FAT2_RAT
ID FAT2_RAT Reviewed; 4351 AA.
AC O88277;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 23-FEB-2022, entry version 139.
DE RecName: Full=Protocadherin Fat 2;
DE AltName: Full=Multiple epidermal growth factor-like domains protein 1;
DE Short=Multiple EGF-like domains protein 1;
DE Flags: Precursor;
GN Name=Fat2; Synonyms=Fath2, Megf1;
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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9693030; DOI=10.1006/geno.1998.5341;
RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
RT "Identification of high-molecular-weight proteins with multiple EGF-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [2]
RP PROTEIN SEQUENCE OF 673-681; 2566-2572; 2968-2976 AND 3081-3088, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12213440; DOI=10.1006/mcne.2002.1146;
RA Nakayama M., Nakajima D., Yoshimura R., Endo Y., Ohara O.;
RT "MEGF1/fat2 proteins containing extraordinarily large extracellular domains
RT are localized to thin parallel fibers of cerebellar granule cells.";
RL Mol. Cell. Neurosci. 20:563-578(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-3588 AND ARG-3651.
RX PubMed=29053796; DOI=10.1093/brain/awx251;
RA Nibbeling E.A.R., Duarri A., Verschuuren-Bemelmans C.C., Fokkens M.R.,
RA Karjalainen J.M., Smeets C.J.L.M., de Boer-Bergsma J.J., van der Vries G.,
RA Dooijes D., Bampi G.B., van Diemen C., Brunt E., Ippel E., Kremer B.,
RA Vlak M., Adir N., Wijmenga C., van de Warrenburg B.P.C., Franke L.,
RA Sinke R.J., Verbeek D.S.;
RT "Exome sequencing and network analysis identifies shared mechanisms
RT underlying spinocerebellar ataxia.";
RL Brain 140:2860-2878(2017).
CC -!- FUNCTION: Involved in the regulation of cell migration
CC (PubMed:29053796). May be involved in mediating the organization of the
CC parallel fibers of granule cells during cerebellar development
CC (PubMed:12213440). {ECO:0000269|PubMed:29053796,
CC ECO:0000303|PubMed:12213440}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12213440}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Cell junction {ECO:0000250|UniProtKB:Q9NYQ8}.
CC Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:12213440,
CC ECO:0000269|PubMed:29053796}. Note=Localized at adhesion zippers (early
CC state of adherens junctions) of keratinocytes.
CC {ECO:0000250|UniProtKB:Q9NYQ8}.
CC -!- TISSUE SPECIFICITY: Cerebellum-specific expression. Expressed in thin
CC parallel fibers of cerebellar granule cells.
CC {ECO:0000269|PubMed:12213440, ECO:0000269|PubMed:9693030}.
CC -!- DEVELOPMENTAL STAGE: In the developing cerebellum, expressed in granule
CC cells in the inner external germinal layer and in migrating granule
CC cells whereas proliferating cells in the outer extessornal germinal
CC layer did not shown expression. Expression levels in the internal
CC granule cell layer peak during the third postnatal week and remain
CC considerably high in the adult cerebellum.
CC {ECO:0000269|PubMed:12213440}.
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DR EMBL; AB011527; BAA32458.1; -; mRNA.
DR PIR; T00252; T00252.
DR RefSeq; NP_075243.1; NM_022954.1.
DR SMR; O88277; -.
DR BioGRID; 249241; 1.
DR STRING; 10116.ENSRNOP00000055459; -.
DR GlyGen; O88277; 37 sites.
DR iPTMnet; O88277; -.
DR PhosphoSitePlus; O88277; -.
DR PaxDb; O88277; -.
DR PRIDE; O88277; -.
DR GeneID; 65048; -.
DR KEGG; rno:65048; -.
DR UCSC; RGD:620656; rat.
DR CTD; 2196; -.
DR RGD; 620656; Fat2.
DR eggNOG; KOG1219; Eukaryota.
DR InParanoid; O88277; -.
DR OrthoDB; 12779at2759; -.
DR PhylomeDB; O88277; -.
DR PRO; PR:O88277; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:UniProtKB.
DR GO; GO:0010631; P:epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
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; IPR001791; Laminin_G.
DR Pfam; PF00028; Cadherin; 27.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 33.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 33.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00232; CADHERIN_1; 14.
