FAT3_RAT
ID FAT3_RAT Reviewed; 4555 AA.
AC Q8R508;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 23-FEB-2022, entry version 113.
DE RecName: Full=Protocadherin Fat 3;
DE AltName: Full=FAT tumor suppressor homolog 3;
DE Flags: Precursor;
GN Name=Fat3;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=11811999; DOI=10.1006/bbrc.2002.6338;
RA Mitsui K., Nakajima D., Ohara O., Nakayama M.;
RT "Mammalian fat3: a large protein that contains multiple cadherin and EGF-
RT like motifs.";
RL Biochem. Biophys. Res. Commun. 290:1260-1266(2002).
CC -!- FUNCTION: May play a role in the interactions between neurites derived
CC from specific subsets of neurons during development. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Restricted to the nervous system. Abundantly
CC expressed in the fetal brain. {ECO:0000269|PubMed:11811999}.
CC -!- DEVELOPMENTAL STAGE: Present in brain and peaks at E15 during embryonic
CC development. Also present in the spinal cord (at protein level).
CC {ECO:0000269|PubMed:11811999}.
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DR EMBL; AB076401; BAB86869.1; -; mRNA.
DR RefSeq; NP_612553.1; NM_138544.1.
DR SMR; Q8R508; -.
DR BioGRID; 251318; 1.
DR STRING; 10116.ENSRNOP00000015976; -.
DR GlyGen; Q8R508; 26 sites.
DR iPTMnet; Q8R508; -.
DR PhosphoSitePlus; Q8R508; -.
DR PaxDb; Q8R508; -.
DR PRIDE; Q8R508; -.
DR GeneID; 191571; -.
DR KEGG; rno:191571; -.
DR UCSC; RGD:620657; rat.
DR CTD; 120114; -.
DR RGD; 620657; Fat3.
DR eggNOG; KOG1219; Eukaryota.
DR InParanoid; Q8R508; -.
DR OrthoDB; 12779at2759; -.
DR PhylomeDB; Q8R508; -.
DR PRO; PR:Q8R508; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:2000171; P:negative regulation of dendrite development; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0010842; P:retina layer formation; ISO:RGD.
DR CDD; cd00110; LamG; 1.
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; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 27.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 32.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 34.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00232; CADHERIN_1; 19.
DR PROSITE; PS50268; CADHERIN_2; 32.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Developmental protein; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Methylation; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..4555
FT /note="Protocadherin Fat 3"
FT /id="PRO_0000324636"
FT TOPO_DOM 32..4153
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4154..4174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4175..4555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..157
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 158..265
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 263..374
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 376..471
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 472..577
