTT
NCPATIFIED VNDNVPKFGS RYYTATISGK SNETVAIVQA NDNDVDVKNQ KLQYHLLNYH
DFFQLDKETG KVTTIQDVPM TWQRLNISIS AVNMDSERFL QSKTFLLVTV TSSSKLAVQL
NSGNLIRIFK NDKIGEKVGH LDIASSETVY WSTLDPRLHV DSSGNIILIR RNAKQASTGF
DIILTSENGE KTEKVNFEVE FVDSERSEDV EKVMDIVLNE NTTEVSNLMN DWKNWKISRV
ILENANNSGN NTFFLEHKKL WRTKNATVSN AYIILESEDQ EGSPKSFKLL HVTTSPSPSS
ESSCISPAHL ISPPSTVPLP SNCSNVKLQN LKTSLQIHEN NLLIPTQSEL INHVDLVSTQ
NSDMKPFMMT LIKDYLSEDV RFSTNNVLML LSSIHPIGTS FGRVTAESGY RIRYYIVGTD
KISIDADTGE LILKERFYRN LNDILIVAVI PKGIAKAKIT IEVIEDRLIL PQSNFFIPSP
PSFNSKSKIG KIPIDRDDVT IDVIDEHFYV RNFEIFVKRH FIPNSNFYDL KGTVKKGKLS
APISVTLFFG EKMKSREIRE NELMFEIEEN SPIGTVVGVV PNSDTTKYRL VDPTCGLLID
QEGIIRTTTV FDRENTSLLK TKMIEPSENR IWNLLIFIAD VNDNKPKILN APGRIIVYDD
LNYKLEWEDL DAIASDVSFS IVDGDVFGNL EIEDSGVISL NSIPNESFNA TIRIYDNRPP
FKVHFDDVTI EFQVTQKLRA VTCEDAEFWM FFGNEDVGML IASEIVTWRI VPQIGSDSFK
IDPITGIIQS TPNTKPTSDI AKLKIQAISY DGERVGFCDV KIHIDKAAFV ENVVLSNGTF
EFNISETADR FTEVGKIVIL GAGLEGSVFR IQDNDYNFTI SPFDGTIFTN SPLDFENIKT
YRFNITAGKS TSQVIIHVTD ENDEAPRFIT GDVVNLKVLE ELDTVSYPLI IGSSIAEDLD
EGQNGLVTYS ILSGNTSLFA VNSTTGDILS LIPLDREESS LHELLIEAKD AGIPSLSATS
KILIHVGDIN DNTPEFELSS YFIKISENSK IGSKIIRILA TDKDKDAELQ YSLESNDEIT
IPFRINVATG WITVAGKVNR EENEEFRFFV KVTDGEKSSK VIVEIHVEDF NDNHPMINDR
NSDIFVPDPT RSVEIIHVIN VHDLDKSDHL KFSLNNSNLN LSENGEITLK SPLQTAVPVR
VTVSDDAGHV AFMEYLFHPH SRKHFPVFVE KLDTVSVREH DEQELAVFKA NGDSIRYSIV
SRCSDHLEME KSTGILKTKS SLDAEEYSEC LVFIIATTYF DNKPLSTITK ATIKIVDIND
NSPRFDQQLY RFNVTENSGP KLIGHVIARD IDRSSRVFYE IVGGDANHEF MVTESGQIES
VRDLDRETKS EYHLIVEAID DGKPRRRGNT TVIVTVLDED DNAPRFSRIF HVEVPEDVRI
GEPVIQLSAS DADEHSNHRF ELDGGGEGIP FRVDENTGMV FVNDSLDFEK KQSYRIKVKL
TDGAWLIETS LFVNVKDVND NAPIFEKPEY LFISEENSAE IGQFHASDMD SENNGKIRYS
VTSPYFKIEP STGVLSRFRQ QLPQPLMSLK VTATDHGVPR LQKTVLAHLV DKSSFGKIKQ
RRIRETTKVG DVIGKKIDSG ATIFPLDVAT VTRDGDVVLK KNATQFWILE NDTIYEFVKT
DAMESTKNEN ITLNITSDIS MNSDNFKVLR NGSLIVFGFS GNQAHLKIQC DDGFWPKQDR
KIINLVVNNL DADRNSFPLA RQPTIRKSMS LPKTMILNIP FDSPTGTIIW KNLENAVQYM
ENQKNVNFSN GSKNLILKTP LEETMQIDIF GQNFERSALT ITPNRSLMAC PVFQKNFYFF
ESVANLDSKH PTEIHNFGWS SDEIKGCQID IFDKTHLFYQ NGSSLIFLKP LLPGTYQFSL
QIKSQSDSKI RSACHVVVTV IPPTNLTTWN IPSVIFATRN YNIPNLFHLP SGYSLSSDQR
TFSLIGSGTG KNISKLSSGV YQVNVVGKDE KKEIVRILLD DVADDVTSKD IEYHVVSSTL
SNLKIPTPID VECFPRTEEN LYEITKDCRL LFNSDVINTT IPVVTSPANS TWNLRIINES
PETVKSLENN AVSLEIITQK SSIPRLITDL RVTYSDMKIY CLGTWQTSED IKYHITFVIV
DRNGVVIEES EARQTLTSFL KKHRPGYLDF VDFDKDPCDG VTCIQKNSTC QPTLVGDSAS
RLVSRSSSVI FDLPLKKLTA RCFCSSGIDC YDDTTNETIQ KTQKINVITT CDDIDCGPRG
KCFMEESSQP ICRCGQGFES MYSCERADDV FSMSTGGSVE ISVRNGTSHL LKCSENCDGR
DIQKIEFDFR TVQLEKSELF RVDFGKQVAL IELIGGSLTF SITDAYARPI ETRIEKRVND
GRWHRLLFQM SEDGRRISIQ VNGRGKEVKS RVPLQMLFTA KKIQLMTPAA FCFRRLLAQN
QFVHPILNRN KFFEISSTGT SRNECQFDSI QSGSGGFRLF SNFSNTTTLI LLITLALISL
IGFSVCLLAI RRRWRQKSPG DQKQTERSNG WTGHVMPRRR GHINRSMVKS PDDDTYDVAT
VYGMKSTSTD DITHIYTSSS SRRYQPPTAP SYRRDGHINM AYL
//