DR PROSITE; PS50268; CADHERIN_2; 33.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..4351
FT /note="Protocadherin Fat 2"
FT /id="PRO_0000004019"
FT TOPO_DOM 19..4050
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4051..4071
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4072..4351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..148
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 149..256
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 363..458
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 459..564
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 565..669
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 716..820
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 821..925
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 926..1032
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1033..1142
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1138..1242
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1243..1346
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1350..1448
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1449..1555
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1556..1660
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1661..1758
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1759..1872
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1873..1968
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1969..2070
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2071..2171
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2172..2272
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2273..2379
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2380..2481
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2482..2585
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2586..2692
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2693..2799
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2800..2908
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2909..3013
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3014..3115
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3116..3220
FT /note="Cadherin 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3221..3323
FT /note="Cadherin 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3324..3428
FT /note="Cadherin 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3429..3533
FT /note="Cadherin 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3534..3631
FT /note="Cadherin 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3775..3946
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3949..3986
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3988..4024
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 4316..4340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 789
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 996
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1998
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3603
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3770
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3842
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3906
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3991
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 3914..3946
FT /evidence="ECO:0000250"
FT DISULFID 3953..3964
FT /evidence="ECO:0000250"
FT DISULFID 3958..3974
FT /evidence="ECO:0000250"
FT DISULFID 3976..3985
FT /evidence="ECO:0000250"
FT DISULFID 3992..4003
FT /evidence="ECO:0000250"
FT DISULFID 3997..4012
FT /evidence="ECO:0000250"
FT DISULFID 4014..4023
FT /evidence="ECO:0000250"
FT MUTAGEN 3588
FT /note="K->N: Increased localization to Golgi apparatus. Has
FT no effect on cell migration."
FT /evidence="ECO:0000269|PubMed:29053796"
FT MUTAGEN 3651
FT /note="R->Q: Increased localization to Golgi apparatus. Has
FT no effect on cell migration."
FT /evidence="ECO:0000269|PubMed:29053796"
SQ SEQUENCE 4351 AA; 480654 MW; C564E7F98EBB3888 CRC64;
MTLVLLGLAI LLLHRAACEK SLEETIPPLS WRFTHSLYNA TIYENSAPKT YVESPVKMGM
YLAEPHWVVK YRIISGDAAG VFKTEEHVVG NFCFLRIRTK SSNTALLNRE VRDSYTLIVQ
ASDKSLEFEA LTQVVVHILD QNDLKPLFSP PSYRVTISED RPLKSPICKV TATDADLGQN
AEFYYAFNAR SEVFAIHPTS GVVTVAGKLN VTRRGKYELQ VLAVDRMRKI SEGNGFGNLA
SLVIRVEPVH RKPPAINLVV LNPPEGDEGD IYAIVTVDTN GSGAEVDSLE VVGGDPGKYF
KVLRSYAQGN EFNLVAVRDI NWAEHPHGFN ISLQTHSWSR FPPHSIIRAF HLPSWKLANL
RFEKAVYRVK LSEFSPPGSR VALVKVTTAL PNLRYSLKPS SRNTAFKLNA RTGLITTTKL
VDFHEQNQYQ LHVKTSLGQA TTTVIIDIVD CNNHAPVFNR SSYEGTLDEN IPPGTSVLTV
TATDQDHGDN GHITYSIAGP KAVPFSIDPL LGVISTTKPM DYELMKRIYT FRVRASDWGS
PFRQEKEVSV SLRLKNLNDN QPMFEEVNCT VSLRQDVPVG KSIMAVSAID MDELQNLKYE
IVSGNEQDYF HLNHFSGVIS LKRSFMNLTA VRPTIYSLKI TASDGKNYAS PTTLKVTVVK
DPHSEVPVQC DKTGVLTHIT KTILQSAGLQ SQELGEEEFT SLSNYQINHH SPQFEDHFPQ
SIDILEQVPI NTPLARLAAT DPDTGFHGKL VYVISDGNEE GCFDIELETG LLMVAAALDY
ETTSFYVLNV TVYDLGTPPK SSWKLLTVTV KDWNDNPPRF PPGGYQLTIS EDTEVGTTIA
ELKTEDADSE DNRRVRYTLL TPTEKFSLHP FTGELVVTGH LDRESESQYI LKAEARDQPT
KGHQLFSVTD LIVTLEDIND NPPQCITEHR RLKVPEDMPL GTVLTFLDAS DPDLGPAGEV
KYILVEDAHG TFQVHPMTGA LSLEKELDFE RRAGYNLSFW ASDSGKPLSR RTLCHVEVLV
MDVNENLHSP HFSSFVYQGQ VQENSPAGTP VMVVTAQDDD SGLDGELQYF LRAGTGLETF
SINQDTGMLE TLAPLDREFT PYYWLTVLAV DRGSVPLSAV TEVYIEVTDI NDNIPSMSRP
VFYPSVLEDA PLGTSVLQLE AWDPDSSSQG KLTFNLTSGN HLGHFIVHPF TGLLTTAKQL
DRENKDEYVL EVTVQDNGDP SLRSTSRVVV CILDVNDNPP MFSHKLFNVR LSERLSPLSP
EPVYRLVASD PDEGLNGSVT YSIEESDEES FRIDPVTGVV SSSSTFAAGE YNILTIKATD
SGQPALSTSV RLHIEWIPQP RPSSIPLSFD ESYYSFTVME TDPVNHMVGV ISVEGRPGLF
WFHISDGDKD MDFDIEKTTG SIVIARPLDT RRKSSYNLTV EVTDGFHTIA TQVHIFMIAN
INHHRPQFLQ DHYEIRVPQD TLPGVELLRV QATDQDHGKG LIYTILSSQD PGSANLFQLD
PSSGVLVTVG TLELHSGPSQ HILTVMVRDQ EMPIKRNFVW VTIHVEDGNL HSPHFTQLRY
EANVPDTTAP GTELLQVRAV DADRGANAEI HYSFLKGNSD GFFNIDSLLG IITVAQRLYH
VHLTRHALTV KAEDQGSPRR HDLALVVIHV HPSDSSAPVF SKDEYFIEIP ESVPIGSPIL