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 578..680
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 726..830
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 831..935
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 936..1042
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1043..1147
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1148..1253
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1254..1358
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1362..1459
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1460..1565
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1566..1768
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1769..1882
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1883..1985
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1982..2083
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2084..2185
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2186..2286
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2287..2393
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2394..2495
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2496..2599
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2600..2707
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2708..2813
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2814..2923
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2924..3028
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3029..3130
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3131..3235
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3236..3340
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3341..3445
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3446..3550
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3551..3652
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3794..3832
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3834..4017
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 4020..4057
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4059..4095
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 4097..4133
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4326..4347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4395..4424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4452..4472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4508
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BNA6"
FT MOD_RES 4518
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8BNA6"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 879
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1006
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1367
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 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1993
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 2208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3926
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3798..3809
FT /evidence="ECO:0000250"
FT DISULFID 3803..3821
FT /evidence="ECO:0000250"
FT DISULFID 3823..3831
FT /evidence="ECO:0000250"
FT DISULFID 3984..4017
FT /evidence="ECO:0000250"
FT DISULFID 4024..4035
FT /evidence="ECO:0000250"
FT DISULFID 4029..4045
FT /evidence="ECO:0000250"
FT DISULFID 4047..4056
FT /evidence="ECO:0000250"
FT DISULFID 4063..4074
FT /evidence="ECO:0000250"
FT DISULFID 4068..4083
FT /evidence="ECO:0000250"
FT DISULFID 4085..4094
FT /evidence="ECO:0000250"
FT DISULFID 4101..4112
FT /evidence="ECO:0000250"
FT DISULFID 4106..4121
FT /evidence="ECO:0000250"
FT DISULFID 4123..4132
FT /evidence="ECO:0000250"
SQ SEQUENCE 4555 AA; 502088 MW; B47CBC10638EA73B CRC64;
MGVTMRHCID TRPPSCLIFL LLKLCATVSQ GLPGTGPLGF HFTHALYNAT VYENSAARTY
VNSQSRMGIT LIDLSWDIKY RIVSGDEEGF FKAEEVIIAD FCFLRIRTKG GNSAILNREI
QDNYLLIIKG SVRGEDLEAW TKVNIQVLDM NDLRPLFSPT TYSVTIAEST PLRTSVAQVT
ATDADIGSNG EFYYYFKNKV DLFSVHPTSG VISLSGRLNY DEKNRYDLEI LAVDRGMKLY
GNNGVSSTAK LYVHIERINE HAPIIHVVTH TPFSLDKEPT YAVVTVDDLD EGANGEIESV
SIVDGDPLEQ FFLAKEGKWM NEYKVKERRQ VDWESFSYGY NLTIQAKDKG SPQKFSELKT
VHIANPRRDS TPIKFEKDVY DISISEFSPP GVMVAIVKVN PEPLDVEYKL LPGKDAEYFK
INPRSGLIVT AQPLNTVKKE VYKLEVSDKE GDAKAQVTIG IEDANDHTPE FQETLYETFV
NESVPVGTNV LTVSASDKDK GENGYITYSI ASLNLLPFAI NQFTGVISTT EELDFESSPE
TYRFIVRASD WGSPYRHESE VNVTIRVGNV NDNSPLFEKV ACQGVISYDF PVGGHITAIS
AIDIDELELV KYKIISGNEL GFFYLNPDSG VLQLKKSLMN SGIKNGNFAL RITATDGENF
ADPMAINISV LHGKVSSKSF SCRETRVAQK LAEKLLIKAK ANGKLNQEDG FLDFYSINRQ
GPHFDKSFPS DVAVKENMPV GTNILKIKAY DADSGFNGKV LFTISDGNTD SCFNIDMETG
QLKVLMPMDR EHTDLYVLNI TIYDLGKPQK SSWRLLTVNV EDANDNSPVF LQDSYSVSIL
ESSSIGTEII QVEARDKDLG SNGEVTYSVL TDTHQFVINS STGIVYIADQ LDRESKANYS
LKIEARDKAE SGQQLFSVVT LKIFLDDVND CSPAFIPSSY SVKVLEDLPV GTVIAWLETQ
DPDLGLGGQV RYSLVNDYNG RFEIDKASGA IRLSKELDYE KQQFYNLTVR AKDKGRPVSL
SSISFVEVEV VDVNENLHTP YFPDFAVVGS VKENSRIGTS VLQVTAHDED SGRDGEIQYS
IRDGSGLGRF NIDDESGVIT AADILDRETT ASYWLTVYAT DRGVVPLYST IEVYIEVEDV
NDNAPLTSEP IYYPVVMENS PKDVSVIQIQ AEDPDSGSNE KLTYRITSGN PQNFFAINIK
TGLITTTSRK LDREQQAEHF LEVTVTDGGS SPKQSTIWVV VQVLDENDNK PQFPEKVYQI
KLPERDRKKR GEPIYRAFAF DRDEGPNAEI SYSIVDGNDD GKFFIDPKTG MVSSRKQFTA
GSYDILTIKA VDNGRPQKSS TARLHIEWIK KPPPSPIPLT FDEPFYNFTI MESDKVTEIV
GVVSVQPANT PLWFDIIGGN FDSSFDAEKG VGTIVIAKPL DAEQRSVYNM SVEVTDGTNV
AVTQVFITVL DNNDNGPEFS QPHYDVTISE DVPPDTEILQ IEATDRDEKH KLSYTIHSSI
DAISMRKFRI DPSTGVLYTA ERLDHEAQDK HILNIMVRDQ EFPYRRNLAR VIVNVEDAND
HSPYFTNPLY EASVFESAAL GSVVLQVTAL DKDKGENAEL IYSIEAGNTG NTFKIEPVLG
IITISKEPDM TAMGQFVLSV KVTDQGSPPM SATAIVRISI SMSDNSHPKF THKDYQAEVN
ENVDIGTSVI LISAISQSTL IYEVKDGNIN GVFTINPYSG VITTRRALDY EHTSSYQLII
QATNMAGMAS NATVSVQVVD ENDNPPVFLF SQYSGSLSEA APINSLVRSL DNSPLVIRAT
DADSNQNALL VYQIVESTAK KFFTVDSSTG AIRTIANLDH EVIAHFHFHV HVRDSGNPQL
TAESPVEVNI EVTDVNDNPP VFTQAVFETV LLLPTYVGVE VLKVSATDPD SEVPPELTYS
