ID LTBP2_RAT Reviewed; 1764 AA.
AC O35806;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Latent-transforming growth factor beta-binding protein 2;
DE Short=LTBP-2;
DE Flags: Precursor;
GN Name=Ltbp2;
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 TISSUE=Lung;
RX PubMed=10028916;
RX DOI=10.1002/(sici)1098-1136(19990215)25:4<332::aid-glia3>3.0.co;2-1;
RA Krohn K.;
RT "TGF-beta1-dependent differential expression of a rat homolog for latent
RT TGF-beta binding protein in astrocytes and C6 glioma cells.";
RL Glia 25:332-342(1999).
RN [2]
RP REVIEW.
RX PubMed=10743502; DOI=10.1016/s1359-6101(99)00010-6;
RA Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.;
RT "Latent transforming growth factor-beta binding proteins (LTBPs)
RT -- structural extracellular matrix proteins for targeting TGF-beta
RT action.";
RL Cytokine Growth Factor Rev. 10:99-117(1999).
RN [3]
RP REVIEW.
RX PubMed=11104663; DOI=10.1042/bj3520601;
RA Oklu R., Hesketh R.;
RT "The latent transforming growth factor beta binding protein (LTBP)
RT family.";
RL Biochem. J. 352:601-610(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP CLEAVAGE OF SIGNAL PEPTIDE AFTER ALA-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820;
RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.;
RT "Peptidomics for studying limited proteolysis.";
RL J. Proteome Res. 14:4921-4931(2015).
CC -!- FUNCTION: May play an integral structural role in elastic-fiber
CC architectural organization and/or assembly.
CC {ECO:0000250|UniProtKB:Q14767}.
CC -!- SUBUNIT: Forms part of the large latent transforming growth factor beta
CC precursor complex; removal is essential for activation of complex.
CC Interacts with SDC4. Interacts (via C-terminal domain) with FBN1 (via
CC N-terminal domain) in a Ca(+2)-dependent manner.
CC {ECO:0000250|UniProtKB:Q14767}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q14767}.
CC -!- TISSUE SPECIFICITY: Expressed in cortical astrocytes and glioma cells.
CC Expression is up-regulated by TGFB1. {ECO:0000269|PubMed:10028916}.
CC -!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:Q14767}.
CC -!- PTM: Contains hydroxylated asparagine residues.
CC {ECO:0000250|UniProtKB:Q14766}.
CC -!- SIMILARITY: Belongs to the LTBP family. {ECO:0000305}.
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DR EMBL; Y12760; CAA73300.1; -; mRNA.
DR RefSeq; NP_067597.2; NM_021586.2.
DR AlphaFoldDB; O35806; -.
DR STRING; 10116.ENSRNOP00000071831; -.
DR GlyCosmos; O35806; 8 sites, No reported glycans.
DR GlyGen; O35806; 8 sites.
DR iPTMnet; O35806; -.
DR PhosphoSitePlus; O35806; -.
DR PaxDb; 10116-ENSRNOP00000038437; -.
DR GeneID; 59106; -.
DR KEGG; rno:59106; -.
DR UCSC; RGD:68380; rat.
DR AGR; RGD:68380; -.
DR CTD; 4053; -.
DR RGD; 68380; Ltbp2.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; O35806; -.
DR OrthoDB; 354414at2759; -.
DR PhylomeDB; O35806; -.
DR Reactome; R-RNO-2129379; Molecules associated with elastic fibres.
DR Reactome; R-RNO-2173789; TGF-beta receptor signaling activates SMADs.
DR PRO; PR:O35806; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019838; F:growth factor binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0050436; F:microfibril binding; IBA:GO_Central.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; NAS:RGD.
DR CDD; cd00054; EGF_CA; 13.
DR Gene3D; 2.10.25.10; Laminin; 18.
DR Gene3D; 3.90.290.10; TGF-beta binding (TB) domain; 4.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR017878; TB_dom.
DR InterPro; IPR036773; TB_dom_sf.
DR PANTHER; PTHR24034; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24034:SF166; VACUOLAR-SORTING RECEPTOR 1; 1.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07645; EGF_CA; 14.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00683; TB; 4.
DR PIRSF; PIRSF036312; Fibrillin; 1.
DR SMART; SM00181; EGF; 19.
DR SMART; SM00179; EGF_CA; 17.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
DR SUPFAM; SSF57581; TB module/8-cys domain; 4.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 12.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 11.
DR PROSITE; PS50026; EGF_3; 15.
DR PROSITE; PS01187; EGF_CA; 15.