LLSAGSSSEV TYELREGNKD SVFSMNSYSG LISTQKRLDH EKVPSYRLRI RGSNMAGVFT
EVVALVYIID ENDNPPAFGK PTFLGHISEA APLHSLILGE DNSPLVVRAS DSDREANSLL
VYKILEPEAL KFFKIDPSMG TLTTTSELDF EDTPLFQFNI YVHDQGTPIL FAPRSAKVII
HVRDVNDSPP RFSEQIYEVA VVEPIHPGMG LLTVQAEDND SRVTYSIKTS NADEAVTIHP
TTGQISVVNP ATLRLFQKFS IRASDGLYHD TAVVKISLTQ VLDKSLQFDQ DVYRARVTEN
TPHRKALVIL GVHGNHLNDT LSYFLLNGTD LFHMIESAGV LQTRGGTFDR EQQDTHEVAV
EVRDNRVPQR VAQALVRVSV EDVNDNIPEF QHLPYYTVIQ DGTEPGDVLF QVSATDKDLG
ANGSVTYGFA EDYAYFRIDP YVGDISLKKP FDYQALNKYH LRVIARDSGI PPLQTEVEVH
VTVRNKSNPL FQSPYYKVKV PENITLYTPI LHTQARSPEG LRLIYNIVEE EPLMLFTTDF
KTGVLTVTGP LDYESKNKHV FTVRATDTAL GSFSEATVEV LVEDINDNPP TFSQLVYTTS
VSEGSPAQTP VIQLLASDQD SGQNQDVSYQ IVEDGSDVSK FFRINGSTGE IFTIQELDYE
THQHFRVKVR AMDKGDPPLT GETLVVVNVS DINDNPPKFR EPQYEANVSE LATCGHLVLK
VQALDPDIGD TSRLEYLILS GNQDRHFSIN STSGIISMFN LCKKQLDSSY NLRVGASDGV
FRATVPVYIN TTNANKYSPE FQQNVYEAEL AENAKVGTKV IELLAIDKDS GPYGTVDYTI
INKLAGERFF INPRGQITTL QKLDRENSTE RVIAIKVMAR DGGGKVAFCT VKIILTDEND
NAPQFKASGY TVSIPSNVSR DSPIIQVLAY DADEGRNADV TYSVDSTEDL AEEIIEVNPT
TGVVKVKESL VGLENRAVDF NIKAQDGGPP HWDSLVPVRL QVVPNEIPLP KFSEPLYTFS
APEDLPEGSE IGSVKAVAAQ DPIIYSLVQG TTPESNSDDV FSLDQDTGVL KVRKAMDHES
TKWYQIDLMA HCPHEDTDLV SLVSVSIQVE DVNDNRPVFE ADPYKAFLTE NMPGGTTVIQ
VTANDQDTGS DGQVSYRLSV EPGSNIHELF AVDSESGWIT TLQELDCETQ QTYRFYVVAF
DHGQTIQLSS QALVEVSITD ENDNPPRFAS EDYRGSVVEN NEPGELVATL KTLDADVSDQ
NRQVTCYITE GDPLGQFSIS QVGDEWRISS RKTLDREHIA KYLLRVTASD GKFQASVPVE
VFVVDINDNS PQCSQLLYTG KVREDVTPGH FILKVSAIDV DMDTNAQITY SLHGPGAQEF
KLDPHTGELT TLTVLDRERK DVYNLVAKAT DGGGQSCQAE VTLHIEDVND NAPRFFPSHC
DVAVFDNTTV KTPVAVVFAR DPDQGANAQV VYSLTDSADG QFSIDATSGV IRLEKPLQVR
ASSAVELTVR ASDLGTPIPL STLGTVTVSV VGLEDYLPIF LNAEHSTQVP EDAPIDMEVL
HLATLTRPGS EKTGYHITGG NEQGKFRLDA HTGILYVNGS LDFETNPKYF LSIECSRKSS
SSLSDVTTIV INVTDVNEHH PRFTHDLYTV RVLENAVVGD VILTVSASDD DGPVNSAITY
SLVGGNQLGH FTINPKKGKL QVAKALDWEQ TPSYSLRLRA TDSGQPPLHE DTEVAVEVVD
VNDNPPRFFQ LNYSTSVQEN SPIGIKVLQL ILDDPDSPQN GPPYFFRITE GNTGSVFRVT
PDGWLVTAAS LSKKAREWYQ LHIEVSDSGL PPLSSSTLVR VQVTEQSRYP PSTLPLEISI
TKGEEEFQGG MIGKIHATDR DPQDTLTYSL EQEGGLDRYF TVGASDGKII ASQGLPHGRY
SFNVTVSDGT FTTTTGVHVH VWHMEPEVPQ QAVWLGFHQL TPEELVSDHW RNLQRFLSNL
LDVKRANIHL ASLQPAEVTA GVDVLLVFER HSGTSYDLQE LASAIAHSVR EIEHSVGIRM
RSALPVVPCQ GQSCQDQTCQ ETVSLEPRVG PSYSTARLSI LTPRHHLGRN CSCNGTTLRF
SGQSYVQYRP LEAQNWQIHF YLKTLQPWAL LMFTNETASI SLKLANGFSH LEYHCPGGFY
GNLSSRYPVN DGQWHSMLLE ERDTSVHLLV DITDNASLVI PEECQGLRTE RQLLLGGLVP
SNPSSNVSLG FEGCLDAVVV NGERLELLGR EKKMEGRLET WALSQCCWPG TACSQSPCLN
GGSCSPALGS GYLCRCPPPF SGRNCELGRE NCTSAPCQEG GTCVSSPEGT SCNCPHPYTG
DRCEMEARGC SGGHCLITPE IKRGDWGQQE FLVITVALPL VIIATVGLLL YCRRRKSHKP
VTMEDPDLLA RSIGVDTQAS PAIELDPLNT SSCNNLNQPE PSKTSVPNEL VTFGPSSKQR
PMVCSVPPRL PPAAVSSHPG HEPIIKRTWS GEELVYPSGA AVWPPTYSRK KHWEYPHPET
MQGTLPPSPR RHVGPAVMPD PTGLYGGFPF PLELENKRAP LPPRYSNQNL EDLMPPRPPS
PREHLLAPCL NEYTAISYYH SQFRQGGGGP CLAEGGYKGV SMRLSRAGPS YADCEVNGGP
ATGRSQPRAP PNYEGSDMVE SDYGSCEEVM F