LMEGSVDHFL MDPNTGVLTI KNNNLSKDHY MLIVRVSDGK FYSTAMVTIM VKEAMDSGLH
FTQSFYSTSI SENSTNITKV AIVNAVGNRL NEPLKYSILN PGNKFKIKST SGVIQTTGVP
FDREEQELYE LVVEASRELD HLRVARVVVR VNIEDVNDNS PVFVGLPYYA AVQVDAEPGT
LIYRVTAIDK DKGANGEVTY VLQDDYGHFE INPNSGNVIL KEAFNSDLSN IDYGVTILAK
DGGTPSLSTF VELPITIVNK AMPVFDKPFY TASINEDISI NTPILSINAT SPEGQGIIYL
IIDGDPFQQF NIDFDTGVLK VISPLDYEVM SVYKLTVRAS DALTGARAEV TVDLLVDDVN
DNPPVFDQPT YNTTLSESSL IGTPVLQLVS TDADSGNNNL VHYQIVQDTY NSTDYFHIDS
SSGLILTARM LDHELVQHCT LKVTATDNGF PSLSSEVLVQ IYISDVNDNP PVFNQLIYES
YVSELAPRGH FVTCVQASDA DSSDFDRLEY SILSGNDRTS FLMDSKSGVL TLSSHRKQRM
EPLYSLNVSV SDGLFTSTAQ VHIRVLGANL YSPAFSQSTY VAEVRENAAS GTKVIHVRAT
DGDPGTYGQV SYSIINDFAK DRFLIDSNGQ IITTERLDRE NPLEGDISIY LRALDGGGRT
TFCTVRVIVV DENDNAPQFM TLEYRASVRA DVGRGHLVTQ VQALDPDDGA NSRITYSLYS
EASVSVADLL EIDPDNGWMV TKGNFNQLRN TVLSFFVKAV DGGIPVRHSL IPVYIHVLPP
ETFLPSFTQS QYSFTIAEDT SIGSTIDTLR ILPNQSVRFS TVNGERPENN KENVFIIEQE
TGAIKLDKRL DHEVSPAFHF KVAATIPLDK VDIVFTVDVD VKVLDLNDNK PVFETSSYET
IIMEGMPVGT KLAQVRAIDT DWGANGQVTY SLHSDSHLEK VMEAFNIDSN TGWISTLKDL
DHETDPTFSF FVVASDLGEA FSLSSMALVS VKVTDINDNA PVFAHEVYRG NVKESDPPGE
VVAVLSTLDK DTSNINRQVS YHITGGNPRG RFALGMVQSE WKVYVKRPLD REEQDIYFLN
ITASDGLFVT QAMVEVTVSD VNDNSPVCDQ VAYSASLPED IPSNKIILKV SAKDADIGSN
GDIRYSLYGS GNSDFFLDPE SGELKTLALL DRERVPVYNL IARATDGGGR FCSSTVLLLL
EDVNDNPPVF SSNHYTACVY ENTATKALLT RVQAVDPDVG INRKVVYSLE DSASGVFSID
SSSGVIVLEQ PLDREQQSSY NISVRATDQS PGQSLSSLTS VTITVLDIND NPPVFERRDY
LVTVPEDTSL GTQVLSVFAT SKDIGTNAEI TYLIRSGNEQ GKFRINPKTG GISVLEALDY
EMCKRFYLVV EAKDGGTPAL STAATVSIDL TDVNDNPPRF SQDVYSAVIS EDALEGDSVI
LLIAEDVDSK PNGQIRFSIV GGDRDNEFAV DPILGLVKVK KKLDRERVSG YSLLIQAVDS
GIPAMSSTTT VNIDISDVND NSPVFTPANY TAVIQENKPV GTSILQLVVT DRDSFHNGPP
FSFSILSGNE DEEFMLDSHG ILRSAVVFRH MESPEYLLCI QAKDSGKPQQ VSHTYIRVRV
IEESTHKPTA IPLEIFIVTM EDDFPGGVIG KIHATDQDMY DVLTFALKSE QKSLFKVNSH
DGKIIALGGL DSGKYVLNVS VSDGRFQVPI DVVVHVEQLV HEMLQNTVTI RFENVSPEDF
VGLHMHGFRR ILRNAVLTQK QDSLRIISIQ PVVGTNQLDM LFAVEMHSSE FYKPAYLIQK
LSNARRHLEN VMHIAAILEK NCSGLDCQEQ HCEQGLSLDS HALMTYSTAR ISFVCPRFYR
NVRCTCNGGV CPGSNDPCVE KPCPEDMQCV GYEASRRPFL CQCPPGKLGE CSGHTSLSFA
GNSYIKYRLS ENSREEDFKL ALRLRTLQSN GIIMYTRANP CMILKIVEGK LWFQLDCGSG
PGILGISSRA VNDGSWHSVF LELNRNFTSL SLDDSYVERR RAPLYFQTLS TDSAIFFGAL
VQADNIRSLT DTRVTQVLGG FQGCLDSVVL NHNELPLQNK RSSFAEVVGL TELKLGCVLY
PDACQRSPCL HGGSCSGLPS GGYQCSCLSQ FTGTNCESEI TACFPNPCRN GGSCDPIGNT
FICSCKAGLT GVTCEDDVDE CEREECENGG SCVNLFGSFF CNCTPGYVGQ YCGLRPVVVP
NIQAGHSYVG KEELIGIAVV LFVIFTLIVL FIVFRKKVFR KNYSRNNITL VQDPATAALL
HKSNGIPFRS LRAGDGRNVY QEVGPPQVPV RPMAYTPCFQ SDSRSNLDKG LDALGGEPQE
LSTFHPESPR ILTARRGVVV CSVAPNLPAV SPCRSDCDSI RKNGWDTGSE NKGAEDTGEV
TCFANSNKGS NSEVQSLNSF QSDSGDDNAY HWDTSDWMPG ARLSDIEEMP NYESQDGGAV
HQGSTRELES DYYLGGYDID SEYPPPHEEE FLSQDQLPPP LPEDFPEQYE ALPPSQPTSL
TGTMSPDCRR RPRFHPSQYL PPHPLPGETD LGGPPSSCDF STFAVSMNQG TEVMAPTDSV
SLSLHNSRGT SSSDMSARCG FDDSEVAMSD YESAGELSLT NLHIPFVETQ HQTQV