DR PROSITE; PS51364; TB; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW Growth factor binding; Heparin-binding; Hydroxylation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:26479776"
FT CHAIN 36..1764
FT /note="Latent-transforming growth factor beta-binding
FT protein 2"
FT /id="PRO_0000007645"
FT DOMAIN 181..213
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 383..415
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 538..590
FT /note="TB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 608..648
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 658..710
FT /note="TB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 834..876
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 877..919
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 920..959
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 960..999
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1000..1040
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1041..1082
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1083..1124
FT /note="EGF-like 10; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1125..1165
FT /note="EGF-like 11; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1166..1207
FT /note="EGF-like 12; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1208..1248
FT /note="EGF-like 13; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1249..1290
FT /note="EGF-like 15; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1291..1333
FT /note="EGF-like 16; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1357..1409
FT /note="TB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1431..1473
FT /note="EGF-like 17; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1474..1513
FT /note="EGF-like 18; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1530..1582
FT /note="TB 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DOMAIN 1676..1716
FT /note="EGF-like 19; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1717..1761
FT /note="EGF-like 20; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 80..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..115
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 220..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..243
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 484..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 729..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1764
FT /note="C-terminal domain"
FT /evidence="ECO:0000250|UniProtKB:Q14767"
FT COMPBIAS 110..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 331..341
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 175
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 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 602
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 185..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 189..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 203..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 387..397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 405..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 540..562
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 549..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 563..578
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 612..623
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 618..632
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 634..647
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 660..682
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 669..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 683..698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 684..710
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 838..851
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 846..860
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 862..875
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 881..892
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 886..901
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 903..918
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 924..935
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 930..944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 946..958
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 964..975
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 970..984
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 987..998
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1004..1015
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1010..1024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1026..1039
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1045..1056
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1051..1065
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1068..1081
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1087..1098
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1093..1107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1110..1123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1129..1141
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1136..1150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1152..1164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1170..1182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1176..1191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1193..1206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1212..1223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1218..1232
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1234..1247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1253..1265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1259..1274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1276..1289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1295..1307
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1302..1316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1318..1332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1359..1382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1369..1394
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1383..1397
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1435..1448
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1443..1457
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1459..1472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1478..1488
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1483..1497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1499..1512
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1532..1555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1541..1567
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1556..1570
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1557..1582
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00697"
FT DISULFID 1680..1691
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1686..1700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1702..1715
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1721..1736
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1731..1745
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1747..1760
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1764 AA; 189867 MW; 245D57F9CE3386D0 CRC64;
MRAPTTVRCS GRIQRARWRG FLPLVLALLM GTSHAQRDSV GRYEPASRDA NRLWRPVGNH
PAAAAAKVYS LFREPDAPVP GLSPSEWNQP GQGIPGRLAE AEARRPSRAQ QLRRVQSPVQ
TRRSNPRGQQ PPAARTAHSV VRLATPQRPA AARRGRLTGR NVCGGQCCPG WTTSNSTNHC
IKPVCQPPCQ NRGSCSRPQL CICRSGFRGA RCEEVIPEEE FDPQNARPVP RRSVEGAPGP
HRSSEARGSL VTRIQPLLPP LPPPPSRTLS QTRPLQQHAG LSRTVRRYPA TGTNGQLMSN
ALPSGPGPEL RDSSQQAAHM NHLSHPWGLN LTEKIKKIKV VFTPTICKQT CARGRCANTC
EKGDTTTLYS QGGHGHDPKS GFRIYFCQIP CLNGGRCIGR DECWCPANST GKFCHLPVPQ
PDREPPGRGS QHRALLEGPL KQSTFTLPLS NQLASVNPSL VKVQMQHPPE ASVQIHQVAR
VRGEVDPVPE DNSVETRASH RPHGSSGHSH WASNSIPARA GEAPRPPPVP SRHYGLLGQC
YLSTVNGQCA NPLGELTSQE DCCGSVGTSW GVTSCAPCPP RPAFPVIENG QLECPQGYKR
LNLSHCQDIN ECLTLGLCKD SECVNTRGSY LCTCRPGLML DPSRSRCVSD KAVSMKQGLC
YRSMVSGTCT LPLVQRITKQ ICCCSRVGKA WGSKCEHCPL PGTEAFREIC PAGHGYAYSS
SDIRLSMRKA EEEELASPVR EQRQQSSGPP PGAAERQPLR AATATWIEAE TLPDKGDSRA
IQITTSAPHL PARVPGDATG RPTPSLPGQG IPEGPAEEQV IPSSDVLVTH GPPGFDPCFA
GASNICGPGT CVKLPNGYRC VCSPGYQLHP SQDYCTDDNE CLRNPCEGRG RCVNSVGSYS
CLCYPGYTLA TLGDTQECQD VDECEQPGVC SGGRCSNTEG SYHCECDQGY VMVRRGHCQD
INECRHPGTC PDGRCVNSPG SYTCLACEEG YIGQSGNCVD MNECLTPGIC AHGRCINMEG
SFRCSCEPGY ELTPDKKGCR DVDECASRAS CPTGLCLNTE GSFTCSACQS GYWVNEDGTA
CEDLDECAFP GVCPTGVCTN TVGSFSCKDC DRGFRPSPLG NSCEDVDECE GPQNSCLGGE
CKNTDGSYQC LCPQGFQLAN GTVCEDVDEC VGEEHCAPHG ECLNSPGSFF CLCAPGFASA
EGGTRCQDVD ECATTEPCLG GHCVNTEGSF NCLCETGFQP APDSGECVDI DECANDTVCG
NHGFCDNTDG SFRCLCDQGF ETSPSGWECV DVNECELMLA VCGDALCENV EGSFLCLCAS
DLEEYDAEEG HCRPRVAGAQ RIPEVPTEEQ AAGLTGMECY AEHNGGPPCS QILGQNSTQA
ECCSTQGARW GETCDPCPSE DSVEFSELCP SGQGYIPVEG AWTFGQAMYT DADECILFGP
ALCQNGRCLN TVPGYICLCN PGYHYDAVSR KCQDHNECQD LACENGECVN TEGSFHCFCS
PPLILDLSGQ RCVNSTSSSE DFPDHDIHMD ICWKKVTNDV CSQPLRGHHT TYTECCCQDG
EAWSQQCALC PPRSSEVYAQ LCNVARIEAE REAGIHFRPG YEYGPGPDDL PETLYGPDGA
PFYNYLGPED TVPEPPFSNT ASHLGDNTPI LEPPLQPSEL QPPAIQNPLA SFEGLQAEEC
GILNGCENGR CVRVREGYTC DCFEGFQLDT ALMACVDVNE CEDLNGAARL CAHGHCENTE
GSYRCHCSPG YVAEPGPPHC AAKE
//
